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   27-MAR-2024, entry version 177.
DE   RecName: Full=Probable GTPase-activating protein GYL1;
DE   AltName: Full=GYP5-like protein 1;
GN   Name=GYL1; Synonyms=APP2; OrderedLocusNames=YMR192W;
GN   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; 82.
DR   DIP; DIP-2891N; -.
DR   IntAct; Q04322; 21.
DR   MINT; Q04322; -.
DR   STRING; 4932.YMR192W; -.
DR   iPTMnet; Q04322; -.
DR   MaxQB; Q04322; -.
DR   PaxDb; 4932-YMR192W; -.
DR   PeptideAtlas; Q04322; -.
DR   EnsemblFungi; YMR192W_mRNA; YMR192W; YMR192W.
DR   GeneID; 855230; -.
DR   KEGG; sce:YMR192W; -.
DR   AGR; SGD:S000004804; -.
DR   SGD; S000004804; GYL1.
DR   VEuPathDB; FungiDB:YMR192W; -.
DR   eggNOG; KOG1102; Eukaryota.
DR   HOGENOM; CLU_005350_11_0_1; -.
DR   InParanoid; Q04322; -.
DR   OMA; HESECFC; -.
DR   OrthoDB; 2039814at2759; -.
DR   BioCyc; YEAST:G3O-32879-MONOMER; -.
DR   BioGRID-ORCS; 855230; 0 hits in 10 CRISPR screens.
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; IBA:GO_Central.
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   Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR   Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR   InterPro; IPR000195; Rab-GAP-TBC_dom.
DR   InterPro; IPR035969; Rab-GAP_TBC_sf.
DR   PANTHER; PTHR47219:SF9; GTPASE ACTIVATING PROTEIN AND CENTROSOME-ASSOCIATED, ISOFORM B; 1.
DR   PANTHER; PTHR47219; RAB GTPASE-ACTIVATING PROTEIN 1-LIKE; 1.
DR   Pfam; PF00566; RabGAP-TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 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
//