SYT1_YEAST
ID SYT1_YEAST Reviewed; 1226 AA.
AC Q06836; D6W494;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Arf guanine nucleotide exchange factor SYT1;
DE Short=Arf-GEF SYT1;
DE AltName: Full=Suppressor of YPT3 protein 1;
GN Name=SYT1; OrderedLocusNames=YPR095C; ORFNames=P9513.17;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION.
RX PubMed=10430582; DOI=10.1093/genetics/152.4.1543;
RA Jones S., Jedd G., Kahn R.A., Franzusoff A., Bartolini F., Segev N.;
RT "Genetic interactions in yeast between Ypt GTPases and Arf guanine
RT nucleotide exchangers.";
RL Genetics 152:1543-1556(1999).
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 SUBCELLULAR LOCATION.
RX PubMed=15023338; DOI=10.1016/s1097-2765(04)00083-8;
RA Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
RA Murray D., Emr S.D., Lemmon M.A.;
RT "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
RT homology domains.";
RL Mol. Cell 13:677-688(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277, 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 THR-277, 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: Guanine nucleotide exchange factor for Arf GTPases,
CC stimulating the nucleotide exchange from the GDP-bound to the GTP-bound
CC form. Catalyzes both the GDP release by and the GTP binding to ARF2.
CC Has no exchange activity on Rab GTPases. Involved in vesicular
CC transport. {ECO:0000269|PubMed:10430582}.
CC -!- ACTIVITY REGULATION: Inhibited by brefeldin A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15023338}.
CC -!- DOMAIN: The SEC7 domain is sufficient for nucleotide exchange activity.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U51033; AAB68141.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11510.1; -; Genomic_DNA.
DR PIR; S69078; S69078.
DR RefSeq; NP_015420.1; NM_001184192.1.
DR AlphaFoldDB; Q06836; -.
DR SMR; Q06836; -.
DR BioGRID; 36263; 143.
DR IntAct; Q06836; 2.
DR MINT; Q06836; -.
DR STRING; 4932.YPR095C; -.
DR iPTMnet; Q06836; -.
DR MaxQB; Q06836; -.
DR PaxDb; Q06836; -.
DR PRIDE; Q06836; -.
DR EnsemblFungi; YPR095C_mRNA; YPR095C; YPR095C.
DR GeneID; 856210; -.
DR KEGG; sce:YPR095C; -.
DR SGD; S000006299; SYT1.
DR VEuPathDB; FungiDB:YPR095C; -.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_008280_0_0_1; -.
DR InParanoid; Q06836; -.
DR OMA; QENINIY; -.
DR BioCyc; YEAST:G3O-34236-MON; -.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SCE-5620916; VxPx cargo-targeting to cilium.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR PRO; PR:Q06836; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06836; protein.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0032014; P:positive regulation of ARF protein signal transduction; IDA:SGD.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:SGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Guanine-nucleotide releasing factor; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1226
FT /note="Arf guanine nucleotide exchange factor SYT1"
FT /id="PRO_0000270620"
FT DOMAIN 405..620
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 844..1074
FT /note="PH"
FT REGION 17..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 1226 AA; 137583 MW; 562029624DDAB658 CRC64;
MNQSISSLIK LKFLQSHSND KNGNKKGGSN VSTGIDKLRE SESYRSPFLQ LAEIQEHTNN
DDDKLDVKEC EPTKKHSKLS RIRRKMGRLD LNFRSANEKG SEDDEILVAQ HLRNGQDPEE
MPFKSENNID SIEKVPKPDG ERVTLTSSGS DNVKRNSKHA PFIPVKPALE KFPSSNRLSR
DYRKSQEPTL FNGDRLVPTL PTVSRISTSS SVGSSTAASR YFNPSKRAVV ASSSSSSSSI
KFNSLHAIPL DATPQIELAK QQDEISKRRF GRRRSRTVDV FDYINKNNTA KNKPPLSPSS
FIRTIDEKNT NSLMQDPMGS RGPLLPDDAN IISNDTDGAE ASHPDHQVLS RSRSQSTSFV
QGKGGKRKSI EDEGYHNKLG LPHGSGPTSV YNNKSNANST ITGMSRRSSS IVNALSSFVN
LRSSSLSSSR QQHLQQQQQL QQKLDVSLED LPPVPAPEFS DSCKDFLIKL APYGKFIGII
LTEKDDEFKK NCLNYLLTNC FEFKNDPLDI ALRKLLMFLE LPKETQQIDR LIMAFSFAYY
KAQKSYSKKK GIECPWSNAD QVYFIAFSLL MLHTDYFNPN NKSKMTKHDF VDLVHNDKYS
GGNEIPMAVL TYFYENVTAK ESPKFNYFLM SPMALDDSIL DKDAFDTNFA ITLSSNSMYS
PIDMIKRGSI IPKEASLSPI FYPLTNSISA SGIAPSTAAS CPPSTSGTIN GANLGTANSN
SNRPASNSIS SYFSYNPSSS SSGNATLVQD DINVYSHIIN DTLNEVNLFP EVSKYWNKNA
LKANLLRNEE HKYEKYYSIM NDTKGGYLRF HKSQLNKLNL PNFEILNDNS RSGCKNSDYK
YCKILQMGAI MNLGMPSRKF SIVNSAKIHW KKEFAILTSL GLLICDKMDW INPQMMKDPK
SGTTNYIIDF KSGFSFVPGS TIDVYNGLFA DRERDSLGKS HFASLVLAYT EHHSTGSHTS
NTTAASSSAK HNEGVFEPSS DEEDSITNST DGTSSVSNGE SDNDSVSSSD NQLSSNDSNE
DYHSIKDEYP IFEDENADCL LYLHTCHRNF IWKCANKYER DNWIDSINLF SAYDGCYVEI
GSIANTICNK RKLTILQRME RLRSIKSAKW EKLKKFESTL MLMGKCVPIS TKTKTDMINR
IRQLAVRMDW LIYEIKRSEL FVSIIKEVTR KQAEKNILEH GKGEEEGQGN NDDSDGIDDI
EESFLFNENS LQVCVSDSSY DEYSNE
