MSB4_YEAST
ID MSB4_YEAST Reviewed; 492 AA.
AC Q12317; D6W1V5; Q05377; Q05378;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=GTPase-activating protein MSB4;
DE AltName: Full=Multicopy suppressor of bud emergence 4;
GN Name=MSB4; OrderedLocusNames=YOL112W; ORFNames=HRC492;
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 [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10679030; DOI=10.1091/mbc.11.2.773;
RA Bi E., Chiavetta J.B., Chen H., Chen G.-C., Chan C.S.M., Pringle J.R.;
RT "Identification of novel, evolutionarily conserved Cdc42p-interacting
RT proteins and of redundant pathways linking Cdc24p and Cdc42p to actin
RT polarization in yeast.";
RL Mol. Biol. Cell 11:773-793(2000).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ARG-200.
RX PubMed=12913108; DOI=10.1083/jcb.200302038;
RA Gao X.D., Albert S., Tcheperegine S.E., Burd C.G., Gallwitz D., Bi E.;
RT "The GAP activity of Msb3p and Msb4p for the Rab GTPase Sec4p is required
RT for efficient exocytosis and actin organization.";
RL J. Cell Biol. 162:635-646(2003).
RN [6]
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).
CC -!- FUNCTION: Regulates exocytosis by functioning as a GAP for SEC4. Also
CC required for efficient polarization of the actin patches.
CC {ECO:0000269|PubMed:10679030, ECO:0000269|PubMed:12913108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10679030}. Bud
CC {ECO:0000269|PubMed:10679030}. Bud neck {ECO:0000269|PubMed:10679030}.
CC Note=Localizes to the presumptive bud site, the bud tip and the mother-
CC bud neck.
CC -!- MISCELLANEOUS: Present with 1730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA88150.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z48149; CAA88149.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z48149; CAA88150.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z48149; CAA88148.1; -; Genomic_DNA.
DR EMBL; Z74854; CAA99131.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10671.1; -; Genomic_DNA.
DR PIR; S51885; S51885.
DR RefSeq; NP_014529.1; NM_001183366.1.
DR AlphaFoldDB; Q12317; -.
DR SMR; Q12317; -.
DR BioGRID; 34288; 217.
DR ComplexPortal; CPX-3188; Polarisome.
DR DIP; DIP-2784N; -.
DR IntAct; Q12317; 1.
DR MINT; Q12317; -.
DR STRING; 4932.YOL112W; -.
DR MaxQB; Q12317; -.
DR PaxDb; Q12317; -.
DR PRIDE; Q12317; -.
DR EnsemblFungi; YOL112W_mRNA; YOL112W; YOL112W.
DR GeneID; 854037; -.
DR KEGG; sce:YOL112W; -.
DR SGD; S000005472; MSB4.
DR VEuPathDB; FungiDB:YOL112W; -.
DR eggNOG; KOG2058; Eukaryota.
DR GeneTree; ENSGT00940000176552; -.
DR HOGENOM; CLU_005350_12_1_1; -.
DR InParanoid; Q12317; -.
DR OMA; PDNIHFH; -.
DR BioCyc; YEAST:G3O-33509-MON; -.
DR PRO; PR:Q12317; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12317; protein.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0000133; C:polarisome; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IC:ComplexPortal.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IC:ComplexPortal.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IGI:SGD.
DR GO; GO:0006903; P:vesicle targeting; IC:ComplexPortal.
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 Cytoplasm; GTPase activation; Reference proteome.
FT CHAIN 1..492
FT /note="GTPase-activating protein MSB4"
FT /id="PRO_0000208020"
FT DOMAIN 147..367
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT MUTAGEN 200
FT /note="R->F: Reduced GAP activity."
FT /evidence="ECO:0000269|PubMed:12913108"
FT MUTAGEN 200
FT /note="R->K: Reduced GAP activity."
FT /evidence="ECO:0000269|PubMed:12913108"
SQ SEQUENCE 492 AA; 57093 MW; C8411DBB56003929 CRC64;
MIMSSTMSTE AALVPNESVF DTVSSFNEDD ANYSVLDLYD DDDEGDDSST VERKEILTTR
ELEKAKAFTS LIMADPENFD RYGFSKKGYF ISQEEYDKWW TEYNRYTERR KKKWENFLLK
NKIELHNDNP LVYPARTDEL SKFVRKGIPA EWRGNAWWYF AGGQRQLDAN VGVYDRLKSD
CREGAVSGKD MEAIERDLYR TFPDNIHFHK ESFQNGEPAI IRSLRRVLMA FSVYDKTIGY
CQSMNFLVGL LLLFMEEEKA FWMLVIITGK YLPGVYESDL EGANVDQGVL VLCIKEYLPE
IWSHIESSYM NGNGSTDQIS GPASGEEYLC RLPTLTLCTA SWFMSCFVGV VPIETTLRIW
DCLFYEESHF LFKVALGILK LSESEFLESK SQKLFRQYSS YTFGGSNDSD STFKRLKNKI
KTQEEADMEI LQVIQNFPKR LLNPNDIFEK VLMKKKVALN GITQEKIDRG REYVAMARNR
QRASSRPKER RK
