GVP36_YEAST
ID GVP36_YEAST Reviewed; 326 AA.
AC P40531; D6VVP1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein GVP36;
DE AltName: Full=36 kDa Golgi vesicle protein;
GN Name=GVP36; OrderedLocusNames=YIL041W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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 PROTEIN SEQUENCE OF 25-37; 90-100 AND 141-151, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-305 AND LYS-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA Inadome H., Noda Y., Adachi H., Yoda K.;
RT "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT a novel membrane protein, Svp26, discovered in the Sed5-containing
RT compartments.";
RL Mol. Cell. Biol. 25:7696-7710(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, 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).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-305 AND LYS-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16107716}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16107716}.
CC -!- MISCELLANEOUS: Present with 7721 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z46861; CAA86910.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08507.1; -; Genomic_DNA.
DR PIR; S49937; S49937.
DR RefSeq; NP_012223.3; NM_001179391.3.
DR AlphaFoldDB; P40531; -.
DR BioGRID; 34949; 143.
DR DIP; DIP-7930N; -.
DR IntAct; P40531; 5.
DR MINT; P40531; -.
DR STRING; 4932.YIL041W; -.
DR iPTMnet; P40531; -.
DR UCD-2DPAGE; P40531; -.
DR MaxQB; P40531; -.
DR PaxDb; P40531; -.
DR PRIDE; P40531; -.
DR EnsemblFungi; YIL041W_mRNA; YIL041W; YIL041W.
DR GeneID; 854770; -.
DR KEGG; sce:YIL041W; -.
DR SGD; S000001303; GVP36.
DR VEuPathDB; FungiDB:YIL041W; -.
DR eggNOG; ENOG502QQ2V; Eukaryota.
DR HOGENOM; CLU_059017_0_0_1; -.
DR InParanoid; P40531; -.
DR OMA; DAINIMQ; -.
DR BioCyc; YEAST:G3O-31313-MON; -.
DR PRO; PR:P40531; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40531; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD.
DR GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR018859; BAR_dom-cont.
DR Pfam; PF10455; BAR_2; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Golgi apparatus; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CHAIN 2..326
FT /note="Protein GVP36"
FT /id="PRO_0000083881"
FT REGION 299..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 326 AA; 36670 MW; A692CE1C7A62F351 CRC64;
MSFNAFASSL SKKLQEISTS VSEKTQELPS LAQSTQRMVQ ERLGQVTDIS QLPREYTELE
DKVDTIKLIY NHFLGVTAIY ENGSYDYPKY INESVNEFSR SVASKLTELT HATSASEAQN
ILVAPGPIKE PKTLNYALSK VALNSSECLN KMFPTEEQPL ASALLQFSDV QAKIAQARIQ
QDTLIQTKFN KNLRERLSFE IGKADKCRKD VHSMRLRYDV ARTNLANNKK PEKEASLRVQ
METLEDQFAQ VTEDATVCLQ EVISHANFSE DLKELAKAQA EYFETSAGLM KEFLSNSFAE
EPEAKPEVAE EEKPQTAISM NDEDDA
