VPS17_YEAST
ID VPS17_YEAST Reviewed; 551 AA.
AC P32913; D6W2J0; Q12279;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Vacuolar protein sorting-associated protein 17;
DE AltName: Full=Carboxypeptidase Y-deficient protein 21;
GN Name=VPS17; Synonyms=PEP21; OrderedLocusNames=YOR132W;
GN ORFNames=O3314, YOR3314W;
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=8416961; DOI=10.1016/s0021-9258(18)54188-0;
RA Koehrer K., Emr S.D.;
RT "The yeast VPS17 gene encodes a membrane-associated protein required for
RT the sorting of soluble vacuolar hydrolases.";
RL J. Biol. Chem. 268:559-569(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Plays a role in vesicular protein sorting. Required for the
CC sorting and delivery of a subset of soluble vacuolar hydrolases.
CC Required for retention of late Golgi membrane proteins and vacuolar
CC biogenesis. Component of the membrane-associated retromer complex which
CC is essential in endosome-to-Golgi retrograde transport. The VPS5-VPS17
CC subcomplex may assemble onto the membrane to promote vesicle formation.
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 VPS5 and VPS17. {ECO:0000269|PubMed:9700157}.
CC -!- INTERACTION:
CC P32913; P34110: VPS35; NbExp=3; IntAct=EBI-20366, EBI-20415;
CC P32913; Q92331: VPS5; NbExp=7; IntAct=EBI-20366, EBI-20483;
CC P32913; P53845: YIF1; NbExp=2; IntAct=EBI-20366, EBI-28230;
CC P32913; P53039: YIP1; NbExp=2; IntAct=EBI-20366, EBI-25295;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein;
CC Cytoplasmic side. Note=Membrane-associated on the cytoplasmic side of
CC either the Golgi complex or an intermediate in Golgi to vacuole
CC transport.
CC -!- PTM: Phosphorylated on one or more serine residues.
CC -!- MISCELLANEOUS: Present with 7380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS17 family. {ECO:0000305}.
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DR EMBL; L02869; AAA35213.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64051.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62115.1; -; Genomic_DNA.
DR EMBL; Z75040; CAA99331.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10906.1; -; Genomic_DNA.
DR PIR; S60994; S60994.
DR RefSeq; NP_014775.3; NM_001183551.3.
DR AlphaFoldDB; P32913; -.
DR SMR; P32913; -.
DR BioGRID; 34528; 498.
DR ComplexPortal; CPX-1653; Retromer complex.
DR DIP; DIP-1739N; -.
DR IntAct; P32913; 17.
DR MINT; P32913; -.
DR STRING; 4932.YOR132W; -.
DR TCDB; 9.A.63.1.1; the retromer-dependent vacuolar protein sorting (r-vps) family.
DR iPTMnet; P32913; -.
DR MaxQB; P32913; -.
DR PaxDb; P32913; -.
DR PRIDE; P32913; -.
DR EnsemblFungi; YOR132W_mRNA; YOR132W; YOR132W.
DR GeneID; 854300; -.
DR KEGG; sce:YOR132W; -.
DR SGD; S000005658; VPS17.
DR VEuPathDB; FungiDB:YOR132W; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_028982_1_0_1; -.
DR InParanoid; P32913; -.
DR OMA; LMRDDEM; -.
DR BioCyc; YEAST:G3O-33656-MON; -.
DR PRO; PR:P32913; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32913; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IPI:SGD.
DR GO; GO:0030904; C:retromer complex; IMP:SGD.
DR GO; GO:0030905; C:retromer, tubulation complex; IPI:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IC:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IPI:SGD.
DR CDD; cd06891; PX_Vps17p; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR014461; Retromer_complex_Vps17.
DR InterPro; IPR037907; Vps17_PX.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF011791; Vps17; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..551
FT /note="Vacuolar protein sorting-associated protein 17"
FT /id="PRO_0000065892"
FT DOMAIN 108..227
FT /note="PX"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..385
FT /evidence="ECO:0000255"
FT COMPBIAS 26..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 25
FT /note="D -> G (in Ref. 1; AAA35213)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="A -> T (in Ref. 1; AAA35213)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="I -> V (in Ref. 1; AAA35213)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> G (in Ref. 1; AAA35213)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="P -> S (in Ref. 1; AAA35213)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="A -> T (in Ref. 1; AAA35213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 63204 MW; C709968468144A50 CRC64;
MTSAVPYDPY DDLDNNPFAE PQEEDSEPAA TTTDGSSSMS EERVGTEQTA ASVQDNGTAN
NIQNGLGEEG NATRSKTSNE HNENQQPSQP SERVILPERS DEKKKYTLLA KVTGLERFGS
ATGKKENPTI IFDCSTNLPT FRKQQYKNVK KSYEEFHQLF KYLNVAIQES FVPTLPSAYT
TFGINSEEDR MKVTRNFQLW FNRLSQDPLI IRNEEVAFFI ESDFNTYTPI NKSKSLASGL
KRKTLKQLAP PYDEITELAE FRPLVKSIYV VSQSLQEKLL RVSRNRKMMV QEENAFGQDF
VNLDEHNKLY RRYGKILTAV GDIDSIIATM DMATLYDGLE WIVRDAYAVK EALTNRHFIM
RNLVQAQQNS KAKQEQARRF RSRRDINPMK IDEALRQLKA AAKNEQVLTL KLQRITSNMI
IERKQWISWY EEWIRSSIKE FTLRKIEYER KKLTLLERVR SDIRKADENG GLSRLGRHAV
SNNNSDTSQT LKGDSWTGES NRKSQIPINK IAHTEFDDEL FTEDDGYNSQ DSDTTSLNAR
HAASLLGMST K
