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Metal resistance protein YCF1 (Yeast cadmium factor 1)

 YCFI_YEAST              Reviewed;        1515 AA.
P39109; D6VSB9; Q03905;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
12-SEP-2018, entry version 192.
RecName: Full=Metal resistance protein YCF1;
AltName: Full=Yeast cadmium factor 1;
Name=YCF1; OrderedLocusNames=YDR135C; ORFNames=YD9302.11C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=H9;
PubMed=7521334;
Szczypka M.S., Wemmie J.A., Moye-Rowley S.W., Thiele D.J.;
"A yeast metal resistance protein similar to human cystic fibrosis
transmembrane conductance regulator (CFTR) and multidrug resistance-
associated protein.";
J. Biol. Chem. 269:22853-22857(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8626454; DOI=10.1074/jbc.271.11.6509;
Li Z.S., Szczypka M., Lu Y.P., Thiele D.J., Rea P.A.;
"The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-
conjugate pump.";
J. Biol. Chem. 271:6509-6517(1996).
[5]
FUNCTION.
PubMed=10790694;
DOI=10.1002/(SICI)1097-0061(200004)16:6<561::AID-YEA551>3.0.CO;2-L;
Petrovic S., Pascolo L., Gallo R., Cupelli F., Ostrow J.D.,
Goffeau A., Tiribelli C., Bruschi C.V.;
"The products of YCF1 and YLL015w (BPT1) cooperate for the ATP-
dependent vacuolar transport of unconjugated bilirubin in
Saccharomyces cerevisiae.";
Yeast 16:561-571(2000).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903; SER-908 AND
THR-911, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND SER-914, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-873; SER-903
AND SER-908, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Cooperates for the ATP-dependent vacuolar transport of
bilirubin and glutathione conjugates.
{ECO:0000269|PubMed:10790694, ECO:0000269|PubMed:8626454}.
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:8626454}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00441,
ECO:0000269|PubMed:8626454}.
-!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
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EMBL; L35237; AAA50353.1; -; Genomic_DNA.
EMBL; Z48179; CAA88217.1; -; Genomic_DNA.
EMBL; BK006938; DAA11979.1; -; Genomic_DNA.
PIR; S51863; S51863.
RefSeq; NP_010419.3; NM_001180442.3.
ProteinModelPortal; P39109; -.
SMR; P39109; -.
BioGrid; 32190; 104.
DIP; DIP-2612N; -.
IntAct; P39109; 4.
MINT; P39109; -.
STRING; 4932.YDR135C; -.
TCDB; 3.A.1.208.11; the atp-binding cassette (abc) superfamily.
iPTMnet; P39109; -.
MaxQB; P39109; -.
PaxDb; P39109; -.
PRIDE; P39109; -.
EnsemblFungi; YDR135C; YDR135C; YDR135C.
GeneID; 851713; -.
KEGG; sce:YDR135C; -.
EuPathDB; FungiDB:YDR135C; -.
SGD; S000002542; YCF1.
GeneTree; ENSGT00880000137856; -.
InParanoid; P39109; -.
OMA; ENEWRVD; -.
OrthoDB; EOG092C0QQU; -.
BioCyc; MetaCyc:G3O-29733-MONOMER; -.
BioCyc; YEAST:G3O-29733-MONOMER; -.
Reactome; R-SCE-114608; Platelet degranulation.
Reactome; R-SCE-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
Reactome; R-SCE-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-SCE-2142850; Hyaluronan biosynthesis and export.
Reactome; R-SCE-382556; ABC-family proteins mediated transport.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
PRO; PR:P39109; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0015127; F:bilirubin transmembrane transporter activity; IMP:SGD.
GO; GO:0015431; F:glutathione S-conjugate-exporting ATPase activity; IDA:SGD.
GO; GO:0015723; P:bilirubin transport; IMP:SGD.
GO; GO:0045454; P:cell redox homeostasis; IMP:SGD.
GO; GO:0006749; P:glutathione metabolic process; IGI:SGD.
GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
GO; GO:0010038; P:response to metal ion; IDA:SGD.
GO; GO:0055085; P:transmembrane transport; IMP:SGD.
GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Cadmium resistance; Complete proteome; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport; Vacuole.
CHAIN 1 1515 Metal resistance protein YCF1.
/FTId=PRO_0000093449.
TOPO_DOM 1 32 Vacuolar. {ECO:0000255}.
TRANSMEM 33 53 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 54 73 Cytoplasmic. {ECO:0000255}.
TRANSMEM 74 94 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 95 99 Vacuolar. {ECO:0000255}.
TRANSMEM 100 120 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 121 130 Cytoplasmic. {ECO:0000255}.
TRANSMEM 131 151 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 152 169 Vacuolar. {ECO:0000255}.
TRANSMEM 170 190 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 191 278 Cytoplasmic. {ECO:0000255}.
TRANSMEM 279 299 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 300 345 Vacuolar. {ECO:0000255}.
TRANSMEM 346 366 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 367 422 Cytoplasmic. {ECO:0000255}.
TRANSMEM 423 443 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 444 446 Vacuolar. {ECO:0000255}.
