ID   100K_RAT       STANDARD;      PRT;   889 AA.
AC   Q62671;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   100 KD PROTEIN (EC 6.3.2.-).
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC   Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=WISTAR; TISSUE=TESTIS;
RX   MEDLINE; 92253337.
RA   MUELLER D., REHBEIN M., BAUMEISTER H., RICHTER D.;
RT   "Molecular characterization of a novel rat protein structurally
RT   related to poly(A) binding proteins and the 70K protein of the U1
RT   small nuclear ribonucleoprotein particle (snRNP).";
RL   Nucleic Acids Res. 20:1471-1475(1992).
RN   [2]
RP   ERRATUM.
RA   MUELLER D., REHBEIN M., BAUMEISTER H., RICHTER D.;
RL   Nucleic Acids Res. 20:2624-2624(1992).
CC   -!- FUNCTION: E3 UBIQUITIN-PROTEIN LIGASE WHICH ACCEPTS UBIQUITIN FROM
CC       AN E2 UBIQUITIN-CONJUGATING ENZYME IN THE FORM OF A THIOESTER AND
CC       THEN DIRECTLY TRANSFERS THE UBIQUITIN TO TARGETED SUBSTRATES (BY
CC       SIMILARITY). THIS PROTEIN MAY BE INVOLVED IN MATURATION AND/OR
CC       POST-TRANSCRIPTIONAL REGULATION OF MRNA.
CC   -!- TISSUE SPECIFICITY: HIGHEST LEVELS FOUND IN TESTIS. ALSO PRESENT
CC       IN LIVER, KIDNEY, LUNG AND BRAIN.
CC   -!- DEVELOPMENTAL STAGE: IN EARLY POST-NATAL LIFE, EXPRESSION IN
CC       THE TESTIS INCREASES TO REACH A MAXIMUM AROUND DAY 28.
CC   -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR
CC       UBIQUITIN-THIOLESTER FORMATION.
CC   -!- SIMILARITY: CONTAINS AN HECT-TYPE E3 UBIQUITIN-PROTEIN LIGASE
CC       DOMAIN.
CC   -!- SIMILARITY: A CENTRAL REGION (AA 485-514) IS SIMILAR TO THE
CC       C-TERMINAL DOMAINS OF MAMMALIAN AND YEAST POLY (A) RNA BINDING
CC       PROTEINS (PABP).
CC   -!- SIMILARITY: THE C-TERMINAL HALF SHOWS HIGH SIMILARITY TO
CC       DROSOPHILA HYPERPLASMIC DISC PROTEIN AND SOME, TO HUMAN E6-AP.
CC   -!- SIMILARITY: CONTAINS MIXED-CHARGE DOMAINS SIMILAR TO RNA-BINDING
CC       PROTEINS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X64411; CAA45756.1; -.
DR   PFAM; PF00632; HECT; 1.
DR   PFAM; PF00658; PABP; 1.
KW   Ubiquitin conjugation; Ligase.
FT   DOMAIN       77     88       ASP/GLU-RICH (ACIDIC).
FT   DOMAIN      127    150       PRO-RICH.
FT   DOMAIN      420    439       ARG/GLU-RICH (MIXED CHARGE).
FT   DOMAIN      448    457       ARG/ASP-RICH (MIXED CHARGE).
FT   DOMAIN      485    514       PABP-LIKE.
FT   DOMAIN      579    590       ASP/GLU-RICH (ACIDIC).
FT   DOMAIN      786    889       HECT DOMAIN.
FT   DOMAIN      827    847       PRO-RICH.
FT   BINDING     858    858       UBIQUITIN (BY SIMILARITY).
