VPS35_YEAST
ID VPS35_YEAST Reviewed; 944 AA.
AC P34110; D6VW33;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Vacuolar protein sorting-associated protein 35;
DE AltName: Full=Vacuolar protein-targeting protein 7;
GN Name=VPS35; Synonyms=VPT7; OrderedLocusNames=YJL154C; ORFNames=J0580;
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].
RX PubMed=1498362; DOI=10.1091/mbc.3.4.415;
RA Paravicini G., Horazdovsky B.F., Emr S.D.;
RT "Alternative pathways for the sorting of soluble vacuolar proteins in
RT yeast: a vps35 null mutant missorts and secretes only a subset of vacuolar
RT hydrolases.";
RL Mol. Biol. Cell 3:415-427(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-937.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [5]
RP IDENTIFICATION IN THE RETROMER COMPLEX.
RX PubMed=9700157; DOI=10.1083/jcb.142.3.665;
RA Seaman M.N., McCaffery J.M., Emr S.D.;
RT "A membrane coat complex essential for endosome-to-Golgi retrograde
RT transport in yeast.";
RL J. Cell Biol. 142:665-681(1998).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-868, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-846 AND SER-848, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in vesicular protein sorting. Required for the
CC endosome-to-Golgi retrieval of the vacuolar protein sorting receptor
CC VPS10. Vacuolar carboxypeptidase Y (CPY) sorting is completely
CC dependent on the presence of functional VPS35. The latter may play a
CC role in the function, modification or packaging of a CPY-specific
CC receptor complex. Component of the membrane-associated retromer complex
CC which is essential in endosome-to-Golgi retrograde transport. The
CC VPS29-VPS26-VPS35 subcomplex may be involved in cargo selection.
CC -!- SUBUNIT: Component of the retromer complex which consists of VPS29,
CC VPS26, VPS35, VPS5 and VPS17. Component of a retromer subcomplex
CC consisting of VPS29, VPS26 and VPS35. {ECO:0000269|PubMed:9700157}.
CC -!- INTERACTION:
CC P34110; P32913: VPS17; NbExp=3; IntAct=EBI-20415, EBI-20366;
CC P34110; P38759: VPS29; NbExp=2; IntAct=EBI-20415, EBI-13092;
CC P34110; Q92331: VPS5; NbExp=3; IntAct=EBI-20415, EBI-20483;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}.
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DR EMBL; S42186; AAB22844.1; -; Genomic_DNA.
DR EMBL; Z49429; CAA89449.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60801.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08649.1; -; Genomic_DNA.
DR PIR; S56936; S56936.
DR RefSeq; NP_012381.1; NM_001181587.1.
DR AlphaFoldDB; P34110; -.
DR SMR; P34110; -.
DR BioGRID; 33606; 435.
DR ComplexPortal; CPX-1653; Retromer complex.
DR DIP; DIP-1743N; -.
DR IntAct; P34110; 17.
DR MINT; P34110; -.
DR STRING; 4932.YJL154C; -.
DR TCDB; 9.A.63.1.1; the retromer-dependent vacuolar protein sorting (r-vps) family.
DR iPTMnet; P34110; -.
DR MaxQB; P34110; -.
DR PaxDb; P34110; -.
DR PRIDE; P34110; -.
DR EnsemblFungi; YJL154C_mRNA; YJL154C; YJL154C.
DR GeneID; 853287; -.
DR KEGG; sce:YJL154C; -.
DR SGD; S000003690; VPS35.
DR VEuPathDB; FungiDB:YJL154C; -.
DR eggNOG; KOG1107; Eukaryota.
DR GeneTree; ENSGT00390000007315; -.
DR HOGENOM; CLU_005836_0_0_1; -.
DR InParanoid; P34110; -.
DR OMA; WWVVENP; -.
DR BioCyc; YEAST:G3O-31595-MON; -.
DR Reactome; R-SCE-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:P34110; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P34110; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IPI:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0030904; C:retromer complex; IMP:SGD.
DR GO; GO:0030906; C:retromer, cargo-selective complex; IPI:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; IGI:ParkinsonsUK-UCL.
DR GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IGI:ParkinsonsUK-UCL.
DR GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IPI:SGD.
DR Gene3D; 1.25.40.660; -; 1.
DR InterPro; IPR005378; Vps35.
DR InterPro; IPR042491; Vps35_C.
DR PANTHER; PTHR11099; PTHR11099; 1.
DR Pfam; PF03635; Vps35; 1.
DR PIRSF; PIRSF009375; Retromer_Vps35; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..944
FT /note="Vacuolar protein sorting-associated protein 35"
FT /id="PRO_0000065899"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 14..20
FT /note="Missing (in Ref. 1; AAB22844)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="D -> E (in Ref. 1; AAB22844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 944 AA; 109142 MW; DE1BC57B9DFB606E CRC64;
MAYADSPENA IAVIKQRTAL MNRCLSQHKL MESLQHTSIM LTELRNPNLS PKKYYELYVI
IFDSLTNLST YLIENHPQNH HLADLYELVQ YTGNVVPRLY LMITVGTSYL TFNEAPKKEI
LKDMIEMCRG VQNPIRGLFL RYYLSQRTKE LLPEDDPSFN SQFIMNNFIE MNKLWVRLQH
QGPLRERETR TRERKELQIL VGSQLVRLSQ IIDDNFQMYK QDILPTILEQ VIQCRDLVSQ
EYLLDVICQV FADEFHLKTL DTLLQTTLHL NPDVSINKIV LTLVDRLNDY VTRQLEDDPN
ATSTNAYLDM DVFGTFWDYL TVLNHERPDL SLQQFIPLVE SVIVLSLKWY PNNFDNLNKL
FELVLQKTKD YGQKNISLES EHLFLVLLSF QNSKLQLTSS TTAPPNSPVT SKKHFIFQLI
SQCQAYKNIL ALQSISLQKK VVNEIIDILM DREVEEMADN DSESKLHPPG HSAYLVIEDK
LQVQRLLSIC EPLIISRSGP PANVASSDTN VDEVFFNRHD EEESWILDPI QEKLAHLIHW
IMNTTSRKQT MKNKIQFSLE AQLEILLLIK SSFIKGGINV KYTFPAIITN FWKLMRKCRM
IQEYLLKKRP DNKTLLSHYS NLLKQMFKFV SRCINDIFNS CNNSCTDLIL KLNLQCAILA
DQLQLNEISY DFFSQAFTIF EESLSDSKTQ LQALIYIAQS LQKTRSLYKE AYYDSLIVRC
TLHGSKLLKK QDQCRAVYLC SHLWWATEIS NIGEEEGITD NFYRDGKRVL ECLQRSLRVA
DSIMDNEQSC ELMVEILNRC LYYFIHGDES ETHISIKYIN GLIELIKTNL KSLKLEDNSA
SMITNSISDL HITGENNVKA SSNADDGSVI TDKESNVAIG SDGTYIQLNT LNGSSTLIRG
VVATASGSKL LHQLKYIPIH HFRRTCEYIE SQREVDDRFK VIYV
