MSC2_YEAST
ID MSC2_YEAST Reviewed; 724 AA.
AC Q03455; D6VSI6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Probable zinc transporter MSC2;
DE AltName: Full=Meiotic sister chromatid recombination protein 2;
GN Name=MSC2; OrderedLocusNames=YDR205W; ORFNames=YD8142.02;
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 MUTANT ANALYSIS.
RX PubMed=10511544; DOI=10.1093/genetics/153.2.621;
RA Thompson D.A., Stahl F.W.;
RT "Genetic control of recombination partner preference in yeast meiosis.
RT Isolation and characterization of mutants elevated for meiotic unequal
RT sister-chromatid recombination.";
RL Genetics 153:621-641(1999).
RN [4]
RP ERRATUM OF PUBMED:10511544.
RA Thompson D.A., Stahl F.W.;
RL Genetics 164:1241-1241(2003).
RN [5]
RP FUNCTION.
RX PubMed=11058603; DOI=10.1074/jbc.m008969200;
RA Li L., Kaplan J.;
RT "The yeast gene MSC2, a member of the cation diffusion facilitator family,
RT affects the cellular distribution of zinc.";
RL J. Biol. Chem. 276:5036-5043(2001).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Probably act as a zinc ion transporter moving zinc from the
CC nucleus/endoplasmic reticulum to the cytoplasm. Involved in zinc ion
CC homeostasis and cellular distribution. {ECO:0000269|PubMed:11058603}.
CC -!- INTERACTION:
CC Q03455; P53735: ZRG17; NbExp=3; IntAct=EBI-34990, EBI-28507;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}. Nucleus membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Originally MSC2 was identified in a screen for mutants
CC that show an increase in meiotic unequal sister-chromatid recombination
CC (SCR). MSC2 may also be involved in chromosome instability, rather than
CC SRC.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA92344.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z68194; CAA92344.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA12046.1; -; Genomic_DNA.
DR PIR; S61568; S61568.
DR RefSeq; NP_010491.4; NM_001180513.3.
DR AlphaFoldDB; Q03455; -.
DR SMR; Q03455; -.
DR BioGRID; 32255; 92.
DR DIP; DIP-5209N; -.
DR IntAct; Q03455; 2.
DR MINT; Q03455; -.
DR STRING; 4932.YDR205W; -.
DR TCDB; 2.A.4.4.1; the cation diffusion facilitator (cdf) family.
DR MaxQB; Q03455; -.
DR PaxDb; Q03455; -.
DR PRIDE; Q03455; -.
DR EnsemblFungi; YDR205W_mRNA; YDR205W; YDR205W.
DR GeneID; 851786; -.
DR KEGG; sce:YDR205W; -.
DR SGD; S000002613; MSC2.
DR VEuPathDB; FungiDB:YDR205W; -.
DR eggNOG; KOG1484; Eukaryota.
DR GeneTree; ENSGT00940000159571; -.
DR HOGENOM; CLU_013430_11_1_1; -.
DR InParanoid; Q03455; -.
DR OMA; RIFNPIH; -.
DR BioCyc; YEAST:G3O-29789-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR Reactome; R-SCE-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR PRO; PR:Q03455; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03455; protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:SGD.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR GO; GO:1904257; P:zinc ion import into Golgi apparatus; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; IMP:SGD.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR045316; Msc2-like.
DR PANTHER; PTHR45755; PTHR45755; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Ion transport; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..724
FT /note="Probable zinc transporter MSC2"
FT /id="PRO_0000206115"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..58
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..134
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..219
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..298
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..417
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..491
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..563
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 614..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 80578 MW; 05463664C1CA89E7 CRC64;
MNLQELLAKV PLLLSYPTII LSSNLIVPSH NDLISRAAST SAAEYADEKL IFFSTDHAIR
LIFLPTFVAS SFNLFAHYFN FINYSSRRKY YVLFTAIYFL SILTAIFHPI QSTCITLLII
KLLTTADESS PKIALNFKTI LKTFVPFITL TLVILRWDPS FDASSGDVNK ISTSLAAYAL
LILTLRYASP LILSTLSSSI GVVSKDTSVA QHSISRNKRF PLILVLPIFS FVLLYLMTIV
NKTYNIQLLM VFVFFGCLSI FFLSLKDLFT EDGNQKKGGQ EDEYCRMFDI KYMISYLWLT
RFTILLTGIM AIVVHFLSFN EITSSIKTDL LSLLFVVVAE YVSSFSNKQP DSHSHNHAHH
HSHLTDSLPL ENESMFKQMA LNKDTRSIFS FLLLNTAFMF VQLLYSFRSK SLGLLSDSLH
MALDCTSLLL GLIAGVLTKK PASDKFPFGL NYLGTLAGFT NGVLLLGIVC GIFVEAIERI
FNPIHLHATN ELLVVATLGL LVNLVGLFAF DHGAHDHGGT DNENMKGIFL HILADTLGSV
GVVISTLLIK LTHWPIFDPI ASLLIGSLIL LSALPLLKST SANILLRLDD KKHNLVKSAL
NQISTTPGIT GYTTPRFWPT ESGSSGHSHA HTHSHAENHS HEHHHDQKNG SQEHPSLVGY
IHVQYVDGEN STIIKKRVEK IFENVSIKAW VQVEPQNSTC WCRATSMNTI SANPNSLPLQ
PIAN
