VPS10_YEAST
ID VPS10_YEAST Reviewed; 1579 AA.
AC P32319; D6VPY3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Vacuolar protein sorting/targeting protein VPS10;
DE AltName: Full=Carboxypeptidase Y receptor;
DE Short=CPY receptor;
DE AltName: Full=Carboxypeptidase Y-deficient protein 1;
DE AltName: Full=Sortilin VPS10;
DE AltName: Full=Vacuolar carboxypeptidase sorting receptor VPS10;
DE AltName: Full=Vacuolar protein sorting-associated protein 10;
DE AltName: Full=Vacuolar protein-targeting protein 1;
DE Flags: Precursor;
GN Name=PEP1; Synonyms=VPS10, VPT1; OrderedLocusNames=YBL017C;
GN ORFNames=YBL03.22, YBL0302;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8187177; DOI=10.1016/0092-8674(94)90219-4;
RA Marcusson E.G., Horazdovsky B.F., Cereghino J.L., Gharakhanian E.,
RA Emr S.D.;
RT "The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by
RT the VPS10 gene.";
RL Cell 77:579-586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441754; DOI=10.1002/yea.320080910;
RA van Dyck L., Purnelle B., Skala J., Goffeau A.;
RT "An 11.4 kb DNA segment on the left arm of yeast chromosome II carries the
RT carboxypeptidase Y sorting gene PEP1, as well as ACH1, FUS3 and a putative
RT ARS.";
RL Yeast 8:769-776(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=3538017; DOI=10.1073/pnas.83.23.9075;
RA Bankaitis V.A., Johnson L.M., Emr S.D.;
RT "Isolation of yeast mutants defective in protein targeting to the
RT vacuole.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9075-9079(1986).
RN [6]
RP FUNCTION.
RX PubMed=3062374; DOI=10.1128/mcb.8.11.4936-4948.1988;
RA Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.;
RT "Protein sorting in Saccharomyces cerevisiae: isolation of mutants
RT defective in the delivery and processing of multiple vacuolar hydrolases.";
RL Mol. Cell. Biol. 8:4936-4948(1988).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=8534908; DOI=10.1091/mbc.6.9.1089;
RA Cereghino J.L., Marcusson E.G., Emr S.D.;
RT "The cytoplasmic tail domain of the vacuolar protein sorting receptor
RT Vps10p and a subset of VPS gene products regulate receptor stability,
RT function, and localization.";
RL Mol. Biol. Cell 6:1089-1102(1995).
RN [8]
RP FUNCTION.
RX PubMed=8662642; DOI=10.1074/jbc.271.20.11865;
RA Westphal V., Marcusson E.G., Winther J.R., Emr S.D., van den Hazel H.B.;
RT "Multiple pathways for vacuolar sorting of yeast proteinase A.";
RL J. Biol. Chem. 271:11865-11870(1996).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=8636229; DOI=10.1083/jcb.133.3.529;
RA Cooper A.A., Stevens T.H.;
RT "Vps10p cycles between the late-Golgi and prevacuolar compartments in its
RT function as the sorting receptor for multiple yeast vacuolar hydrolases.";
RL J. Cell Biol. 133:529-541(1996).
RN [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=10095782; DOI=10.1046/j.1432-1327.1999.00176.x;
RA Jorgensen M.U., Emr S.D., Winther J.R.;
RT "Ligand recognition and domain structure of Vps10p, a vacuolar protein
RT sorting receptor in Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 260:461-469(1999).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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. May execute
CC multiple rounds of sorting by cycling between the late Golgi and a
CC prevacuolar endosome-like compartment. Binds the Golgi-modified P2 form
CC of CPY, and this interaction is dependent on the presence of an intact
CC CPY vacuolar protein sorting signal. {ECO:0000269|PubMed:10095782,
CC ECO:0000269|PubMed:3062374, ECO:0000269|PubMed:3538017,
CC ECO:0000269|PubMed:8187177, ECO:0000269|PubMed:8534908,
CC ECO:0000269|PubMed:8636229, ECO:0000269|PubMed:8662642}.