SQ   SEQUENCE   889 AA;  100368 MW;  DD7E6C7A CRC32;
     MMSARGDFLN YALSLMRSHN DEHSDVLPVL DVCSLKHVAY VFQALIYWIK AMNQQTTLDT
     PQLERKRTRE LLELGIDNED SEHENDDDTS QSATLNDKDD ESLPAETGQN HPFFRRSDSM
     TFLGCIPPNP FEVPLAEAIP LADQPHLLQP NARKEDLFGR PSQGLYSSSA GSGKCLVEVT
     MDRNCLEVLP TKMSYAANLK NVMNMQNRQK KAGEDQSMLA EEADSSKPGP SAHDVAAQLK
     SSLLAEIGLT ESEGPPLTSF RPQCSFMGMV ISHDMLLGRW RLSLELFGRV FMEDVGAEPG
     SILTELGGFE VKESKFRREM EKLRNQQSRD LSLEVDRDRD LLIQQTMRQL NNHFGRRCAT
     TPMAVHRVKV TFKDEPGEGS GVARSFYTAI AQAFLSNEKL PNLDCIQNAN KGTHTSLMQR
     LRNRGERDRE REREREMRRS SGLRAGSRRD RDRDFRRQLS IDTRPFRPAS EGNPSDDPDP
     LPAHRQALGE RLYPRVQAMQ PAFASKITGM LLELSPAQLL LLLASEDSLR ARVEEAMELI
     VAHGRENGAD SILDLGLLDS SEKVQENRKR HGSSRSVVDM DLDDTDDGDD NAPLFYQPGK
     RGFYTPRPGK NTEARLNCFR NIGRILGLCL LQNELCPITL NRHVIKVLLG RKVNWHDFAF
     FDPVMYESLR QLILASQSSD ADAVFSAMDL AFAVDLCKEE GGGQVELIPN GVNIPVTPQN
     VYEYVRKYAE HRMLVVAEQP LHAMRKGLLD VLPKNSLEDL TAEDFRLLVN GCGEVNVQML
     ISFTSFNDES GENAEKLLQF KRWFWSIVER MSMTERQDLV YFWTSSPSLP ASEEGFQPMP
     SITIRPPDDQ HLPTANTCIS RLYVPLYSSK QILKQKLLLA IKTKNFGFV
//
ID   104K_THEPA     STANDARD;      PRT;   924 AA.
AC   P15711;
DT   01-APR-1990 (Rel. 14, Created)
DT   01-APR-1990 (Rel. 14, Last sequence update)
DT   01-AUG-1992 (Rel. 23, Last annotation update)
DE   104 KD MICRONEME-RHOPTRY ANTIGEN.
OS   Theileria parva.
OC   Eukaryota; Alveolata; Apicomplexa; Piroplasmida; Theileriidae;
OC   Theileria.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=MUGUGA;
RX   MEDLINE; 90158697.
RA   IAMS K.P., YOUNG J.R., NENE V., DESAI J., WEBSTER P.,
RA   OLE-MOIYOI O.K., MUSOKE A.J.;
RT   "Characterisation of the gene encoding a 104-kilodalton microneme-
RT   rhoptry protein of Theileria parva.";
RL   Mol. Biochem. Parasitol. 39:47-60(1990).
CC   -!- SUBCELLULAR LOCATION: IN MICRONEME/RHOPTRY COMPLEXES.
CC   -!- DEVELOPMENTAL STAGE: SPOROZOITE ANTIGEN.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M29954; AAA18217.1; -.
DR   PIR; A44945; A44945.
KW   Antigen; Sporozoite; Repeat.
FT   DOMAIN        1     19       HYDROPHOBIC.
FT   DOMAIN      905    924       HYDROPHOBIC.
SQ   SEQUENCE   924 AA;  103625 MW;  4563AAA0 CRC32;
     MKFLILLFNI LCLFPVLAAD NHGVGPQGAS GVDPITFDIN SNQTGPAFLT AVEMAGVKYL
     QVQHGSNVNI HRLVEGNVVI WENASTPLYT GAIVTNNDGP YMAYVEVLGD PNLQFFIKSG
     DAWVTLSEHE YLAKLQEIRQ AVHIESVFSL NMAFQLENNK YEVETHAKNG ANMVTFIPRN
     GHICKMVYHK NVRIYKATGN DTVTSVVGFF RGLRLLLINV FSIDDNGMMS NRYFQHVDDK
     YVPISQKNYE TGIVKLKDYK HAYHPVDLDI KDIDYTMFHL ADATYHEPCF KIIPNTGFCI
     TKLFDGDQVL YESFNPLIHC INEVHIYDRN NGSIICLHLN YSPPSYKAYL VLKDTGWEAT
     THPLLEEKIE ELQDQRACEL DVNFISDKDL YVAALTNADL NYTMVTPRPH RDVIRVSDGS
     EVLWYYEGLD NFLVCAWIYV SDGVASLVHL RIKDRIPANN DIYVLKGDLY WTRITKIQFT
     QEIKRLVKKS KKKLAPITEE DSDKHDEPPE GPGASGLPPK APGDKEGSEG HKGPSKGSDS
     SKEGKKPGSG KKPGPAREHK PSKIPTLSKK PSGPKDPKHP RDPKEPRKSK SPRTASPTRR
     PSPKLPQLSK LPKSTSPRSP PPPTRPSSPE RPEGTKIIKT SKPPSPKPPF DPSFKEKFYD
     DYSKAASRSK ETKTTVVLDE SFESILKETL PETPGTPFTT PRPVPPKRPR TPESPFEPPK
     DPDSPSTSPS EFFTPPESKR TRFHETPADT PLPDVTAELF KEPDVTAETK SPDEAMKRPR
     SPSEYEDTSP GDYPSLPMKR HRLERLRLTT TEMETDPGRM AKDASGKPVK LKRSKSFDDL
     TTVELAPEPK ASRIVVDDEG TEADDEETHP PEERQKTEVR RRRPPKKPSK SPRPSKPKKP
     KKPDSAYIPS ILAILVVSLI VGIL
//
ID   108_LYCES      STANDARD;      PRT;   102 AA.
