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SLA2_SCHPO
ID   SLA2_SCHPO              Reviewed;        1102 AA.
AC   Q9P6L5; P78916;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Endocytosis protein end4;
DE   AltName: Full=SLA2 protein homolog;
GN   Name=end4; Synonyms=sla2; ORFNames=SPAC688.11;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1102.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [4]
RP   FUNCTION.
RX   PubMed=15300681; DOI=10.1002/yea.1134;
RA   Iwaki T., Tanaka N., Takagi H., Giga-Hama Y., Takegawa K.;
RT   "Characterization of end4+, a gene required for endocytosis in
RT   Schizosaccharomyces pombe.";
RL   Yeast 21:867-881(2004).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15827087; DOI=10.1242/jcs.02311;
RA   Castagnetti S., Behrens R., Nurse P.;
RT   "End4/Sla2 is involved in establishment of a new growth zone in
RT   Schizosaccharomyces pombe.";
RL   J. Cell Sci. 118:1843-1850(2005).
RN   [6]
RP   REVISION OF GENE MODEL, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA   Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA   Hagan I.M., Miller C.J.;
RT   "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT   additional genes required for growth and viability.";
RL   Genetics 187:1207-1217(2011).
CC   -!- FUNCTION: Required for cellular morphogenesis and polarization of the
CC       cortical cytoskeleton. Required for establishment of new polarized
CC       growth zones where it acts in actin organization. Involved plasma
CC       membrane internalization and is essential for fluid-phase endocytosis.
CC       {ECO:0000269|PubMed:15300681, ECO:0000269|PubMed:15827087}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:15827087}. Note=Localizes at cell ends during
CC       interphase and to the medial ring at cell division.
CC   -!- SIMILARITY: Belongs to the SLA2 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB90777.2; -; Genomic_DNA.
DR   EMBL; D89267; BAA13928.1; -; mRNA.
DR   PIR; T43195; T43195.
DR   RefSeq; NP_594069.2; NM_001019493.2.
DR   AlphaFoldDB; Q9P6L5; -.
DR   SMR; Q9P6L5; -.
DR   BioGRID; 279759; 19.
DR   STRING; 4896.SPAC688.11.1; -.
DR   MaxQB; Q9P6L5; -.
DR   PaxDb; Q9P6L5; -.
DR   EnsemblFungi; SPAC688.11.1; SPAC688.11.1:pep; SPAC688.11.
DR   GeneID; 2543336; -.
DR   KEGG; spo:SPAC688.11; -.
DR   PomBase; SPAC688.11; end4.
DR   VEuPathDB; FungiDB:SPAC688.11; -.
DR   eggNOG; KOG0980; Eukaryota.
DR   HOGENOM; CLU_004601_0_0_1; -.
DR   InParanoid; Q9P6L5; -.
DR   OMA; IREYVYF; -.
DR   Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q9P6L5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR   GO; GO:0035841; C:new growing cell tip; IDA:PomBase.
DR   GO; GO:0035840; C:old growing cell tip; IDA:PomBase.
DR   GO; GO:0003779; F:actin binding; ISM:PomBase.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0035615; F:clathrin adaptor activity; ISS:PomBase.
DR   GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISM:PomBase.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:PomBase.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:PomBase.
DR   GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR011417; ANTH_dom.
DR   InterPro; IPR013809; ENTH.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR035964; I/LWEQ_dom_sf.
DR   InterPro; IPR002558; ILWEQ_dom.
DR   InterPro; IPR030224; Sla2_fam.
DR   PANTHER; PTHR10407; PTHR10407; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00307; ILWEQ; 1.
DR   SUPFAM; SSF109885; SSF109885; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50945; I_LWEQ; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis;
KW   Reference proteome.
FT   CHAIN           1..1102
FT                   /note="Endocytosis protein end4"
FT                   /id="PRO_0000071944"
FT   DOMAIN          9..139
FT                   /note="ENTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT   DOMAIN          858..1100
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT   REGION          265..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          338..661
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1102 AA;  124373 MW;  9101E230871A5DD0 CRC64;
     MSSFRLQSDH MQSDASLMTS VRKATSIDET APKRKHVRSC IIFTWDHHTA RPFWTAIKVQ
     PLLANEVQTF KALITIHRVL QEGHKSALVD SQSEKGWLKT CERQYDGESS PKGYSDLIRD
     YVDYLLDKLS FHAQHPEFNG TFEYKEYISL RQVDDPNEGY ETVYDMMNLQ DHIDEFQKQL
     FSNFKRSNKN ECRIAALVPL VQESYGIYRF LTSMLRALYS TVDAPETLEP LKHRYKSQHH
     RLRQFYADCS NLRYLTSLIS VPRLPHDPPD LEGDDNIPDL PKRPASIAPQ PTGASTIAPQ
     PTGTSPSPPV EMNFPDTSDI TPAYSEPEPI QDFWSDPTLD QQLAAQQAAQ QAAQQQAELA
     AQQAAAQQAQ LAAQQAAEME RQRMAAQQHQ QALEAIQMAQ AEQQRIAQEQ LAQQQFQMQT
     QGQLAELEQQ LLATRGQLEQ SNVLLNQYDA RVRTLENELS QAGVNLQEQI HQNDDLIESL
     KNQILTWKNK YEALAKLYTQ LRQEHLDLLS KYKQIQLKAS SAQEAIDKKE KMEREMKNKN
     LELADMILER DRARHELETM HRSQRDKQES TERELRLLQE KAASLERNKS SEVSNLLSRY
     NTEVAHLEDA LHSKDRELAN LGVELKSTEN RYRQLLQEKE EELEIQKAAV DESLLQLSKL
     QLDRNDIDQA MDTQIDELLK SQLEKLDDIV DSVLATGIQR LDTSLYELDS PMHAGNQYAT
     PEFILSTIEN ASNNATDFST AFNNYFADGP NADHSEVING VNLFSTAIYE VANNAKGLSR
     TTGDDQGSDR FVGLSRDLVN MAKRFLSSLF SVNTRKMDVN VKTDLVIGEN IELQRYLQQL
     TQYSEKFLNK ESENTVGLLN APGENIEELV DNQLAETAQA IQQAILRLQN IAAKPKDDSL
     SPSELQVHDS LLSASIAITE AIARLIKAAT ASQAEIVAQG RGSSSRGAFY KKHNRWTEGL
     ISAAKAVARA TTTLIETADG VVNGTSSFEH LIVACNGVSA ATAQLVAASR VKANFASKVQ
     DHLEDAAKAV TEACKALVRQ VESVALKAKE VQHEDFSSLG VHEYRRKEIE QQVQILKLEN
     DLVAARRRLF DMRKTSYHVA EE
 
 
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