YMC1_YEAST
ID YMC1_YEAST Reviewed; 307 AA.
AC P32331; D6W464; Q12002;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Mitochondrial glycine transporter YMC1 {ECO:0000305};
DE AltName: Full=Yeast mitochondrial carrier protein 1 {ECO:0000303|PubMed:8488731};
GN Name=YMC1 {ECO:0000303|PubMed:8488731};
GN OrderedLocusNames=YPR058W {ECO:0000312|SGD:S000006262}; ORFNames=YP9499.14;
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=8488731; DOI=10.1002/yea.320090310;
RA Graf R., Baum B., Braus G.H.;
RT "YMC1, a yeast gene encoding a new putative mitochondrial carrier
RT protein.";
RL Yeast 9:301-305(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 SUBCELLULAR LOCATION.
RX PubMed=10930523; DOI=10.1016/s0005-2736(00)00222-4;
RA Belenkiy R., Haefele A., Eisen M.B., Wohlrab H.;
RT "The yeast mitochondrial transport proteins: new sequences and consensus
RT residues, lack of direct relation between consensus residues and
RT transmembrane helices, expression patterns of the transport protein genes,
RT and protein-protein interactions with other proteins.";
RL Biochim. Biophys. Acta 1467:207-218(2000).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [6]
RP FUNCTION.
RX PubMed=26821380; DOI=10.1371/journal.pgen.1005783;
RA Fernandez-Murray J.P., Prykhozhij S.V., Dufay J.N., Steele S.L., Gaston D.,
RA Nasrallah G.K., Coombs A.J., Liwski R.S., Fernandez C.V., Berman J.N.,
RA McMaster C.R.;
RT "Glycine and folate ameliorate models of congenital sideroblastic anemia.";
RL PLoS Genet. 12:E1005783-E1005783(2016).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA He C., Jia C., Zhang Y., Xu P.;
RT "Enrichment-based proteogenomics identifies microproteins, missing
RT proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL J. Proteome Res. 17:2335-2344(2018).
CC -!- FUNCTION: Secondary mitochondrial glycine transporter required for the
CC biosynthesis of heme at high glycine concentrations. Imports the
CC precursor glycine into the mitochondrial matrix, where it is condensed
CC with succinyl-CoA to produce 5-aminolevulinate (ALA), the first step of
CC heme biosynthesis. {ECO:0000269|PubMed:26821380}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823961, ECO:0000305|PubMed:10930523}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16823961,
CC ECO:0000305|PubMed:10930523}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; X67122; CAA47602.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95003.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89176.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11480.1; -; Genomic_DNA.
DR PIR; S54080; S54080.
DR RefSeq; NP_015383.1; NM_001184155.1.
DR AlphaFoldDB; P32331; -.
DR SMR; P32331; -.
DR BioGRID; 36232; 58.
DR DIP; DIP-3895N; -.
DR IntAct; P32331; 1.
DR MINT; P32331; -.
DR STRING; 4932.YPR058W; -.
DR TCDB; 2.A.29.8.12; the mitochondrial carrier (mc) family.
DR MaxQB; P32331; -.
DR PaxDb; P32331; -.
DR PRIDE; P32331; -.
DR EnsemblFungi; YPR058W_mRNA; YPR058W; YPR058W.
DR GeneID; 856171; -.
DR KEGG; sce:YPR058W; -.
DR SGD; S000006262; YMC1.
DR VEuPathDB; FungiDB:YPR058W; -.
DR eggNOG; KOG0758; Eukaryota.
DR GeneTree; ENSGT00940000176446; -.
DR HOGENOM; CLU_015166_16_2_1; -.
DR InParanoid; P32331; -.
DR OMA; HCITETV; -.
DR BioCyc; YEAST:G3O-34210-MON; -.
DR Reactome; R-SCE-70635; Urea cycle.
DR PRO; PR:P32331; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32331; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IGI:SGD.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005342; F:organic acid transmembrane transporter activity; IGI:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904983; P:glycine import into mitochondrion; IGI:SGD.
DR GO; GO:0006783; P:heme biosynthetic process; IGI:SGD.
DR GO; GO:1990575; P:mitochondrial L-ornithine transmembrane transport; IBA:GO_Central.
DR GO; GO:0006839; P:mitochondrial transport; IGI:SGD.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..307
FT /note="Mitochondrial glycine transporter YMC1"
FT /id="PRO_0000019265"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 26..106
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 121..204
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 218..305
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT CONFLICT 101
FT /note="E -> Q (in Ref. 1; CAA47602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33376 MW; 106C1464B8DCC09A CRC64;
MSEEFPSPQL IDDLEEHPQH DNARVVKDLL AGTAGGIAQV LVGQPFDTTK VRLQTSSTPT
TAMEVVRKLL ANEGPRGFYK GTLTPLIGVG ACVSLQFGVN EAMKRFFHHR NADMSSTLSL
PQYYACGVTG GIVNSFLASP IEHVRIRLQT QTGSGTNAEF KGPLECIKKL RHNKALLRGL
TPTILREGHG CGTYFLVYEA LIANQMNKRR GLERKDIPAW KLCIFGALSG TALWLMVYPL
DVIKSVMQTD NLQKPKFGNS ISSVAKTLYA NGGIGAFFKG FGPTMLRAAP ANGATFATFE
LAMRLLG
