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SPA2_YEAST
ID   SPA2_YEAST              Reviewed;        1466 AA.
AC   P23201; D6VXY3;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Protein SPA2;
GN   Name=SPA2; Synonyms=PEA1; OrderedLocusNames=YLL021W; ORFNames=L1209;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=2211820; DOI=10.1083/jcb.111.4.1451;
RA   Gehrung S., Snyder M.;
RT   "The SPA2 gene of Saccharomyces cerevisiae is important for pheromone-
RT   induced morphogenesis and efficient mating.";
RL   J. Cell Biol. 111:1451-1464(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9046100;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<183::aid-yea65>3.0.co;2-v;
RA   Purnelle B., Goffeau A.;
RT   "The sequence of 32kb on the left arm of yeast chromosome XII reveals six
RT   known genes, a new member of the seripauperins family and a new ABC
RT   transporter homologous to the human multidrug resistance protein.";
RL   Yeast 13:183-188(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   INTERACTION WITH SHS1.
RX   PubMed=9790978; DOI=10.1006/bbrc.1998.9541;
RA   Mino A., Tanaka K., Kamei T., Umikawa M., Fujiwara T., Takai Y.;
RT   "Shs1p: a novel member of septin that interacts with spa2p, involved in
RT   polarized growth in Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 251:732-736(1998).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; SER-254;
RP   SER-585; SER-599; SER-646; SER-883; SER-937; SER-961; SER-979; THR-1179;
RP   SER-1180 AND SER-1263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-820; SER-937;
RP   SER-961; SER-1053 AND SER-1056, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-254; SER-274;
RP   SER-301; SER-585; SER-599; SER-865; SER-883; SER-910; SER-979; THR-1179 AND
RP   SER-1180, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; THR-220;
RP   SER-254; SER-274; SER-585; SER-599; SER-817; SER-820; SER-883; SER-961;
RP   SER-979; SER-1173; THR-1179; SER-1180; THR-1251 AND SER-1263, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in pheromone-induced morphogenesis and efficient
CC       mating, perhaps as a cytoskeletal protein.
CC   -!- SUBUNIT: Interacts with SHS1. {ECO:0000269|PubMed:9790978}.
CC   -!- SUBCELLULAR LOCATION: Cell tip. Note=Localizes to a sharp patch at the
CC       shmoo tip (mating projection) which corresponds to the site of
CC       polarized cell growth.
CC   -!- MISCELLANEOUS: Present with 274 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X53731; CAA37763.1; -; Genomic_DNA.
DR   EMBL; X97560; CAA66170.1; -; Genomic_DNA.
DR   EMBL; Z73126; CAA97469.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09299.1; -; Genomic_DNA.
DR   PIR; A36426; A36426.
DR   RefSeq; NP_013079.1; NM_001181841.1.
DR   AlphaFoldDB; P23201; -.
DR   SMR; P23201; -.
DR   BioGRID; 31232; 195.
DR   ComplexPortal; CPX-3188; Polarisome.
DR   DIP; DIP-99N; -.
DR   IntAct; P23201; 14.
DR   MINT; P23201; -.
DR   STRING; 4932.YLL021W; -.
DR   iPTMnet; P23201; -.
DR   MaxQB; P23201; -.
DR   PaxDb; P23201; -.
DR   PRIDE; P23201; -.
DR   EnsemblFungi; YLL021W_mRNA; YLL021W; YLL021W.
DR   GeneID; 850639; -.
DR   KEGG; sce:YLL021W; -.
DR   SGD; S000003944; SPA2.
DR   VEuPathDB; FungiDB:YLL021W; -.
DR   eggNOG; ENOG502QS1N; Eukaryota.
DR   GeneTree; ENSGT00940000176499; -.
DR   HOGENOM; CLU_002012_0_0_1; -.
DR   InParanoid; P23201; -.
DR   OMA; MKRNQAR; -.
DR   BioCyc; YEAST:G3O-32125-MON; -.
DR   PRO; PR:P23201; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P23201; protein.
DR   GO; GO:0005826; C:actomyosin contractile ring; IBA:GO_Central.
DR   GO; GO:0005938; C:cell cortex; IDA:SGD.
DR   GO; GO:1902716; C:cell cortex of growing cell tip; IBA:GO_Central.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR   GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR   GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR   GO; GO:0000133; C:polarisome; IDA:SGD.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:SGD.
DR   GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR   GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR   GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IC:ComplexPortal.
DR   GO; GO:0036267; P:invasive filamentous growth; IGI:SGD.
DR   GO; GO:0031382; P:mating projection formation; IGI:SGD.
DR   GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
DR   GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0031384; P:regulation of initiation of mating projection growth; IMP:SGD.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR   GO; GO:0031385; P:regulation of termination of mating projection growth; IMP:SGD.
DR   GO; GO:0006903; P:vesicle targeting; IC:ComplexPortal.
DR   InterPro; IPR022018; GIT1_C.
DR   InterPro; IPR013724; GIT_SHD.
DR   InterPro; IPR039892; Spa2/Sph1.
DR   PANTHER; PTHR21601; PTHR21601; 1.
DR   Pfam; PF12205; GIT1_C; 1.
DR   Pfam; PF08518; GIT_SHD; 2.
DR   SMART; SM00555; GIT; 4.