AC   Q43495;
DT   15-JUL-1999 (Rel. 38, Created)
DT   15-JUL-1999 (Rel. 38, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   PROTEIN 108 PRECURSOR.
OS   Lycopersicon esculentum (Tomato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons;
OC   core eudicots; Asteridae; euasterids I; Solanales; Solanaceae;
OC   Solanum.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. VF36; TISSUE=ANTHER;
RX   MEDLINE; 94143497.
RA   CHEN R., SMITH A.G.;
RT   "Nucleotide sequence of a stamen- and tapetum-specific gene from
RT   Lycopersicon esculentum.";
RL   Plant Physiol. 101:1413-1413(1993).
CC   -!- TISSUE SPECIFICITY: STAMEN- AND TAPETUM-SPECIFIC.
CC   -!- SIMILARITY: BELONGS TO THE A9 / FIL1 FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; Z14088; CAA78466.1; -.
DR   MENDEL; 8853; LYCes;1133;1.
KW   Signal.
FT   SIGNAL        1     30       POTENTIAL.
FT   CHAIN        31    102       PROTEIN 108.
FT   DISULFID     41     77       BY SIMILARITY.
FT   DISULFID     51     66       BY SIMILARITY.
FT   DISULFID     67     92       BY SIMILARITY.
FT   DISULFID     79     99       BY SIMILARITY.
SQ   SEQUENCE   102 AA;  10576 MW;  AFA4875A CRC32;
     MASVKSSSSS SSSSFISLLL LILLVIVLQS QVIECQPQQS CTASLTGLNV CAPFLVPGSP
     TASTECCNAV QSINHDCMCN TMRIAAQIPA QCNLPPLSCS AN
//
ID   10KD_VIGUN     STANDARD;      PRT;    75 AA.
AC   P18646;
DT   01-NOV-1990 (Rel. 16, Created)
DT   01-NOV-1990 (Rel. 16, Last sequence update)
DT   01-FEB-1995 (Rel. 31, Last annotation update)
DE   10 KD PROTEIN PRECURSOR (CLONE PSAS10).
OS   Vigna unguiculata (Cowpea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons;
OC   core eudicots; Rosidae; eurosids I; Fabales; Fabaceae; Papilionoideae;
OC   Vigna.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=COTYLEDON;
RX   MEDLINE; 91355865.
RA   ISHIBASHI N., YAMAUCHI D., MINIAMIKAWA T.;
RT   "Stored mRNA in cotyledons of Vigna unguiculata seeds: nucleotide
RT   sequence of cloned cDNA for a stored mRNA and induction of its
RT   synthesis by precocious germination.";
RL   Plant Mol. Biol. 15:59-64(1990).
CC   -!- FUNCTION: THIS PROTEIN IS REQUIRED FOR GERMINATION.
CC   -!- SIMILARITY: BELONGS TO THE GAMMA-PUROTHIONIN FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; X16877; CAA34760.1; -.
DR   PIR; S11156; S11156.
DR   HSSP; P45639; 1CHL.
DR   PFAM; PF00304; Gamma-thionin; 1.
DR   PROSITE; PS00940; GAMMA_THIONIN; 1.
