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VPS10_SCHPO
ID   VPS10_SCHPO             Reviewed;        1466 AA.
AC   O42930;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Vacuolar protein sorting/targeting protein 10;
DE   AltName: Full=Carboxypeptidase Y receptor;
DE            Short=CPY receptor;
DE   AltName: Full=Sortilin vps10;
DE   AltName: Full=Vacuolar carboxypeptidase sorting receptor vps10;
DE   Flags: Precursor;
GN   Name=vps10; Synonyms=pep1; ORFNames=SPBC16C6.06;
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   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-1419; PHE-1425 AND
RP   PHE-1426.
RX   PubMed=16622069; DOI=10.1099/mic.0.28627-0;
RA   Iwaki T., Hosomi A., Tokudomi S., Kusunoki Y., Fujita Y., Giga-Hama Y.,
RA   Tanaka N., Takegawa K.;
RT   "Vacuolar protein sorting receptor in Schizosaccharomyces pombe.";
RL   Microbiology 152:1523-1532(2006).
CC   -!- FUNCTION: Functions as a sorting receptor in the Golgi compartment
CC       required for the intracellular sorting and delivery of soluble vacuolar
CC       proteins, like carboxypeptidase Y (CPY) and proteinase A. Executes
CC       multiple rounds of sorting by cycling between the late Golgi and a
CC       prevacuolar endosome-like compartment. {ECO:0000269|PubMed:16622069}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:16622069}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:16622069}. Prevacuolar compartment membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Note=Cycles between the Golgi apparatus and the prevacuolar
CC       compartment. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA16914.1; -; Genomic_DNA.
DR   PIR; T39557; T39557.
DR   RefSeq; NP_596804.1; NM_001023825.2.
DR   AlphaFoldDB; O42930; -.
DR   SMR; O42930; -.
DR   BioGRID; 276408; 6.
DR   STRING; 4896.SPBC16C6.06.1; -.
DR   iPTMnet; O42930; -.
DR   MaxQB; O42930; -.
DR   PaxDb; O42930; -.
DR   PRIDE; O42930; -.
DR   EnsemblFungi; SPBC16C6.06.1; SPBC16C6.06.1:pep; SPBC16C6.06.
DR   GeneID; 2539861; -.
DR   KEGG; spo:SPBC16C6.06; -.
DR   PomBase; SPBC16C6.06; vps10.
DR   VEuPathDB; FungiDB:SPBC16C6.06; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   HOGENOM; CLU_000700_0_0_1; -.
DR   InParanoid; O42930; -.
DR   OMA; ATMSEFI; -.
DR   PhylomeDB; O42930; -.
DR   PRO; PR:O42930; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; IDA:PomBase.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:PomBase.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0005048; F:signal sequence binding; ISO:PomBase.
DR   GO; GO:0006895; P:Golgi to endosome transport; IMP:PomBase.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IMP:PomBase.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IMP:PomBase.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR031777; Sortilin_C.
DR   InterPro; IPR031778; Sortilin_N.
DR   InterPro; IPR006581; VPS10.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF15902; Sortilin-Vps10; 2.
DR   Pfam; PF15901; Sortilin_C; 2.
DR   SMART; SM00602; VPS10; 2.
PE   1: Evidence at protein level;
KW   Glycoprotein; Golgi apparatus; Membrane; Nucleotide-binding;
KW   Protein transport; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..1466
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /id="PRO_0000316211"
FT   TOPO_DOM        34..1363
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1364..1384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1385..1466
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          71..82
FT                   /note="BNR 1"
FT   REPEAT          115..126
FT                   /note="BNR 2"
FT   REPEAT          388..399
FT                   /note="BNR 3"
FT   REPEAT          457..468
FT                   /note="BNR 4"
FT   REPEAT          498..509
FT                   /note="BNR 5"
FT   REPEAT          738..749
FT                   /note="BNR 6"
FT   REPEAT          778..789
FT                   /note="BNR 7"
FT   REPEAT          836..847
FT                   /note="BNR 8"
FT   REPEAT          1039..1050
FT                   /note="BNR 9"
FT   REPEAT          1112..1123
FT                   /note="BNR 10"
FT   REPEAT          1153..1164
FT                   /note="BNR 11"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        986
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         1419
FT                   /note="F->A: No cpy1 secretion; localizes to Golgi and
FT                   vacuolar membrane."
