GYL1_YEAST
ID GYL1_YEAST Reviewed; 720 AA.
AC Q04322; D6W016;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Probable GTPase-activating protein GYL1;
DE AltName: Full=GYP5-like protein 1;
GN Name=GYL1; Synonyms=APP2; OrderedLocusNames=YMR192W; ORFNames=YM9646.04;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [4]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=EJY251-11b;
RX PubMed=15542864; DOI=10.1074/mcp.m400154-mcp200;
RA Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,
RA Gygi S.P.;
RT "A proteomic strategy for gaining insights into protein sumoylation in
RT yeast.";
RL Mol. Cell. Proteomics 4:246-254(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH GYP5, AND
RP IDENTIFICATION IN SEC4-CONTAINING COMPLEXES.
RX PubMed=15331637; DOI=10.1242/jcs.01349;
RA Chesneau L., Dupre S., Burdina A., Roger J., Le Panse S., Jacquet M.,
RA Cuif M.-H.;
RT "Gyp5p and Gyl1p are involved in the control of polarized exocytosis in
RT budding yeast.";
RL J. Cell Sci. 117:4757-4767(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH GYP5 AND RVS167.
RX PubMed=15802519; DOI=10.1534/genetics.104.040063;
RA Friesen H., Colwill K., Robertson K., Schub O., Andrews B.;
RT "Interaction of the Saccharomyces cerevisiae cortical actin patch protein
RT Rvs167p with proteins involved in ER to Golgi vesicle trafficking.";
RL Genetics 170:555-568(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17 AND SER-37, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17; SER-37; SER-73 AND
RP SER-139, AND 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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: Probable GTPase-activating protein which stimulates the GTP
CC hydrolysis rate by GYP5 of YPT1 and SEC4. Involved in ER to Golgi
CC trafficking and polarized exocytosis. {ECO:0000269|PubMed:15331637,
CC ECO:0000269|PubMed:15802519}.
CC -!- SUBUNIT: Interacts with GYP5 and RVS167. Is part of SEC4-containing
CC complexes. {ECO:0000269|PubMed:15331637, ECO:0000269|PubMed:15802519}.
CC -!- INTERACTION:
CC Q04322; P53281: LSB1; NbExp=2; IntAct=EBI-27427, EBI-23329;
CC Q04322; P43603: LSB3; NbExp=6; IntAct=EBI-27427, EBI-22980;
CC Q04322; O14455: RPL36B; NbExp=2; IntAct=EBI-27427, EBI-14624;
CC Q04322; P39743: RVS167; NbExp=8; IntAct=EBI-27427, EBI-14500;
CC Q04322; P53049: YOR1; NbExp=2; IntAct=EBI-27427, EBI-29324;
CC Q04322; P32793: YSC84; NbExp=6; IntAct=EBI-27427, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15331637}. Bud
CC {ECO:0000269|PubMed:15331637}. Bud neck {ECO:0000269|PubMed:15331637}.
CC -!- MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GYP5 family. {ECO:0000305}.
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DR EMBL; Z47815; CAA87813.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10090.1; -; Genomic_DNA.
DR PIR; S50920; S50920.
DR RefSeq; NP_013917.1; NM_001182698.1.
DR AlphaFoldDB; Q04322; -.
DR SMR; Q04322; -.
DR BioGRID; 35370; 80.
DR DIP; DIP-2891N; -.
DR IntAct; Q04322; 21.
DR MINT; Q04322; -.
DR STRING; 4932.YMR192W; -.
DR iPTMnet; Q04322; -.
DR MaxQB; Q04322; -.
DR PaxDb; Q04322; -.
DR PRIDE; Q04322; -.
DR EnsemblFungi; YMR192W_mRNA; YMR192W; YMR192W.
DR GeneID; 855230; -.
DR KEGG; sce:YMR192W; -.
DR SGD; S000004804; GYL1.
DR VEuPathDB; FungiDB:YMR192W; -.
DR eggNOG; KOG1102; Eukaryota.
DR HOGENOM; CLU_005350_11_0_1; -.
DR InParanoid; Q04322; -.
DR OMA; YLSYHET; -.
DR BioCyc; YEAST:G3O-32879-MON; -.
DR PRO; PR:Q04322; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04322; protein.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:SGD.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0017157; P:regulation of exocytosis; IGI:SGD.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; ER-Golgi transport; Exocytosis;
KW GTPase activation; Isopeptide bond; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..720
FT /note="Probable GTPase-activating protein GYL1"
FT /id="PRO_0000208062"
FT DOMAIN 297..477
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..696
FT /evidence="ECO:0000255"
FT COMPBIAS 1..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15542864"
SQ SEQUENCE 720 AA; 82131 MW; E1423DB4F15F7267 CRC64;
MNSNEDIHEE RIEVPRTPHQ TQPEKDSDRI ALRDEISVPE GDEKAYSDEK VEMATTNASS
NFGSNESAKD GESIGAFSNP HEALMQSKLR EESQSKTILP SDDLSQQLET EESKVEEALK
RITSPPLPPR ADCIEESASA LKSSLPPVLA GNKNDQAPLD RPQLPPRQVV NAETLHLKAP
HGNATPSKSP TSAVGNSSSS TPPTLPPRRI EDPLDLAAQK HFLASTFKRN MLFYKSEDNS
IKCDLDKNIL NLKEDSKKIN NNEIPEEVSS FWLKVIGDYQ NILINDIETL HFQLSRGIPA
AYRLVVWQLV SYAKSKSFDP IYETYLTEMA PFDVQEFENQ LKMMDEVPSE YVKRISNVLK
AYLLFDPECE FSTDIAYIIN MILDVCEEEA NAFGLLVRLM KVYGLRLLFL PSASEIDILC
YKFDRLVEEF YPEIHNHMVE KGVRSSMFLP GFFTTLFQKK LPTEIQPRIG DMVFLEGIDS
IMRILATLLS NSRDHLLKMG FDDMLELLKS GLLDAYIKQN DGTRGDTLLS NECMDKLLQD
SMMKVAITPK TMKKYSSEYE EIHRLDNEKE VQYKSITEKN LHLQKHVRKL ENDYTSLNRE
HVTIANELVK NRLNIESVLN ENNGYKLQIL DLKKKLDSEK KKQVLGVYVP NDLKKDLEET
MKKNTQVMDE NLKLQDRISE LERLIEEIKT ANKNGTLFEY SNSKNNPLGA GWSGFKKVFK