CC -!- INTERACTION:
CC P32319; Q04338: VTI1; NbExp=2; IntAct=EBI-13123, EBI-20519;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Single-pass type I membrane protein. Prevacuolar compartment membrane;
CC Single-pass type I membrane protein. Note=Cycles between the Golgi
CC apparatus and the prevacuolar compartments.
CC -!- DOMAIN: The lumenal domain contains two regions of approximately 650 AA
CC that exhibit 20% identity. The cytoplasmic domain serves as a Golgi
CC retention/recycling signal. {ECO:0000269|PubMed:10095782,
CC ECO:0000269|PubMed:8534908, ECO:0000269|PubMed:8636229}.
CC -!- MISCELLANEOUS: Present with 7210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC {ECO:0000305}.
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DR EMBL; U07621; AAA18831.1; -; Unassigned_DNA.
DR EMBL; X68577; CAA48568.1; -; Genomic_DNA.
DR EMBL; Z35778; CAA84836.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07103.1; -; Genomic_DNA.
DR PIR; S25329; S25329.
DR RefSeq; NP_009536.1; NM_001178257.1.
DR AlphaFoldDB; P32319; -.
DR SMR; P32319; -.
DR BioGRID; 32681; 205.
DR DIP; DIP-5900N; -.
DR IntAct; P32319; 25.
DR MINT; P32319; -.
DR STRING; 4932.YBL017C; -.
DR TCDB; 9.A.63.1.1; the retromer-dependent vacuolar protein sorting (r-vps) family.
DR MaxQB; P32319; -.
DR PaxDb; P32319; -.
DR PRIDE; P32319; -.
DR EnsemblFungi; YBL017C_mRNA; YBL017C; YBL017C.
DR GeneID; 852264; -.
DR KEGG; sce:YBL017C; -.
DR SGD; S000000113; PEP1.
DR VEuPathDB; FungiDB:YBL017C; -.
DR eggNOG; KOG3511; Eukaryota.
DR GeneTree; ENSGT01030000234563; -.
DR HOGENOM; CLU_000700_0_1_1; -.
DR InParanoid; P32319; -.
DR OMA; IFMHVTT; -.
DR BioCyc; YEAST:G3O-28921-MON; -.
DR PRO; PR:P32319; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32319; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0005048; F:signal sequence binding; IMP:SGD.
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:0000423; P:mitophagy; IMP:SGD.
DR GO; GO:0000425; P:pexophagy; IMP:SGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0007034; P:vacuolar transport; IMP:SGD.
DR GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; TAS:ParkinsonsUK-UCL.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR036278; Sialidase_sf.
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.
DR SUPFAM; SSF50939; SSF50939; 1.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1579
FT /note="Vacuolar protein sorting/targeting protein VPS10"
FT /id="PRO_0000022037"
FT TOPO_DOM 22..1397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1398..1414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1415..1579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 57..68
FT /note="BNR 1"
FT REPEAT 101..112
FT /note="BNR 2"
FT REPEAT 179..190
FT /note="BNR 3"
FT REPEAT 415..426
FT /note="BNR 4"
FT REPEAT 487..498
FT /note="BNR 5"
FT REPEAT 533..544
FT /note="BNR 6"
FT REPEAT 764..775
FT /note="BNR 7"
FT REPEAT 861..872
FT /note="BNR 8"
FT REPEAT 1143..1154
FT /note="BNR 9"
FT REPEAT 1184..1195
FT /note="BNR 10"
