COT1_YEAST
ID COT1_YEAST Reviewed; 439 AA.
AC P32798; D6W314;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cobalt uptake protein COT1;
GN Name=COT1; OrderedLocusNames=YOR316C; ORFNames=O6131;
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=1508175; DOI=10.1128/mcb.12.9.3678-3688.1992;
RA Conklin D.S., McMaster J.A., Culbertson M.R., Kung C.;
RT "COT1, a gene involved in cobalt accumulation in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 12:3678-3688(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896266;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA Schweizer M.;
RT "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT XV reveals regions of similarity to chromosomes I and XIII.";
RL Yeast 12:1021-1031(1996).
RN [3]
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 [4]
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 [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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-301, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, 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 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: Probably responsible for the uptake of cobalt ions. It
CC appears to act in a dosage-dependent manner to counteract the adverse
CC effects of cobalt ions on cells. It may participate in the regulation
CC of cobalt levels under normal physiological conditions and may be
CC important in the supply of metal that is required for metalloenzyme or
CC cofactor synthesis. It reduces the toxicity of cobalt and rhodium ions.
CC Other components responsible for cobalt transport exist.
CC -!- INTERACTION:
CC P32798; P38310: FTH1; NbExp=3; IntAct=EBI-5006, EBI-20959;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC protein. Note=Another possibility exists that it is associated with
CC another unidentified membrane that has been enriched in the
CC mitochondrial membrane fractions.
CC -!- MISCELLANEOUS: Present with 2070 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}.
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DR EMBL; M88252; AAA74884.1; -; Genomic_DNA.
DR EMBL; X90565; CAA62171.1; -; Genomic_DNA.
DR EMBL; Z75224; CAA99636.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11080.1; -; Genomic_DNA.
DR PIR; S58327; S58327.
DR RefSeq; NP_014961.3; NM_001183736.3.
DR AlphaFoldDB; P32798; -.
DR SMR; P32798; -.
DR BioGRID; 34703; 43.
DR DIP; DIP-7554N; -.
DR IntAct; P32798; 15.
DR MINT; P32798; -.
DR STRING; 4932.YOR316C; -.
DR TCDB; 2.A.4.2.1; the cation diffusion facilitator (cdf) family.
DR iPTMnet; P32798; -.
DR MaxQB; P32798; -.
DR PaxDb; P32798; -.
DR PRIDE; P32798; -.
DR TopDownProteomics; P32798; -.
DR EnsemblFungi; YOR316C_mRNA; YOR316C; YOR316C.
DR GeneID; 854494; -.
DR KEGG; sce:YOR316C; -.
DR SGD; S000005843; COT1.
DR VEuPathDB; FungiDB:YOR316C; -.
DR eggNOG; KOG1483; Eukaryota.
DR GeneTree; ENSGT00940000172026; -.
DR HOGENOM; CLU_013430_4_3_1; -.
DR InParanoid; P32798; -.
DR OMA; IFHHAGI; -.
DR BioCyc; YEAST:G3O-33798-MON; -.
DR Reactome; R-SCE-425410; Metal ion SLC transporters.
DR PRO; PR:P32798; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32798; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IGI:SGD.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:SGD.
DR GO; GO:0006824; P:cobalt ion transport; IMP:SGD.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006829; P:zinc ion transport; IGI:SGD.
DR Gene3D; 1.20.1510.10; -; 2.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Cobalt; Isopeptide bond; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..439
FT /note="Cobalt uptake protein COT1"
FT /id="PRO_0000206102"
FT TRANSMEM 10..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 207..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:14557538"
FT CONFLICT 227
FT /note="G -> E (in Ref. 1; AAA74884)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..334
FT /note="HI -> RV (in Ref. 1; AAA74884)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="I -> V (in Ref. 1; AAA74884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48155 MW; AC88AAA5F2EE4AED CRC64;
MKLGSKQVKI ISLLLLDTVF FGIEITTGYL SHSLALIADS FHMLNDIISL VVALWAVNVA
KNRNPDSTYT YGWKRAEILG ALINAVFLIA LCVSILIEAL QRIIAPPVIE NPKFVLYVGV
AGLISNTVGL FLFHDNDQEH GHGHGHSHGG IFADHEMHMP SSHTHTHAHV DGIENTTPMD
STDNISEIMP NAIVDSFMNE NTRLLTPENA SKTPSYSTSS HTIASGGNYT EHNKRKRSLN
MHGVFLHVLG DALGNIGVML SAFFIWKTDY SWKYYTDPLV SLIITGIIFS SALPLSCKAS
KILLQATPST LSGDQVEGDL LKIPGIIAIH DFHIWNLTES IFIASLHIQL DISPEQFTDL
AKIVRSKLHR YGIHSATLQP EFITREVTST ERAGDSQGDH LQNDPLSLRP KTYGTGISGS
TCLIDDAANC NTADCLEDH