PE   1: Evidence at protein level;
KW   Cell shape; Coiled coil; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1466
FT                   /note="Protein SPA2"
FT                   /id="PRO_0000072090"
FT   REPEAT          818..825
FT                   /note="1"
FT   REPEAT          826..834
FT                   /note="2"
FT   REPEAT          835..843
FT                   /note="3"
FT   REPEAT          860..868
FT                   /note="4"
FT   REPEAT          875..883
FT                   /note="5"
FT   REPEAT          884..892
FT                   /note="6"
FT   REPEAT          893..901
FT                   /note="7"
FT   REPEAT          902..910
FT                   /note="8"
FT   REPEAT          911..919
FT                   /note="9"
FT   REPEAT          920..928
FT                   /note="10"
FT   REPEAT          929..937
FT                   /note="11"
FT   REPEAT          938..946
FT                   /note="12"
FT   REPEAT          947..953
FT                   /note="13"
FT   REPEAT          954..961
FT                   /note="14"
FT   REPEAT          962..970
FT                   /note="15"
FT   REPEAT          971..979
FT                   /note="16"
FT   REPEAT          980..988
FT                   /note="17"
FT   REPEAT          989..997
FT                   /note="18"
FT   REPEAT          998..1006
FT                   /note="19"
FT   REPEAT          1007..1015
FT                   /note="20"
FT   REPEAT          1036..1044
FT                   /note="21"
FT   REPEAT          1045..1053
FT                   /note="22"
FT   REPEAT          1054..1062
FT                   /note="23"
FT   REPEAT          1072..1080
FT                   /note="24"
FT   REPEAT          1081..1087
FT                   /note="25"
FT   REGION          123..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..1087
FT                   /note="25 X 9 AA approximate tandem repeats"
FT   REGION          954..1086
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1098..1130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1276..1312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          286..388
FT                   /evidence="ECO:0000255"
FT   COILED          1169..1189
FT                   /evidence="ECO:0000255"
FT   COILED          1275..1302
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        148..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..748
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..780
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..985
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1015
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1083
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1107..1122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1171..1190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1208..1246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1284..1310
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         220
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         585
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         599
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         817
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         865
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         883
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         910
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         937
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950"
FT   MOD_RES         961
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT   MOD_RES         979
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         1053
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         1056
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         1080
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377"
FT   MOD_RES         1173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1179
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         1180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         1251
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         1263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   1466 AA;  163143 MW;  2EBB616152382C89 CRC64;
     MGTSSEVSLA HHRDIFHYYV SLKTFFEVTG ENRDRSNSTR AQKARAKLLK LSSSQFYELS
     TDVSDELQRR IGEDANQPDY LLPKANFHMK RNQARQKLAN LSQTRFNDLL DDILFEIKRR
     GFDKDLDAPR PPLPQPMKQE VSKDSDDTAR TSTNSSSVTQ VAPNVSVQPS LVIPKMASID
     WSSEEEEEEQ VKEKPNEPEG KQTSMDEKKE AKPALNPIVT DSDLPDSQVL ARDITSMART
     PTTTHKNYWD VNDSPIIKVD KDIDNEKGPE QLKSPEVQRA ENNNPNSEME DKVKELTDLN
     SDLHLQIEDL NAKLASLTSE KEKEKKEEKE EKEKEKNLKI NYTIDESFQK ELLSLNSQIG
     ELSIENENLK QKISEFELHQ KKNDNHNDLK ITDGFISKYS SADGLIPAQY ILNANNLIIQ
     FTTRLSAVPI GDSTAISHQI GEELFQILSQ LSNLISQLLL SADLLQYKDQ VILLKASLSH
     AITSIRYFSV YGPVLIPKIT VQAAVSEVCF AMCNLIDSAK IKSDSNGEST TSNEGNRQVL
     EYSSPTATTP MTPTFPSTSG INMKKGFINP RKPASFLNDV EEEESPVKPL KITQKAINSP
     IIRPSSSNGV PTTSRKPSGT GLFSLMIDSS IAKNSSHKED NDKYVSPIKA VTSASNSASS
     NISEIPKLTL PPQAKIGTVI PPSENQVPNI KIENTEEDNK RSDITNEISV KPTSSIADKL
     KQFEQSSEKK SSPKENPIAK EEMDSKPKLS NKFITSMNDV STDDSSSDGN ENDDADDDDD
     FTYMALKQTM KREGSKIEKN NDSKLPANIV ELDLHESPES VKIESPESIK EITSSEMSSE
     MPSSSLPKRL VEDVEPSEMP EKGASVESVR KKNFQEPLGN VESPDMTQKV KSLGMTGKAV
     GPESDSRVES PGMTGQIKSL NMAGKVVGPE ADSRVESPGM KEQIKSLGMT GKITAQESIK
     SPEAARKLAS SGEVDKIESP RMVRESESLE AVGNTIPSNM TVKMESPNLK GNTVSEPQEI
     RRDIASSEPI ENVDPPKVLK KIVFPKAVNR TGSPKSVEKT PSSATLKKSG LPEPNSQIVS
     PELAKNSPLA PIKKNVELRE TNKPHTETIT SVEPTNKDAN TSWRDADLNR TIKREEEDED
     FDRVNHNIQI TGAYTKTGKI DYHKIPVDRK AKSEAEVHTS EEDIDESNNV NGKRADAQIH
     ITERKHAFVN PTENSQVKKT SHSPFLNSKP VQYENSESNG GINNHIKIKN TGETTAHDEK
     HYSDDDDSSY QFVPMKHEEQ EQEQNRSEEE ESEDDDEEEE DSDFDVDTFD IENPDNTLSE
     LLLYLEHQTM DVISTIQSLL TSIKKPQVTK GNLRGESNAI NQVIGQMVDA TSISMEQSRN
     ANLKKHGDWV VQSLRDCSRR MTILCQLTGD GILAKEKSDQ DYADKNFKQR LAGIAFDVAK
     CTKELVKTVE EASLKDEINY LNSKLK
 
 
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