SLA2_YEAST
ID SLA2_YEAST Reviewed; 968 AA.
AC P33338; D6W0V0; Q02434;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 5.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Protein SLA2;
DE AltName: Full=Transmembrane protein MOP2;
GN Name=SLA2; Synonyms=END4, MOP2, UFG1; OrderedLocusNames=YNL243W;
GN ORFNames=N1102;
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].
RC STRAIN=DDY 228;
RX PubMed=8335689; DOI=10.1083/jcb.122.3.635;
RA Holtzman D.A., Yang S., Drubin D.G.;
RT "Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2,
RT that control membrane cytoskeleton assembly in Saccharomyces cerevisiae.";
RL J. Cell Biol. 122:635-644(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7896828; DOI=10.1074/jbc.270.12.6815;
RA Na S., Hincapie M., McCusker J.H., Haber J.E.;
RT "MOP2 (SLA2) affects the abundance of the plasma membrane H(+)-ATPase of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:6815-6823(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 344.
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 [5]
RP NUCLEOTIDE SEQUENCE OF 327-968.
RC STRAIN=117-8A;
RA Yoon H., Donahue T.F.;
RT "DNA sequence of ufg1 gene in yeast.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 820-968.
RX PubMed=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294 AND SER-308, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-298 AND SER-308, AND
RP 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: Required for cellular morphogenesis and polarization of the
CC cortical cytoskeleton. It might act in concert with proteins such as
CC CDC42 and CDC43 to limit the region of cortical patch formation to the
CC cortex of the bud. Required for the accumulation and/or maintenance of
CC plasma membrane H(+)-ATPase on the cell surface.
CC -!- INTERACTION:
CC P33338; Q12518: ENT1; NbExp=2; IntAct=EBI-17323, EBI-31494;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00243}. Cytoplasm,
CC cytoskeleton, actin patch. Cytoplasm, cell cortex. Bud tip.
CC -!- MISCELLANEOUS: Present with 40600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SLA2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA19161.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z22811; CAA80464.1; -; Genomic_DNA.
DR EMBL; L12352; AAA74726.1; -; Genomic_DNA.
DR EMBL; Z71519; CAA96149.1; -; Genomic_DNA.
DR EMBL; Z71518; CAA96148.1; -; Genomic_DNA.
DR EMBL; U07938; AAA19161.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; Z69381; CAA93355.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10316.2; -; Genomic_DNA.
DR PIR; S63211; S63211.
DR RefSeq; NP_014156.2; NM_001183081.2.
DR PDB; 5AHV; EM; 13.60 A; F=5-272.
DR PDB; 7B2L; EM; 3.90 A; B/D/G/I/L/N/Q/S=1-286.
DR PDBsum; 5AHV; -.
DR PDBsum; 7B2L; -.
DR AlphaFoldDB; P33338; -.
DR SMR; P33338; -.
DR BioGRID; 35596; 933.
DR DIP; DIP-973N; -.
DR IntAct; P33338; 27.
DR MINT; P33338; -.
DR STRING; 4932.YNL243W; -.
DR iPTMnet; P33338; -.
DR MaxQB; P33338; -.
DR PaxDb; P33338; -.
DR PRIDE; P33338; -.
DR EnsemblFungi; YNL243W_mRNA; YNL243W; YNL243W.
DR GeneID; 855478; -.
DR KEGG; sce:YNL243W; -.
DR SGD; S000005187; SLA2.
DR VEuPathDB; FungiDB:YNL243W; -.
DR eggNOG; KOG0980; Eukaryota.
DR GeneTree; ENSGT00940000153594; -.
DR HOGENOM; CLU_004601_0_0_1; -.
DR InParanoid; P33338; -.
DR OMA; IREYVYF; -.
DR BioCyc; YEAST:G3O-33240-MON; -.
DR PRO; PR:P33338; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P33338; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
DR GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; TAS:SGD.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; TAS:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; TAS:SGD.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; PTHR10407; 2.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109885; SSF109885; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..968
FT /note="Protein SLA2"
FT /id="PRO_0000071945"
FT TRANSMEM 772..791
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 1..127
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 717..965
FT /note="I/LWEQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT REGION 280..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 294
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 52
FT /note="P -> A (in Ref. 2; AAA74726)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> R (in Ref. 3; CAA96148/CAA96149)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="A -> R (in Ref. 5; AAA19161)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="S -> C (in Ref. 5; AAA19161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 968 AA; 108911 MW; E592E09D8040C0E9 CRC64;
MSRIDSDLQK ALKKACSVEE TAPKRKHVRA CIVYTWDHQS SKAVFTTLKT LPLANDEVQL
FKMLIVLHKI IQEGHPSALA EAIRDRDWIR SLGRVHSGGS SYSKLIREYV RYLVLKLDFH
AHHRGFNNGT FEYEEYVSLV SVSDPDEGYE TILDLMSLQD SLDEFSQIIF ASIQSERRNT
ECKISALIPL IAESYGIYKF ITSMLRAMHR QLNDAEGDAA LQPLKERYEL QHARLFEFYA
DCSSVKYLTT LVTIPKLPVD APDVFLINDV DESKEIKFKK REPSVTPART PARTPTPTPP
VVAEPAISPR PVSQRTTSTP TGYLQTMPTG ATTGMMIPTA TGAANAIFPQ ATAQMQPDFW
ANQQAQFANE QNRLEQERVQ QLQQQQAQQE LFQQQLQKAQ QDMMNMQLQQ QNQHQNDLIA
LTNQYEKDQA LLQQYDQRVQ QLESEITTMD STASKQLANK DEQLTALQDQ LDVWERKYES
LAKLYSQLRQ EHLNLLPRFK KLQLKVNSAQ ESIQKKEQLE HKLKQKDLQM AELVKDRDRA
RLELERSINN AEADSAAATA AAETMTQDKM NPILDAILES GINTIQESVY NLDSPLSWSG
PLTPPTFLLS LLESTSENAT EFATSFNNLI VDGLAHGDQT EVIHCVSDFS TSMATLVTNS
KAYAVTTLPQ EQSDQILTLV KRCAREAQYF FEDLMSENLN QVGDEEKTDI VINANVDMQE
KLQELSLAIE PLLNIQSVKS NKETNPHSEL VATADKIVKS SEHLRVDVPK PLLSLALMII
DAVVALVKAA IQCQNEIATT TSIPLNQFYL KNSRWTEGLI SAAKAVAGAT NVLITTASKL
ITSEDNENTS PEQFIVASKE VAASTIQLVA ASRVKTSIHS KAQDKLEHCS KDVTDACRSL
GNHVMGMIED DHSTSQQQQP LDFTSEHTLK TAEMEQQVEI LKLEQSLSNA RKRLGEIRRH
AYYNQDDD