KW   Germination; Signal.
FT   SIGNAL        1      ?       POTENTIAL.
FT   CHAIN         ?     75       10 KD PROTEIN.
FT   DISULFID     31     75       BY SIMILARITY.
FT   DISULFID     42     63       BY SIMILARITY.
FT   DISULFID     48     69       BY SIMILARITY.
FT   DISULFID     52     71       BY SIMILARITY.
SQ   SEQUENCE   75 AA;  8523 MW;  AFF911AB CRC32;
     MEKKSIAGLC FLFLVLFVAQ EVVVQSEAKT CENLVDTYRG PCFTTGSCDD HCKNKEHLLS
     GRCRDDVRCW CTRNC
//
ID   110K_PLAKN     STANDARD;      PRT;   296 AA.
AC   P13813;
DT   01-JAN-1990 (Rel. 13, Created)
DT   01-JAN-1990 (Rel. 13, Last sequence update)
DT   01-FEB-1994 (Rel. 28, Last annotation update)
DE   110 KD ANTIGEN (PK110) (FRAGMENT).
OS   Plasmodium knowlesi.
OC   Eukaryota; Alveolata; Apicomplexa; Haemosporida; Plasmodium.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 88039002.
RA   PERLER F.B., MOON A.M., QIANG B.Q., MEDA M., DALTON M., CARD C.,
RA   SCHMIDT-ULLRICH R., WALLACH D., LYNCH J., DONELSON J.E.;
RT   "Cloning and characterization of an abundant Plasmodium knowlesi
RT   antigen which cross reacts with Gambian sera.";
RL   Mol. Biochem. Parasitol. 25:185-193(1987).
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M19152; AAA29471.1; -.
DR   PIR; A54527; A54527.
KW   Malaria; Antigen; Repeat.
FT   NON_TER       1      1
FT   DOMAIN      131    296       13.5 X 12 AA TANDEM REPEATS OF E-E-T-Q-K-
FT                                T-V-E-P-E-Q-T.
SQ   SEQUENCE   296 AA;  34077 MW;  666F88DF CRC32;
     FNSNMLRGSV CEEDVSLMTS IDNMIEEIDF YEKEIYKGSH SGGVIKGMDY DLEDDENDED
     EMTEQMVEEV ADHITQDMID EVAHHVLDNI THDMAHMEEI VHGLSGDVTQ IKEIVQKVNV
     AVEKVKHIVE TEETQKTVEP EQIEETQNTV EPEQTEETQK TVEPEQTEET QNTVEPEQIE
     ETQKTVEPEQ TEEAQKTVEP EQTEETQKTV EPEQTEETQK TVEPEQTEET QKTVEPEQTE
     ETQKTVEPEQ TEETQKTVEP EQTEETQKTV EPEQTEETQN TVEPEPTQET QNTVEP
//
ID   11S3_HELAN     STANDARD;      PRT;   493 AA.
AC   P19084;
DT   01-NOV-1990 (Rel. 16, Created)
DT   01-NOV-1990 (Rel. 16, Last sequence update)
DT   01-FEB-1994 (Rel. 28, Last annotation update)
DE   11S GLOBULIN SEED STORAGE PROTEIN G3 PRECURSOR (HELIANTHININ G3).
GN   HAG3.
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons;
OC   core eudicots; Asteridae; euasterids II; Asterales; Asteraceae;
OC   Helianthus.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89232734.
RA   VONDER HARR R.A., ALLEN R.D., COHEN E.A., NESSLER C.L., THOMAS T.L.;
RT   "Organization of the sunflower 11S storage protein gene family.";
RL   Gene 74:433-443(1988).
CC   -!- FUNCTION: THIS IS A SEED STORAGE PROTEIN.
CC   -!- SUBUNIT: HEXAMER; EACH SUBUNIT IS COMPOSED OF AN ACIDIC AND A
CC       BASIC CHAIN DERIVED FROM A SINGLE PRECURSOR AND LINKED BY A
CC       DISULFIDE BOND.
CC   -!- SIMILARITY: BELONGS TO THE 11S SEED STORAGE PROTEINS (GLOBULINS)
CC       FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M28832; AAA33374.1; -.
DR   PIR; JA0089; JA0089.
DR   PFAM; PF00190; Seedstore_11s; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
KW   Seed storage protein; Multigene family; Signal.
