ID SAC7_YEAST Reviewed; 654 AA.
AC P17121; D6VT23; Q04163;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 27-MAR-2024, entry version 193.
DE RecName: Full=GTPase-activating protein SAC7;
GN Name=SAC7; OrderedLocusNames=YDR389W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-654.
RX PubMed=2183030; DOI=10.1128/mcb.10.5.2308-2314.1990;
RA Dunn T.M., Shortle D.;
RT "Null alleles of SAC7 suppress temperature-sensitive actin mutations in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 10:2308-2314(1990).
RN [4]
RP FUNCTION.
RX PubMed=9038344; DOI=10.1016/s0092-8674(00)81893-0;
RA Schmidt A., Bickle M., Beck T., Hall M.N.;
RT "The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2
RT via the exchange factor ROM2.";
RL Cell 88:531-542(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-491, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-491 AND SER-632, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-435; SER-491 AND
RP SER-632, AND IDENTIFICATION BY 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: GTPase-activating protein for RHO1. Must be involved in the
CC normal assembly or function or both of actin. Plays an essential role
CC only at low temperatures. {ECO:0000269|PubMed:9038344}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35016.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U32274; AAB64831.1; -; Genomic_DNA.
DR EMBL; M32335; AAA35016.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006938; DAA12233.1; -; Genomic_DNA.
DR PIR; S69673; S69673.
DR RefSeq; NP_010677.1; NM_001180697.1.
DR AlphaFoldDB; P17121; -.
DR SMR; P17121; -.
DR BioGRID; 32450; 526.
DR DIP; DIP-1010N; -.
DR IntAct; P17121; 2.
DR MINT; P17121; -.
DR STRING; 4932.YDR389W; -.
DR iPTMnet; P17121; -.
DR MaxQB; P17121; -.
DR PaxDb; 4932-YDR389W; -.
DR PeptideAtlas; P17121; -.
DR EnsemblFungi; YDR389W_mRNA; YDR389W; YDR389W.
DR GeneID; 851997; -.
DR KEGG; sce:YDR389W; -.
DR AGR; SGD:S000002797; -.
DR SGD; S000002797; SAC7.
DR VEuPathDB; FungiDB:YDR389W; -.
DR eggNOG; KOG2710; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_016108_0_0_1; -.
DR InParanoid; P17121; -.
DR OMA; NNPKSMS; -.
DR OrthoDB; 25175at2759; -.
DR BioCyc; YEAST:G3O-29937-MONOMER; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR Reactome; R-SCE-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 851997; 2 hits in 10 CRISPR screens.
DR PRO; PR:P17121; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P17121; Protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IMP:SGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:SGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04396; RhoGAP_fSAC7_BAG7; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR PANTHER; PTHR15228:SF25; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00620; RhoGAP; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..654
FT /note="GTPase-activating protein SAC7"
FT /id="PRO_0000056764"
FT DOMAIN 134..393
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 654 AA; 73629 MW; 50FD33872D13BBFD CRC64;
MPNNTLKQGS KIENVSPSKG HVPSFWKQFI NNPKSMSSEN ITVPRSPTSL SRNAQPTTLK
RPPLSSRPYS YNTPTKDRKS FSKSAKQNNN NNNANSGTSP HAEFKNYRDM FLSNRNGFTG
RVFGVTLAES LSVASAEVIV QSELVSFGRI PIVVAKCGAY LKANGLETSG IFRIAGNGKR
VKALQYIFSS PPDYGTKFND WETYTVHDVA SLLRRYLNNL AEPLIPLSLY EQFRNPLRSR
PRILRHMLTH EVSHPNANKT NNVTVKSSRQ NYNDDGANDG DIEKEDAKDD EEKRRRKIRH
KRRLTRDIRA AIKEYEELFV TLSNDTKQLT IYLLDLLSLF ARQSQFNLMS GRNLAAIFQP
SILSHPQHDM DPKEYELSRL VVEFLIEYSY KLLPHLLKLA KREQQERLST ENKKNNGDKQ
KTDPIEIPKI TSSDSPPIVS SNKNPPAIDN NNKLDHTTLS PISTSIPENS SDLQTSKMLK
PPKQRRPHSK SFGSTPVPPD VIASNKRRTS LFPWLHKPGI LSDTGDNGDL TATEAEGDDY
EEENVDPYGQ SPSSVHSGSL PKQHYLPIPR MNRSLSGNST NSSFNTRPIS MILTSGNDNS
ADQLELLSNT HSNNERSNAL PLTEDDGDER NSRSRKRESW FQRLTSRSGS ANRA
//
