VPS29_YEAST
ID VPS29_YEAST Reviewed; 282 AA.
AC P38759; D3DKV7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Vacuolar protein sorting-associated protein 29;
DE AltName: Full=Carboxypeptidase Y-deficient protein 11;
DE AltName: Full=Vesicle protein sorting 29;
GN Name=VPS29; Synonyms=PEP11, VTP6; OrderedLocusNames=YHR012W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP IDENTIFICATION.
RA Friedrichsen D.M., Brands A., Hiller M.A., Bachhawat A., Jones E.W.;
RT "Analysis of the PEP11 locus in Saccharomyces cerevisiae.";
RL Unpublished observations (JAN-1995).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION BY 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 [7]
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. Component of the membrane-associated retromer complex which is
CC essential in endosome-to-Golgi retrograde transport. The VPS29-VPS26-
CC 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 P38759; P34110: VPS35; NbExp=2; IntAct=EBI-13092, EBI-20415;
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS29 family. {ECO:0000305}.
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DR EMBL; U10400; AAB68947.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06701.1; -; Genomic_DNA.
DR PIR; S46793; S46793.
DR RefSeq; NP_011876.1; NM_001179142.1.
DR AlphaFoldDB; P38759; -.
DR SMR; P38759; -.
DR BioGRID; 36439; 398.
DR ComplexPortal; CPX-1653; Retromer complex.
DR DIP; DIP-4205N; -.
DR IntAct; P38759; 7.
DR MINT; P38759; -.
DR STRING; 4932.YHR012W; -.
DR TCDB; 9.A.63.1.1; the retromer-dependent vacuolar protein sorting (r-vps) family.
DR iPTMnet; P38759; -.
DR MaxQB; P38759; -.
DR PaxDb; P38759; -.
DR PRIDE; P38759; -.
DR EnsemblFungi; YHR012W_mRNA; YHR012W; YHR012W.
DR GeneID; 856403; -.
DR KEGG; sce:YHR012W; -.
DR SGD; S000001054; VPS29.
DR VEuPathDB; FungiDB:YHR012W; -.
DR eggNOG; KOG3325; Eukaryota.
DR GeneTree; ENSGT00390000012669; -.
DR HOGENOM; CLU_063749_0_0_1; -.
DR InParanoid; P38759; -.
DR OMA; IGCCNGY; -.
DR BioCyc; YEAST:G3O-31075-MON; -.
DR Reactome; R-SCE-3238698; WNT ligand biogenesis and trafficking.
DR PRO; PR:P38759; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38759; 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:0030906; C:retromer, cargo-selective complex; IPI: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 Gene3D; 3.60.21.10; -; 2.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR InterPro; IPR028661; Vps29.
DR PANTHER; PTHR11124; PTHR11124; 1.
DR PANTHER; PTHR11124:SF12; PTHR11124:SF12; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00040; yfcE; 1.
PE 1: Evidence at protein level;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..282
FT /note="Vacuolar protein sorting-associated protein 29"
FT /id="PRO_0000058305"
FT REGION 173..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 31013 MW; D190DBA2377E0653 CRC64;
MLLLALSDAH IPDRATDLPV KFKKLLSVPD KISQVALLGN STKSYDFLKF VNQISNNITI
VRGEFDNGHL PSTKKDKASD NSRPMEEIPM NSIIRQGALK IGCCSGYTVV PKNDPLSLLA
LARQLDVDIL LWGGTHNVEA YTLEGKFFVN PGSCTGAFNT DWPIVFDVED SDEAVTSEVD
KPTKENQSED DDAKGGSTGK EQPGSYTPKE GTAGERENEN ESNVKPENQF KEDEVDMSDS
DINGSNSPSF CLLDIQGNTC TLYIYLYVNG EVKVDKVVYE KE