FT   SIGNAL        1     20
FT   CHAIN        21    305       ACIDIC CHAIN.
FT   CHAIN       306    493       BASIC CHAIN.
FT   DISULFID    103    312       INTERCHAIN (ACIDIC-BASIC) (POTENTIAL).
FT   DOMAIN       23     35       GLN-RICH.
FT   DOMAIN      111    127       GLN/GLY-RICH.
FT   DOMAIN      191    297       GLN-RICH.
SQ   SEQUENCE   493 AA;  55687 MW;  E79DEAAE CRC32;
     MASKATLLLA FTLLFATCIA RHQQRQQQQN QCQLQNIEAL EPIEVIQAEA GVTEIWDAYD
     QQFQCAWSIL FDTGFNLVAF SCLPTSTPLF WPSSREGVIL PGCRRTYEYS QEQQFSGEGG
     RRGGGEGTFR TVIRKLENLK EGDVVAIPTG TAHWLHNDGN TELVVVFLDT QNHENQLDEN
     QRRFFLAGNP QAQAQSQQQQ QRQPRQQSPQ RQRQRQRQGQ GQNAGNIFNG FTPELIAQSF
     NVDQETAQKL QGQNDQRGHI VNVGQDLQIV RPPQDRRSPR QQQEQATSPR QQQEQQQGRR
     GGWSNGVEET ICSMKFKVNI DNPSQADFVN PQAGSIANLN SFKFPILEHL RLSVERGELR
     PNAIQSPHWT INAHNLLYVT EGALRVQIVD NQGNSVFDNE LREGQVVVIP QNFAVIKRAN
     EQGSRWVSFK TNDNAMIANL AGRVSASAAS PLTLWANRYQ LSREEAQQLK FSQRETVLFA
     PSFSRGQGIR ASR
//
ID   11SB_CUCMA     STANDARD;      PRT;   480 AA.
AC   P13744;
DT   01-JAN-1990 (Rel. 13, Created)
DT   01-JAN-1990 (Rel. 13, Last sequence update)
DT   01-NOV-1990 (Rel. 16, Last annotation update)
DE   11S GLOBULIN BETA SUBUNIT PRECURSOR.
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   euphyllophytes; Spermatophyta; Magnoliophyta; eudicotyledons;
OC   core eudicots; Rosidae; eurosids I; Cucurbitales; Cucurbitaceae;
OC   Cucurbita.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CV. KUROKAWA AMAKURI NANKIN;
RX   MEDLINE; 88166744.
RA   HAYASHI M., MORI H., NISHIMURA M., AKAZAWA T., HARA-NISHIMURA I.;
RT   "Nucleotide sequence of cloned cDNA coding for pumpkin 11-S globulin
RT   beta subunit.";
RL   Eur. J. Biochem. 172:627-632(1988).
RN   [2]
RP   SEQUENCE OF 22-30 AND 297-302.
RA   OHMIYA M., HARA I., MASTUBARA H.;
RT   "Pumpkin (Cucurbita sp.) seed globulin IV. Terminal sequences of the
RT   acidic and basic peptide chains and identification of a pyroglutamyl
RT   peptide chain.";
RL   Plant Cell Physiol. 21:157-167(1980).
CC   -!- FUNCTION: THIS IS A SEED STORAGE PROTEIN.
CC   -!- SUBUNIT: HEXAMER; EACH SUBUNIT IS COMPOSED OF AN ACIDIC AND A
CC       BASIC CHAIN DERIVED FROM A SINGLE PRECURSOR AND LINKED BY A
CC       DISULFIDE BOND.
CC   -!- SIMILARITY: BELONGS TO THE 11S SEED STORAGE PROTEINS (GLOBULINS)
CC       FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; M36407; AAA33110.1; -.
DR   PIR; S00366; FWPU1B.
DR   PFAM; PF00190; Seedstore_11s; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
KW   Seed storage protein; Signal.
FT   SIGNAL        1     21
FT   CHAIN        22    480       11S GLOBULIN BETA SUBUNIT.
FT   CHAIN        22    296       GAMMA CHAIN (ACIDIC).
FT   CHAIN       297    480       DELTA CHAIN (BASIC).
FT   MOD_RES      22     22       PYRROLIDONE CARBOXYLIC ACID.