TRANSMEM 447 467 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 468 530 Cytoplasmic. {ECO:0000255}.
TRANSMEM 531 551 Helical; Name=10. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 552 572 Vacuolar. {ECO:0000255}.
TRANSMEM 573 593 Helical; Name=11. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 594 943 Cytoplasmic. {ECO:0000255}.
TRANSMEM 944 964 Helical; Name=12. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 965 1001 Vacuolar. {ECO:0000255}.
TRANSMEM 1002 1023 Helical; Name=13. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1024 1066 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1067 1087 Helical; Name=14. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1088 1088 Vacuolar. {ECO:0000255}.
TRANSMEM 1089 1109 Helical; Name=15. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1110 1180 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1181 1201 Helical; Name=16. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1202 1205 Vacuolar. {ECO:0000255}.
TRANSMEM 1206 1226 Helical; Name=17. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1227 1515 Cytoplasmic. {ECO:0000255}.
DOMAIN 287 590 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 626 853 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 951 1235 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1272 1507 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 663 670 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1306 1313 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 903 903 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 908 908 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 911 911 Phosphothreonine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 914 914 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 713 713 Missing: Loss of function.
MUTAGEN 908 908 S->A: Loss of function.
CONFLICT 680 680 L -> R (in Ref. 1; AAA50353).
{ECO:0000305}.
SEQUENCE 1515 AA; 171121 MW; 30F92FDDBAF60431 CRC64;
MAGNLVSWAC KLCRSPEGFG PISFYGDFTQ CFIDGVILNL SAIFMITFGI RDLVNLCKKK
HSGIKYRRNW IIVSRMALVL LEIAFVSLAS LNISKEEAEN FTIVSQYAST MLSLFVALAL
HWIEYDRSVV ANTVLLFYWL FETFGNFAKL INILIRHTYE GIWYSGQTGF ILTLFQVITC
ASILLLEALP KKPLMPHQHI HQTLTRRKPN PYDSANIFSR ITFSWMSGLM KTGYEKYLVE
ADLYKLPRNF SSEELSQKLE KNWENELKQK SNPSLSWAIC RTFGSKMLLA AFFKAIHDVL
AFTQPQLLRI LIKFVTDYNS ERQDDHSSLQ GFENNHPQKL PIVRGFLIAF AMFLVGFTQT
SVLHQYFLNV FNTGMYIKSA LTALIYQKSL VLSNEASGLS STGDIVNLMS VDVQKLQDLT
QWLNLIWSGP FQIIICLYSL YKLLGNSMWV GVIILVIMMP LNSFLMRIQK KLQKSQMKYK
DERTRVISEI LNNIKSLKLY AWEKPYREKL EEVRNNKELK NLTKLGCYMA VTSFQFNIVP
FLVSCCTFAV FVYTEDRALT TDLVFPALTL FNLLSFPLMI IPMVLNSFIE ASVSIGRLFT
FFTNEELQPD SVQRLPKVKN IGDVAINIGD DATFLWQRKP EYKVALKNIN FQAKKGNLTC
IVGKVGSGKT ALLSCMLGDL FRVKGFATVH GSVAYVSQVP WIMNGTVKEN ILFGHRYDAE
FYEKTIKACA LTIDLAILMD GDKTLVGEKG ISLSGGQKAR LSLARAVYAR ADTYLLDDPL
AAVDEHVARH LIEHVLGPNG LLHTKTKVLA TNKVSALSIA DSIALLDNGE ITQQGTYDEI
TKDADSPLWK LLNNYGKKNN GKSNEFGDSS ESSVRESSIP VEGELEQLQK LNDLDFGNSD
AISLRRASDA TLGSIDFGDD ENIAKREHRE QGKVKWNIYL EYAKACNPKS VCVFILFIVI
SMFLSVMGNV WLKHWSEVNS RYGSNPNAAR YLAIYFALGI GSALATLIQT IVLWVFCTIH
ASKYLHNLMT NSVLRAPMTF FETTPIGRIL NRFSNDIYKV DALLGRTFSQ FFVNAVKVTF
TITVICATTW QFIFIIIPLS VFYIYYQQYY LRTSRELRRL DSITRSPIYS HFQETLGGLA
TVRGYSQQKR FSHINQCRID NNMSAFYPSI NANRWLAYRL ELIGSIIILG AATLSVFRLK
QGTLTAGMVG LSLSYALQIT QTLNWIVRMT VEVETNIVSV ERIKEYADLK SEAPLIVEGH
RPPKEWPSQG DIKFNNYSTR YRPELDLVLK HINIHIKPNE KVGIVGRTGA GKSSLTLALF
RMIEASEGNI VIDNIAINEI GLYDLRHKLS IIPQDSQVFE GTVRENIDPI NQYTDEAIWR
ALELSHLKEH VLSMSNDGLD AQLTEGGGNL SVGQRQLLCL ARAMLVPSKI LVLDEATAAV
DVETDKVVQE TIRTAFKDRT ILTIAHRLNT IMDSDRIIVL DNGKVAEFDS PGQLLSDNKS
LFYSLCMEAG LVNEN


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