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SEC15_SCHPO
ID   SEC15_SCHPO             Reviewed;         768 AA.
AC   O75006;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Exocyst complex component sec15;
GN   Name=sec15; ORFNames=SPCC1183.01, SPCC1672.13;
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   IDENTIFICATION.
RX   PubMed=11854409; DOI=10.1091/mbc.01-11-0542;
RA   Wang H., Tang X., Liu J., Trautmann S., Balasundaram D., McCollum D.,
RA   Balasubramanian M.K.;
RT   "The multiprotein exocyst complex is essential for cell separation in
RT   Schizosaccharomyces pombe.";
RL   Mol. Biol. Cell 13:515-529(2002).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC   -!- SUBUNIT: The exocyst complex is composed of sec3, sec5, sec6, sec8,
CC       sec10, sec15, exo70 and exo84. Interacts with sec4.
CC   -!- SIMILARITY: Belongs to the SEC15 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA20451.2; -; Genomic_DNA.
DR   PIR; T40841; T40841.
DR   RefSeq; NP_587884.2; NM_001022876.2.
DR   AlphaFoldDB; O75006; -.
DR   SMR; O75006; -.
DR   STRING; 4896.SPCC1183.01.1; -.
DR   SwissPalm; O75006; -.
DR   MaxQB; O75006; -.
DR   PaxDb; O75006; -.
DR   EnsemblFungi; SPCC1183.01.1; SPCC1183.01.1:pep; SPCC1183.01.
DR   GeneID; 2538937; -.
DR   KEGG; spo:SPCC1183.01; -.
DR   PomBase; SPCC1183.01; sec15.
DR   VEuPathDB; FungiDB:SPCC1183.01; -.
DR   eggNOG; KOG2176; Eukaryota.
DR   HOGENOM; CLU_009437_2_0_1; -.
DR   InParanoid; O75006; -.
DR   OMA; RDHYNEV; -.
DR   PRO; PR:O75006; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:PomBase.
DR   GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:PomBase.
DR   Gene3D; 1.10.357.30; -; 1.
DR   Gene3D; 1.20.58.670; -; 1.
DR   InterPro; IPR007225; EXOC6/Sec15.
DR   InterPro; IPR042045; EXOC6/Sec15_C_dom1.
DR   InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR   InterPro; IPR046361; Sec15_C.
DR   PANTHER; PTHR12702; PTHR12702; 1.
DR   Pfam; PF04091; Sec15; 1.
DR   PIRSF; PIRSF025007; Sec15; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Exocytosis; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..768
FT                   /note="Exocyst complex component sec15"
FT                   /id="PRO_0000118958"
FT   COILED          69..115
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   768 AA;  88550 MW;  7639A682EDEB0839 CRC64;
     MDIDVLEFVD KIASIESAGD TLDRLPQLIS LACEKGQETQ VYERLNELAS KSAIRVEQLS
     AENNQDFSKS VNQLSVVRSE LRSLQSLMAD LNTDIQASGR DLQNMKQQLN SLSTSERFLT
     KYHNLVRSCM QVLHQVQYSQ ELLSKKQYLP TLRICSEISE VHLKRLDGLG MYSTIQQYIV
     TTKEAICSAV MEDLHEWLFS IRQKLPLVGK SCSQQIDEAR RRWAREYKED LVNLSSKTSI
     SLELYLLEMM DFSPLDNEIV KISFEPLYIC LQVHSYLGLL SSFRSSFERD RRRQQEFLAP
     KSLTTLDMAV VSEWLNSIAG FMIVEYYILQ CIPNFRSYEE VQNIWTIICE KLVETILSVA
     FTEQSTTTII KLKNQIVLLM HTMERFGFSV ESLRNLCVEL IDAFGGALIL KHSVFFEEAF
     EKDVYAPMIV ETQEEYDHYI APYWNFPSEP FPRTMSFSKM CPLCCTTLSK FVRHFFMFLN
     DSVILATEVN EKAPRFYRRF ILRSLVDRLK SLYPKLALSQ MSQLVKNFYA FEDPLLQIEK
     SLVLNKPIHQ IGAEASSSNN VKSTELLEGL ANARKSALHE IFVKINLKID DFLGLAEYDW
     TTTQVRKDVS GYLQEMVTYL QTMYLESLAG LPKHDKSYVY LETLDHLCTA MVDLLSDPSI
     RKVTTAAAEG FKLDVEYLES FAAQVPDQSI VNADSFIELR QCANLLLGDN MEEYLDTDKF
     MRDFNRLQPA VAIKFLERHI NNYSANPLSN DRPKRRAIEI LIATLKKR
 
 
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