FT REGION 1533..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="T -> I (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="D -> E (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="T -> A (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="G -> D (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..99
FT /note="AMNGSY -> SMYESR (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..126
FT /note="GESISPRE -> EKNISSRG (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..153
FT /note="Missing (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..167
FT /note="QFE -> APV (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="P -> A (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> G (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="L -> I (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="F -> L (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="S -> N (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="M -> V (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="K -> R (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089
FT /note="S -> F (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 1266
FT /note="G -> S (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 1476
FT /note="A -> V (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
FT CONFLICT 1557
FT /note="T -> A (in Ref. 1; AAA18831)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1579 AA; 177777 MW; C778A0400612ECF4 CRC64;
MILLHFVYSL WALLLIPLTN AEEFTPKVTK TIAQDSFDIL SFDDSNTLIR KQDTSVTISF
DDGETWEKVE GIEGEITWIY IDPFNRHDRA VATAMNGSYL YITNDQGKSW ERITLPDSGE
SISPRECYIE THPLNKNYFL AKCNYCEKTE VNNDNEENSG DEEGQFEIFN ITRCTDKVFA
SNDGGKSFSE IKSSLERNEN SPISISDCGF AKTSKDSDLE SSDTSIICLF QNMQLIMDEF
SSPYTESKLV LTTDWGKSLK EFDQFKDKVV NGYRILKSHM VVLTQGDRYN DMSSMDVWVS
NDLSNFKMAY MPTQLRHSMQ GEIYEDAMGR IILPMSRERS DQEEDKGIVS EILISDSQGL
KFSPIPWTAN EVFGYINFYQ PTYLKGTMIA SLYPLSRRRN RKGKAKGVKS KGVTKISVDN
GLTWTMLKVV DPDNADSFDC DITDFENCSL QNMFYTREGS TPTAGILMTT GIVGDGSVFD
WGDQRTFISR DGGLTWKLAF DFPCLYAVGD YGNVIVAIPY NADEDDDPQS EFYYSLDQGK
TWTEYQLETT IYPNEVMNTT PDGSGAKFIL NGFTLAHMDG TTNFIYAIDF STAFNDKTCE
ENDFEDWNLA EGKCVNGVKY KIRRRKQDAQ CLVKKVFEDL QLFETACDKC TEADYECAFE
FVRDATGKCV PDYNLIVLSD VCDKTKKKTV PVKPLQLVKG DKCKKPMTVK SVDISCEGVP
KKGTNDKEIV VTENKFDFKI QFYQYFDTVT DESLLMINSR GEAYISHDGG QTIKRFDSNG
ETIIEVVFNP YYNSSAYLFG SKGSIFSTHD RGYSFMTAKL PEARQLGMPL DFNAKAQDTF
IYYGGKNCES ILSPECHAVA YLTNDGGETF TEMLDNAIHC EFAGSLFKYP SNEDMVMCQV
KEKSSQTRSL VSSTDFFQDD KNTVFENIIG YLSTGGYIIV AVPHENNELR AYVTIDGTEF
AEAKFPYDED VGKQEAFTIL ESEKGSIFLH LATNLVPGRD FGNLLKSNSN GTSFVTLEHA
VNRNTFGYVD FEKIQGLEGI ILTNIVSNSD KVAENKEDKQ LKTKITFNEG SDWNFLKPPK
RDSEGKKFSC SSKSLDECSL HLHGYTERKD IRDTYSSGSA LGMMFGVGNV GPNLLPYKEC
STFFTTDGGE TWAEVKKTPH QWEYGDHGGI LVLVPENSET DSISYSTDFG KTWKDYKFCA
DKVLVKDITT VPRDSALRFL LFGEAADIGG SSFRTYTIDF RNIFERQCDF DITGKESADY
KYSPLGSKSN CLFGHQTEFL RKTDENCFIG NIPLSEFSRN IKNCSCTRQD FECDYNFYKA
NDGTCKLVKG LSPANAADVC KKEPDLIEYF ESSGYRKIPL STCEGGLKLD APSSPHACPG
KEKEFKEKYS VSAGPFAFIF ISILLIIFFA AWFVYDRGIR RNGGFARFGE IRLGDDGLIE
NNNTDRVVNN IVKSGFYVFS NIGSLLQHTK TNIAHAISKI RGRFGNRTGP SYSSLIHDQF
LDEADDLLAG HDEDANDLSS FMDQGSNFEI EEDDVPTLEE EHTSYTDQPT TTDVPDTLPE
GNEENIDRPD STAPSNENQ
