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. 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; 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 //