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LSB5_YEAST
ID   LSB5_YEAST              Reviewed;         354 AA.
AC   P25369; D6VQY1; P87004; Q8NIM9;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 3.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=LAS seventeen-binding protein 5;
DE            Short=LAS17-binding protein 5;
GN   Name=LSB5; OrderedLocusNames=YCL034W; ORFNames=YCL186, YCL34W;
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].
RX   PubMed=1897318; DOI=10.1002/yea.320070513;
RA   Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.;
RT   "The complete sequence of a 11,953 bp fragment from C1G on chromosome III
RT   encompasses four new open reading frames.";
RL   Yeast 7:533-538(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [3]
RP   SEQUENCE REVISION.
RA   Gromadka R.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE REVISION.
RA   Valles G., Volckaerts G.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE, FUNCTION, INTERACTION WITH SLA1, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12388763; DOI=10.1091/mbc.e02-05-0262;
RA   Dewar H., Warren D.T., Gardiner F.C., Gourlay C.G., Satish N.,
RA   Richardson M.R., Andrews P.D., Ayscough K.R.;
RT   "Novel proteins linking the actin cytoskeleton to the endocytic machinery
RT   in Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 13:3646-3661(2002).
RN   [7]
RP   INTERACTION WITH LAS17.
RX   PubMed=10512884; DOI=10.1091/mbc.10.10.3521;
RA   Madania A., Dumoulin P., Grava S., Kitamoto H., Scharer-Brodbeck C.,
RA   Soulard A., Moreau V., Winsor B.;
RT   "The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome
RT   protein Las17p interacts with the Arp2/3 complex.";
RL   Mol. Biol. Cell 10:3521-3538(1999).
RN   [8]
RP   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   [9]
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: Essential for the organization of the actin cytoskeleton,
CC       fluid phase endocytosis and vesicle trafficking, together with YSC84.
CC       {ECO:0000269|PubMed:12388763}.
CC   -!- SUBUNIT: Interacts with SLA1 and LAS17. {ECO:0000269|PubMed:10512884,
CC       ECO:0000269|PubMed:12388763}.
CC   -!- INTERACTION:
CC       P25369; P40994: ARF3; NbExp=2; IntAct=EBI-10218, EBI-2824;
CC       P25369; Q12446: LAS17; NbExp=3; IntAct=EBI-10218, EBI-10022;
CC       P25369; P32790: SLA1; NbExp=5; IntAct=EBI-10218, EBI-17313;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000269|PubMed:12388763}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:12388763}. Note=Localizes independently of F-actin.
CC   -!- SIMILARITY: Belongs to the LSB5 family. {ECO:0000305}.
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DR   EMBL; X59720; CAC42957.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07450.1; -; Genomic_DNA.
DR   PIR; S74282; S74282.
DR   RefSeq; NP_009896.2; NM_001178679.1.
DR   AlphaFoldDB; P25369; -.
DR   SMR; P25369; -.
DR   BioGRID; 30949; 47.
DR   DIP; DIP-6258N; -.
DR   IntAct; P25369; 13.
DR   MINT; P25369; -.
DR   STRING; 4932.YCL034W; -.
DR   iPTMnet; P25369; -.
DR   MaxQB; P25369; -.
DR   PaxDb; P25369; -.
DR   PRIDE; P25369; -.
DR   EnsemblFungi; YCL034W_mRNA; YCL034W; YCL034W.
DR   GeneID; 850323; -.
DR   KEGG; sce:YCL034W; -.
DR   SGD; S000000539; LSB5.
DR   VEuPathDB; FungiDB:YCL034W; -.
DR   eggNOG; ENOG502QR8R; Eukaryota.
DR   HOGENOM; CLU_036827_2_0_1; -.
DR   InParanoid; P25369; -.
DR   OMA; GMATNSE; -.
DR   BioCyc; YEAST:G3O-29294-MON; -.
DR   PRO; PR:P25369; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25369; protein.
DR   GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR   GO; GO:0005938; C:cell cortex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0051666; P:actin cortical patch localization; IGI:SGD.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:SGD.
DR   GO; GO:0007015; P:actin filament organization; IPI:SGD.
DR   GO; GO:0006897; P:endocytosis; IGI:SGD.
DR   CDD; cd14232; GAT_LSB5; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR044103; GAT_LSB5.
DR   InterPro; IPR045007; LSB5.
DR   PANTHER; PTHR47789; PTHR47789; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Endocytosis; Reference proteome.
FT   CHAIN           1..354
FT                   /note="LAS seventeen-binding protein 5"
FT                   /id="PRO_0000084502"
FT   DOMAIN          15..161
FT                   /note="VHS"
FT   REGION          160..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  39872 MW;  35772B575D40BEB2 CRC64;
     MGFLSDHPHT AITETIFRIV SSRDYTLEVE LAPLIQLIKA DHNDYNYTVN QEEAARALRK
     KIKYGNRLQQ SRTLDLLDLF ISQGVKFTVM YNDDKLLQRL RGMATNSENS GSGEKYEPRI
     IKKCAAYAIS WLNYITQNNL ENARAYSGLY QLGQTVKQRY SKSSRSRRSG GGSGGRSNFM
     DDSADDTLYQ SNSLTSADRL YRIPQINMNK EAPRIRLIIS DALASAVSLQ NSLIGLPKGK
     FSTDDEEATS KFIQARAIRR KVLRYLQLVT EGEFLGSLIH ANDELVAALT AYDDRSAQDD
     SSDESDHGSY DDGIYDENEQ DNSRYIDSES SEEESLSSYQ PSTISNPFGD HNKI
 
 
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