GMC1_YEAST
ID GMC1_YEAST Reviewed; 608 AA.
AC Q04399; D6VTC8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Putative multicopper oxidase GMC1;
DE EC=1.-.-.-;
DE AltName: Full=Grand meiotic recombination cluster protein 1;
GN Name=GMC1; OrderedLocusNames=YDR506C; ORFNames=D9719.12;
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 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 [4]
RP FUNCTION.
RX PubMed=22194413; DOI=10.1126/science.1215110;
RA Brar G.A., Yassour M., Friedman N., Regev A., Ingolia N.T., Weissman J.S.;
RT "High-resolution view of the yeast meiotic program revealed by ribosome
RT profiling.";
RL Science 335:552-557(2012).
CC -!- FUNCTION: Could be an iron transport multicopper oxidase, which is
CC required for Fe(2+) high affinity uptake. May be required to oxidize
CC Fe(2+) and release it from the transporter. Essential component of
CC copper-dependent iron transport (By similarity). Involved in meiotic
CC prophase and synaptonemal complex (SC) assembly. {ECO:0000250,
CC ECO:0000269|PubMed:22194413}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; U33057; AAB64948.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12338.1; -; Genomic_DNA.
DR PIR; S69564; S69564.
DR RefSeq; NP_010794.3; NM_001180814.3.
DR AlphaFoldDB; Q04399; -.
DR SMR; Q04399; -.
DR BioGRID; 32557; 54.
DR DIP; DIP-5270N; -.
DR IntAct; Q04399; 3.
DR MINT; Q04399; -.
DR STRING; 4932.YDR506C; -.
DR MaxQB; Q04399; -.
DR PaxDb; Q04399; -.
DR PRIDE; Q04399; -.
DR EnsemblFungi; YDR506C_mRNA; YDR506C; YDR506C.
DR GeneID; 852117; -.
DR KEGG; sce:YDR506C; -.
DR SGD; S000002914; GMC1.
DR VEuPathDB; FungiDB:YDR506C; -.
DR eggNOG; KOG1263; Eukaryota.
DR GeneTree; ENSGT00940000176768; -.
DR HOGENOM; CLU_440088_0_0_1; -.
DR InParanoid; Q04399; -.
DR OMA; CNTRAIP; -.
DR BioCyc; YEAST:G3O-30027-MON; -.
DR PRO; PR:Q04399; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04399; protein.
DR GO; GO:0033573; C:high-affinity iron permease complex; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR GO; GO:0070193; P:synaptonemal complex organization; IMP:SGD.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Ion transport; Iron; Iron transport; Meiosis; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..608
FT /note="Putative multicopper oxidase GMC1"
FT /id="PRO_0000085585"
FT DOMAIN 51..163
FT /note="Plastocyanin-like 1"
FT DOMAIN 243..374
FT /note="Plastocyanin-like 2"
FT DOMAIN 421..548
FT /note="Plastocyanin-like 3"
FT BINDING 100
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 457
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
SQ SEQUENCE 608 AA; 69281 MW; D51B830F15E704AC CRC64;
MKVILLKPVQ LPMLLLILLK FIMAAKEGKI HVLEFNASSE YTLDKRRVIS INGYSATFGP
EIRVKSGDTL NLKLTNWICS EEEASKDSDV WKDYCSTALH FHGVVPLANE FDGIPGLTQP
TIGYGESYWY NFTIDQSTCG TFWYHSHSSV QYGDGMRGVL IVECDDYDNH VANTINSVRD
IETLDDGVVT MKKDKHTKEL TDYEVQERII TLSDWYTNWN LDILNDKVLS STGGTDPKFD
GSLINGKSSD GETIKIGFNT EYLLLRIVNS GMSGTQVFHL DGFQLIVLEA DGIMIKPFIV
QTINLAVGQR YTILVKLKSD TSFIRMINGC NKMMGYITKQ WWFYKEGAHL DLPKNPNDVS
IEHLPGFTKA ELYRDIEPTQ EENKKLRTKA DPVAVFEFDY AYYKDESTKQ KYGTGMYKVN
ERTFSEYVKD PVRFGFNETY DIVINSLDHM RHPWHMHGHH FQIISLGNKG DGPFHKDVQE
GKAWSRYQND LRHLARTGKA PMVRDSINIA GNSYAVLRIN TEMPGKWLLH CHVEWHMMKG
LGIVFEVPTT TEDSTKQATT AVLSYPTKEP DPNTVVHTAA LEQNKSKVIA VYILIMCAVD
AIFYWLLM
