YCFI_YEAST
ID YCFI_YEAST Reviewed; 1515 AA.
AC P39109; D6VSB9; Q03905;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Metal resistance protein YCF1;
DE AltName: Full=ABC-type Cd(2+) transporter;
DE EC=7.2.2.2 {ECO:0000269|PubMed:8626454};
DE AltName: Full=ABC-type glutathione-S-conjugate transporter;
DE EC=7.6.2.3 {ECO:0000269|PubMed:8626454};
DE AltName: Full=Yeast cadmium factor 1;
GN Name=YCF1; OrderedLocusNames=YDR135C; ORFNames=YD9302.11C;
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=H9;
RX PubMed=7521334; DOI=10.1016/s0021-9258(17)31723-4;
RA Szczypka M.S., Wemmie J.A., Moye-Rowley S.W., Thiele D.J.;
RT "A yeast metal resistance protein similar to human cystic fibrosis
RT transmembrane conductance regulator (CFTR) and multidrug resistance-
RT associated protein.";
RL J. Biol. Chem. 269:22853-22857(1994).
RN [2]
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 [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, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8626454; DOI=10.1074/jbc.271.11.6509;
RA Li Z.S., Szczypka M., Lu Y.P., Thiele D.J., Rea P.A.;
RT "The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-
RT conjugate pump.";
RL J. Biol. Chem. 271:6509-6517(1996).
RN [5]
RP FUNCTION.
RX PubMed=10790694;
RX DOI=10.1002/(sici)1097-0061(200004)16:6<561::aid-yea551>3.0.co;2-l;
RA Petrovic S., Pascolo L., Gallo R., Cupelli F., Ostrow J.D., Goffeau A.,
RA Tiribelli C., Bruschi C.V.;
RT "The products of YCF1 and YLL015w (BPT1) cooperate for the ATP-dependent
RT vacuolar transport of unconjugated bilirubin in Saccharomyces cerevisiae.";
RL Yeast 16:561-571(2000).
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903; SER-908 AND THR-911, 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 [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND SER-914, AND
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-873; SER-903 AND
RP SER-908, AND 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: Cooperates for the ATP-dependent vacuolar transport of
CC bilirubin and glutathione conjugates. {ECO:0000269|PubMed:10790694,
CC ECO:0000269|PubMed:8626454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.2;
CC Evidence={ECO:0000269|PubMed:8626454};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000269|PubMed:8626454};
CC -!- INTERACTION:
CC P39109; P00330: ADH1; NbExp=2; IntAct=EBI-21779, EBI-2218;
CC P39109; Q03048: COF1; NbExp=2; IntAct=EBI-21779, EBI-4853;
CC P39109; P01120: RAS2; NbExp=2; IntAct=EBI-21779, EBI-14838;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:8626454};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:8626454}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L35237; AAA50353.1; -; Genomic_DNA.
DR EMBL; Z48179; CAA88217.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11979.1; -; Genomic_DNA.
DR PIR; S51863; S51863.
DR RefSeq; NP_010419.3; NM_001180442.3.
DR PDB; 7M68; EM; 4.04 A; A=1-1515.
DR PDB; 7M69; EM; 3.42 A; A=1-1515.
DR PDB; 7MPE; EM; 3.20 A; A=1-1515.
DR PDBsum; 7M68; -.
DR PDBsum; 7M69; -.
DR PDBsum; 7MPE; -.
DR AlphaFoldDB; P39109; -.
DR SMR; P39109; -.
DR BioGRID; 32190; 115.
DR DIP; DIP-2612N; -.
DR IntAct; P39109; 33.
DR MINT; P39109; -.
DR STRING; 4932.YDR135C; -.
DR TCDB; 3.A.1.208.11; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P39109; -.
DR MaxQB; P39109; -.
DR PaxDb; P39109; -.
DR PRIDE; P39109; -.
DR EnsemblFungi; YDR135C_mRNA; YDR135C; YDR135C.