FT   DISULFID    124    303       INTERCHAIN (GAMMA-DELTA) (POTENTIAL).
FT   CONFLICT     27     27       S -> E (IN REF. 2).
FT   CONFLICT     30     30       E -> S (IN REF. 2).
SQ   SEQUENCE   480 AA;  54625 MW;  D515DD6E CRC32;
     MARSSLFTFL CLAVFINGCL SQIEQQSPWE FQGSEVWQQH RYQSPRACRL ENLRAQDPVR
     RAEAEAIFTE VWDQDNDEFQ CAGVNMIRHT IRPKGLLLPG FSNAPKLIFV AQGFGIRGIA
     IPGCAETYQT DLRRSQSAGS AFKDQHQKIR PFREGDLLVV PAGVSHWMYN RGQSDLVLIV
     FADTRNVANQ IDPYLRKFYL AGRPEQVERG VEEWERSSRK GSSGEKSGNI FSGFADEFLE
     EAFQIDGGLV RKLKGEDDER DRIVQVDEDF EVLLPEKDEE ERSRGRYIES ESESENGLEE
     TICTLRLKQN IGRSVRADVF NPRGGRISTA NYHTLPILRQ VRLSAERGVL YSNAMVAPHY
     TVNSHSVMYA TRGNARVQVV DNFGQSVFDG EVREGQVLMI PQNFVVIKRA SDRGFEWIAF
     KTNDNAITNL LAGRVSQMRM LPLGVLSNMY RISREEAQRL KYGQQEMRVL SPGRSQGRRE
//
ID   120K_RICRI     STANDARD;      PRT;  1300 AA.
AC   P14914;
DT   01-APR-1990 (Rel. 14, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   01-FEB-1996 (Rel. 33, Last annotation update)
DE   120 KD SURFACE-EXPOSED PROTEIN.
GN   P120.
OS   Rickettsia rickettsii.
OC   Bacteria; Proteobacteria; alpha subdivision; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=R;
RX   MEDLINE; 90136087.
RA   GILMORE R.D. JR., JOSTE N., MCDONALD G.A.;
RT   "Cloning, expression and sequence analysis of the gene encoding the
RT   120 kD surface-exposed protein of Rickettsia rickettsii.";
RL   Mol. Microbiol. 3:1579-1586(1989).
CC   -!- FUNCTION: MAJOR STRUCTURAL PROTEIN WHICH MAY PLAY A ROLE AS
CC       RICKETTSIAL VIRULENCE FACTOR AND/OR IMMUNOGEN DURING INFECTION.
CC   -!- SUBCELLULAR LOCATION: CELL WALL. THIS BACTERIA IS COVERED BY A
CC       S-LAYER WITH HEXAGONAL SYMMETRY.
CC   -!- PTM: GLYCOSYLATED (POSSIBLE).
CC   -!- DISEASE: RICKETTSIA RICKETTSII IS THE CAUSATIVE AGENT OF ROCKY
CC       MOUNTAIN SPOTTED FEVER (RMSF).
CC   -!- MISCELLANEOUS: ITS C-TERMINUS POTENTIALLY MAY BEAR THE EPITOPES
CC       CONFERRING ANTIGENICITY TO THE PROTEIN.
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DR   EMBL; X16353; CAA34402.1; -.
DR   PIR; S07575; S07575.
KW   Antigen; Glycoprotein; S-layer.
FT   CARBOHYD      7      7       POTENTIAL.
FT   CARBOHYD     66     66       POTENTIAL.
FT   CARBOHYD     86     86       POTENTIAL.
FT   CARBOHYD    103    103       POTENTIAL.
FT   CARBOHYD    147    147       POTENTIAL.
FT   CARBOHYD    268    268       POTENTIAL.
FT   CARBOHYD    330    330       POTENTIAL.
FT   CARBOHYD    375    375       POTENTIAL.
FT   CARBOHYD    415    415       POTENTIAL.
FT   CARBOHYD    424    424       POTENTIAL.
FT   CARBOHYD    430    430       POTENTIAL.
FT   CARBOHYD    436    436       POTENTIAL.
FT   CARBOHYD    444    444       POTENTIAL.
FT   CARBOHYD    515    515       POTENTIAL.
FT   CARBOHYD    547    547       POTENTIAL.
FT   CARBOHYD    593    593       POTENTIAL.