FT                   /evidence="ECO:0000269|PubMed:16622069"
FT   MUTAGEN         1425..1426
FT                   /note="FF->AA: No cpy1 secretion; localizes to Golgi and
FT                   vacuolar membrane."
FT   MUTAGEN         1425
FT                   /note="F->A: No cpy1 secretion."
FT                   /evidence="ECO:0000269|PubMed:16622069"
FT   MUTAGEN         1426
FT                   /note="F->A: No cpy1 secretion."
FT                   /evidence="ECO:0000269|PubMed:16622069"
SQ   SEQUENCE   1466 AA;  165062 MW;  CEB315E0F7688D79 CRC64;
     MFFLTKILPL RGRIFPMFGC LLLIVSLITG CIASPAAEVA ETVFDSKPVD FMTFKDSTNT
     LFLNAEFGDV YLSQDNGQSW RNGVISGQVC PIKKLIKHSF ENSRVFALTE CDTVYYSYDN
     GENWDYFTID HPISITQLPF HFHAKNPDYV IFNNQYCSSS GTWVGKICKP DLYYTKDGFQ
     SDPEPMPVGS SYCIFADSSE KMVVSSEEQI ICISLNPNSA ARPPFSHHIV YSDDWFQSIV
     PVQLHNFLGS DGAYGILSTG SFLVAALIDA ATRKLFVYVS QDGYYWEEAL KFHKGFEFDA
     FTILPSTEYS FFIDSLDSHP NNPTGILYSL DSESNTFVIR QMNTNRYVDG YTDFMLIDYL
     DGLQFVNVVE NVDEIEVDPQ VDKVLSSRIT FDGGKTWSTV ASPESSCNSM KQCSLHLFLD
     PHVSHASIAS SKFAPGILLA SGSVGDRLLS ENQMDLFVSE DGGRNWTLSR DGMHLFAMSG
     FGSIFFASEY LDVINEVYYS LDHGQSWVTV TLDKTIVPIK LFASEDPYAE IFYLLAMTDD
     GEQSNYSLFS FNFGKFLPKE CQFSNSESNK NDFEKWYTRY ANGSPICSEM GKKEFFWRKK
     ATSVCSVPKS ITDLHGSFDA CECTDEDYEC NTQFISNDQG ECKLLDFIGS LLCASEDLDT
     FQKIPYRLVP GNKCTPNKRD SHREPQTFNC DSFNEPGTEI TSFLYDFDEK IVDVVYLEGT
     VPEENTFLIG ISVNSHVYFS EDEGKTWDKF SKEEFSSVLP HAYNKNSVYM VTSKNIVYFT
     TNRGKNFYKF KAPSPPNQNG KSLFSFHPSR PAWLLYAGSE NCEKNPFADD CRDVVFVSLD
     FGDTWSRLPS NLEYCSWAKA EKLVVDDTLI FCIRQNTNDP FKKELISSID FFEYEQDEIL
     NDVVGFMIED EYVIVAVQDE EGTSLSLDVS INGLNFASCS FPAYLNVHPK QAYTILDSQT
     HSLFIHVTTN THLGSEWGDI LKSNSNGTYF MTSLANVNRD SVGYVDFERL EGIQGIALAN
     IVSNTKELTD GGTKKLQTLI TFNDGLDWSY LNLVGGEKIV PKCGKNCYLH LHGYTERNQF
     SDPTSTNAAV GLIIGVGSFS PFLIPYEESQ TFISRDAGVT WYRIFDSPHL WAFLDSGSII
     IAVESISPTN VIKYSADEGR TWQEYQFSEK SKVVVDVSTK PSGVGHQVLL LTTDDENAPI
     SSVLIDFDAL YRRTCVFDEE NSEESDFVRW VPTDISGKPL CLRGRISSFY RKSIHKKCRV
     GSSLLVKEEV LSKCECTRAD FECDYNYRRL KDGTCVLVSG LQPPDTREEQ CSVDDAFEWR
     QPTGYKRTPL TECEGGVPLD AGTLHPCPGK EDDYYKAHPK PGGWSIFLTI IFSILLAAVA
     GCILYYYSRR FLKGAIRLGS DSATENPLES GISYTRGAFS SIPIFFSALY QSVRSLFIRS
     TPTNGEFENA AFLQNYEIDD DDEESV
 
 
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