DR GeneID; 851713; -.
DR KEGG; sce:YDR135C; -.
DR SGD; S000002542; YCF1.
DR VEuPathDB; FungiDB:YDR135C; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000166156; -.
DR HOGENOM; CLU_000604_27_3_1; -.
DR InParanoid; P39109; -.
DR OMA; IRYDFTP; -.
DR BioCyc; MetaCyc:G3O-29733-MON; -.
DR BioCyc; YEAST:G3O-29733-MON; -.
DR BRENDA; 7.2.2.2; 984.
DR BRENDA; 7.6.2.3; 984.
DR Reactome; R-SCE-189483; Heme degradation.
DR Reactome; R-SCE-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-9707564; Cytoprotection by HMOX1.
DR Reactome; R-SCE-9749641; Aspirin ADME.
DR Reactome; R-SCE-9753281; Paracetamol ADME.
DR Reactome; R-SCE-9754706; Atorvastatin ADME.
DR Reactome; R-SCE-9758890; Transport of RCbl within the body.
DR PRO; PR:P39109; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39109; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015434; F:ABC-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IDA:SGD.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015127; F:bilirubin transmembrane transporter activity; IMP:SGD.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:RHEA.
DR GO; GO:0015723; P:bilirubin transport; IMP:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IGI:SGD.
DR GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR GO; GO:0010038; P:response to metal ion; IDA:SGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cadmium resistance; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1515
FT /note="Metal resistance protein YCF1"
FT /id="PRO_0000093449"
FT TOPO_DOM 1..32
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 54..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 95..99
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 121..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 152..169
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 191..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 300..345
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 367..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 444..446
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 468..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 552..572
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 594..943
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 944..964
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 965..1001
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1023
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1024..1066
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1067..1087
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1088
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1110..1180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1181..1201
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1202..1205
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 1206..1226
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1227..1515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 287..590
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 626..853
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 951..1235
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1272..1507
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 663..670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1306..1313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 911
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 713
FT /note="Missing: Loss of function."
FT MUTAGEN 908
FT /note="S->A: Loss of function."
FT CONFLICT 680
FT /note="L -> R (in Ref. 1; AAA50353)"
FT /evidence="ECO:0000305"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 37..56
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 70..95
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 101..127
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 134..160
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 169..188
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 252..268
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 285..301
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 304..322
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 351..378
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 411..419
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 429..433
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 434..444
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 459..492
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 494..499
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 504..517
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 523..553
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 561..579
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 581..601
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 625..636
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 642..645
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 646..654
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 669..676
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 680..685
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 687..691
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 707..712
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 719..728
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 732..737
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 741..743
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 755..769
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 772..777
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 785..794
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 801..804
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 805..810
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 815..819
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 821..827
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 830..835
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 837..841
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 842..844
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 846..851
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 937..944
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 948..981
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 982..984
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 988..1015
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 1016..1018
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1019..1033
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1038..1043
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1046..1049
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1051..1054
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1058..1062
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1065..1072
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1074..1088
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1090..1092
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1093..1125
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1129..1137
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 1140..1146
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1148..1183
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1186..1200
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1206..1216
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 1217..1221
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1222..1246
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1264..1269
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1272..1285
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1287..1292
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1301..1305
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1308..1311
FT /evidence="ECO:0007829|PDB:7MPE"
FT TURN 1317..1321
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1326..1332
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1342..1345
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1346..1348
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1350..1352
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1360..1362
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1363..1366
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1375..1384
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1389..1394
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1405..1408
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1414..1425
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1429..1434
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1442..1455
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1459..1464
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1468..1471
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1474..1481
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1491..1495
FT /evidence="ECO:0007829|PDB:7MPE"
FT STRAND 1496..1499
FT /evidence="ECO:0007829|PDB:7MPE"
FT HELIX 1501..1509
FT /evidence="ECO:0007829|PDB:7MPE"
SQ 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