FT   CARBOHYD    655    655       POTENTIAL.
FT   CARBOHYD    698    698       POTENTIAL.
FT   CARBOHYD    710    710       POTENTIAL.
FT   CARBOHYD    799    799       POTENTIAL.
FT   CARBOHYD    800    800       POTENTIAL.
FT   CARBOHYD    826    826       POTENTIAL.
FT   CARBOHYD    844    844       POTENTIAL.
FT   CARBOHYD    861    861       POTENTIAL.
FT   CARBOHYD    879    879       POTENTIAL.
FT   CARBOHYD    920    920       POTENTIAL.
FT   CARBOHYD    926    926       POTENTIAL.
FT   CARBOHYD   1116   1116       POTENTIAL.
FT   CARBOHYD   1128   1128       POTENTIAL.
FT   CARBOHYD   1140   1140       POTENTIAL.
FT   CARBOHYD   1146   1146       POTENTIAL.
FT   CARBOHYD   1211   1211       POTENTIAL.
SQ   SEQUENCE   1300 AA;  132801 MW;  BC1DCD7C CRC32;
     MVIQSANATG QVNFRHIVDV GADGTTAFKT AASKVTITQD SNFGNTDFGN LAAQIKVPNA
     ITLTGNFTGD ASNPGNTAGV ITFDANGTLE SASADANVAV TNNITAIEAS GAGVVQLSGT
     HAAELRLGNA GSIFKLADGT VINGKVNQTA LVGGALAAGT ITLDGSATIT GDIGNAGGAA
     ALQRITLAND AKKTLTLGGA NIIGAGGGTI DLQANGGTIK LTSTQNNIVV DFDLAIATDQ
     TGVVDASSLT NAQTLTINGK IGTIGANNKT LGQFNIGSSK TVLSNGNVAI NELVIGNDGA
     VQFAHDTYLI TRTTNAAGQG KIIFNPVVNN GTTLAAGTNL GSATNPLAEI NFGSKGVNVD
     TVLNVGEGVN LYATNITTTD ANVGSFVFNA GGTNIVSGTV GGQQGNKFNT VALENGTTVK
     FLGNATFNGN TTIAANSTLQ IGGNYTADCV ASADGTGIVE FVNTGPITVT LNKQAAPVNA
     LKQITVSGPG NVVINEIGNA GNHHGAVTDT IAFENSSLGA VVFLPRGIPF NDAGNTMPLT
     IKSTVGNKTA KGFDVPSVVV LGVDSVIADG QVIGDQNNIV GLGLGSDNGI IVNATTLYAG
     ISTLNNNQGT VTLSGGVPNT PGTVYGLGTG IGASKFKQVT FTTDYNNLGN IIATNATIND
     GVTVTTGGIA GIGFDGKITL GSVNGNGNVR FADGILSNST SMIGTTKANN GTVTYLGNAF
     VGNIGDSDTP VASVRFTGSD SGAGLQGNIY SQVIDFGTYN LGIVNSNIIL GGGTTAINGK
     IDLVTNTLTF ASGTSTWGNN TSIETTLTLA NGNIGHIVIL EGAQVNTTTT GTTTIKVQDN
     ANANFSGTQT YTLIQGGARF NGTLGSPNFA VTGSNRFVNY SLIRAANQDY VITRTNNAEN
     VVTNDIANSP FGGAPGVDQN VTTFVNATNT AAYNNLLLAK NSANSANFVG AIVTDTSAAI
     TNVQLDLAKD IQAQLGNRLG ALRYLGTPET AEMAGPEAGA ISAAVAAGDE AIDNVAYGIW
     AKPFYTDAHQ SKKGGLAGYK AKTTGVVIGL DTLANDNLMI GAAIGITKTD IKHQDYKKGD
     KTDVNGFSFS LYGAQQLVKN FFAQGSAIFS LNQVKNKSQR YFFDANGNMS KQIAAGHYDN
     MTFGGNLTVG YDYNAMQGVL VTPMAGLSYL KSSDENYKET GTTVANKQVN SKFSDRTDLI
     VGAKVAGSTM NRTDLAVYPE VHAFVVHKVT GRLSKTQSVL DGQVTPCINQ PDRTTKTSYN
     LGLSASIRSD AKMEYGIGYD AQISSKYTAH QGTLKVRVNF
//
