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VPS10_ASHGO
ID   VPS10_ASHGO             Reviewed;        1508 AA.
AC   Q754Q4;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   25-MAY-2022, entry version 97.
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; OrderedLocusNames=AFR018C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Prevacuolar
CC       compartment membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Note=Cycles between the Golgi apparatus and the
CC       prevacuolar compartment. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC       {ECO:0000305}.
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DR   EMBL; AE016819; AAS53389.2; -; Genomic_DNA.
DR   RefSeq; NP_985565.2; NM_210919.2.
DR   AlphaFoldDB; Q754Q4; -.
DR   SMR; Q754Q4; -.
DR   STRING; 33169.AAS53389; -.
DR   EnsemblFungi; AAS53389; AAS53389; AGOS_AFR018C.
DR   GeneID; 4621804; -.
DR   KEGG; ago:AGOS_AFR018C; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   HOGENOM; CLU_000700_0_1_1; -.
DR   InParanoid; Q754Q4; -.
DR   OMA; IFMHVTT; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; IBA:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 2.
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   3: Inferred from homology;
KW   Glycoprotein; Golgi apparatus; Membrane; Protein transport; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1508
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /id="PRO_0000407502"
FT   TOPO_DOM        21..1348
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1349..1369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1370..1404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1405..1425
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1426..1508
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REPEAT          164..172
FT                   /note="BNR 1"
FT   REPEAT          372..381
FT                   /note="BNR 2"
FT   REPEAT          452..461
FT                   /note="BNR 3"
FT   REPEAT          497..507
FT                   /note="BNR 4"
FT   REPEAT          717..726
FT                   /note="BNR 5"
FT   REPEAT          812..822
FT                   /note="BNR 6"
FT   REPEAT          1095..1105
FT                   /note="BNR 7"
FT   REPEAT          1137..1146
FT                   /note="BNR 8"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        789
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        911
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1508 AA;  169235 MW;  82214594B3CC3129 CRC64;
     MVGMLFVWQT FLFVWACAAA VEVGEKPRPV IDIVRDVDNL GSIWQFKGTN TLIRHQGREI
     LVRHGGDQWS TVKKFDQGVN TVEVDPYYPE RRAFAWLENN ELYKTDDCGK TWARVMHVEA
     EPGENLQRYS VYSNPDNYKY LMVTSHFERK DSSPVLAESY EKQWVSQDGG KTIAPLGHPD
     PGVYRLCHFL RQARNHDVAK DSTILCIEHD AQKHTAVLYR TDDFGKSKQA LDSFDDEIVS
     SVGLLGKYIL VTTTEDAYNK HAVQHVWVSR DGDKFQKIIF PTHIRDNFFR AVTTSTGNQI
     IFSIPAGKHS HSRKNALYAN YISDSSGIQF HAVADSLDER YKELGPVMAL DANGTLSMVA
     RKSSTEDQVT LLSYDYGYSW QPMHLAEGED HKALGCSKGG KECELPVQLS QLVSSSGLVG
     HGESATSGIL MGIVLKKRGS RGPRKHKYLS VISRDYGLTW SVAFEYPVLS FAGNYGNILL
     ACPYNPGDDG DPEEEIYYSL DQGHTWEEHH IEGKYEFVRV HSAISDGSST AFSFLAVGDD
     QNTIVVDCIF TDIHNGKECT DGDMEEYKLR NGNCLNGARY TINKRKSEAA CLLKNDPSVI
     NPLVKPCDCT NADYECSLGF LGLPDKGCTA DLGMLRSAGA CKDNPRELMP MHKIKGNECT
     KDLNIEPVKV DCSAVQNRPD IEVTAHVFKT QFETYQYFNS AEDDSLMVLT KDKRALISHD
     SGKTFKMLDT LGSGAELITF NRYFGDLAYI FASDDVLYIT DDRGYHFYAV DLPEVRHLFL
     PLAFHAKDNQ TFIYFGGKDC EKLGPKCHST AYITTDGGRN FREMLTGAVS CEFVGSIYSH
     PANKDMIMCE IENKKERRNI LLRSTDEFRT SDKVFDSIIG FHTTGDFTAI AVSEGRQQVS
     SYLTIDGVHF NESRFPPDFV APEKQQSYSV LSAHEGAIFL HMSKSLVKHK EYGTLVKSDS
     NGIDFVVLKD GVNSNAEGLV DFETPEGLDG VILINVVENL DQVQKGKAKA KHLKTAISFN
     DGVDWKYLSP PGKDSSGKKY PCHGKNRAKC SLNLHGYTER KDLRDTYSSG SAIGYMLGVG
     NVGEHLLPYE QCSTFLTTDG GVTWTEVKST PHQWEFGDRG SIIVLVPDGV KTNSITYSVD
     AGRSWQDFKF ADEEVIIDDI ITVPYDTSMR FLLISKEHLR GKSKTYAISF AHIFKRQCEF
     HPGGGRHNGD FEYTSIKHPD YKCLFGKEVE FLKRIKYDCF IGNASYTKDY RTSRICPCTR
     QDFECDYNYI RTSDGTCKLP SGVKPEAPSA VCERNRDLVE YFQPTGYRKI PLSKCEGGLK
     LQRTDSPHPC PGKEKEFYEK YPSSTNASSV VFWWLLLTMV LLVPLWVIYD RGIRRNGGFS
     RFGEIRLDDD DLIEENGLDR AINKVVKVGA YGVAGLFGFL LLLKSKAGAR IRRFRESVSS
     RRGPSYSSLI SDQFLDDAND LLVGHDNDAN NLNAFLDEDG QHFDVDDEIE GADQASYHDD
     VDLGRTSE
 
 
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