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CMC1_YEAST
ID   CMC1_YEAST              Reviewed;         494 AA.
AC   D6W196; P48233; Q45TY5; Q6WV05; Q96US1;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Truncated non-functional calcium-binding mitochondrial carrier SAL1-1;
DE   AltName: Full=Suppressor of AAC2 lethality;
GN   Name=SAL1; OrderedLocusNames=YNL083W; ORFNames=N2312;
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=ATCC 96604 / S288c / FY1679;
RX   PubMed=8740422;
RX   DOI=10.1002/(sici)1097-0061(199604)12:5<485::aid-yea928>3.0.co;2-u;
RA   Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
RT   "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome
RT   XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading
RT   frames.";
RL   Yeast 12:485-491(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8701611;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA   Poehlmann R., Philippsen P.;
RT   "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT   reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT   ORFs.";
RL   Yeast 12:391-402(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 364-436.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA   Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA   Gates K., Gaffney T.D., Philippsen P.;
RT   "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT   comparison to the genome of a related fungus: Ashbya gossypii.";
RL   Genome Biol. 4:R45.1-R45.13(2003).
RN   [6]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RX   PubMed=9178508;
RX   DOI=10.1002/(sici)1097-0061(199705)13:6<573::aid-yea107>3.0.co;2-i;
RA   el Moualij B., Duyckaerts C., Lamotte-Brasseur J., Sluse F.E.;
RT   "Phylogenetic classification of the mitochondrial carrier family of
RT   Saccharomyces cerevisiae.";
RL   Yeast 13:573-581(1997).
RN   [7]
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   [8]
RP   FUNCTION, AND IDENTIFICATION OF FRAMESHIFT IN SAL1-1.
RC   STRAIN=M2915-6A;
RX   PubMed=15238515; DOI=10.1534/genetics.103.023655;
RA   Chen X.J.;
RT   "Sal1p, a calcium-dependent carrier protein that suppresses an essential
RT   cellular function associated With the Aac2 isoform of ADP/ATP translocase
RT   in Saccharomyces cerevisiae.";
RL   Genetics 167:607-617(2004).
RN   [9]
RP   CONFIRMATION OF FRAMESHIFT IN SAL1-1.
RC   STRAIN=ATCC 200879 / BY4716, and ATCC 204508 / S288c;
RX   PubMed=19581448; DOI=10.1534/genetics.109.104497;
RA   Dimitrov L.N., Brem R.B., Kruglyak L., Gottschling D.E.;
RT   "Polymorphisms in multiple genes contribute to the spontaneous
RT   mitochondrial genome instability of Saccharomyces cerevisiae S288C
RT   strains.";
RL   Genetics 183:365-383(2009).
CC   -!- FUNCTION: Calcium-dependent mitochondrial solute carrier.
CC       {ECO:0000269|PubMed:15238515}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Strain S288c has a frameshift in position 403, which disrupts
CC       the gene coding for this protein and produces the non-functional allele
CC       sal1-1. A full-length functional allele can be found in strain CG379
CC       (AC P0CI40). {ECO:0000305}.
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DR   EMBL; X89016; CAA61427.1; -; Genomic_DNA.
DR   EMBL; Z71359; CAA95958.1; -; Genomic_DNA.
DR   EMBL; AY268134; AAR26280.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10462.2; -; Genomic_DNA.
DR   PIR; S57539; S57539.
DR   RefSeq; NP_014316.3; NM_001182921.1.
DR   AlphaFoldDB; D6W196; -.
DR   SMR; D6W196; -.
DR   BioGRID; 35740; 61.
DR   STRING; 4932.YNL083W; -.
DR   iPTMnet; D6W196; -.
DR   PaxDb; D6W196; -.
DR   PRIDE; D6W196; -.
DR   GeneID; 855641; -.
DR   KEGG; sce:YNL083W; -.
DR   SGD; S000005027; SAL1.
DR   eggNOG; KOG0036; Eukaryota.
DR   HOGENOM; CLU_015166_2_1_1; -.
DR   InParanoid; D6W196; -.
DR   BioCyc; YEAST:G3O-33112-MON; -.
DR   PRO; PR:D6W196; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; D6W196; 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; HDA:SGD.
DR   GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IMP:SGD.
DR   GO; GO:0005509; F:calcium ion binding; IDA:SGD.
DR   GO; GO:0015866; P:ADP transport; IMP:SGD.
DR   GO; GO:0015867; P:ATP transport; IMP:SGD.
DR   GO; GO:0006839; P:mitochondrial transport; IMP:SGD.
DR   Gene3D; 1.50.40.10; -; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF00153; Mito_carr; 2.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50920; SOLCAR; 2.
PE   1: Evidence at protein level;
KW   Calcium; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..494
FT                   /note="Truncated non-functional calcium-binding
FT                   mitochondrial carrier SAL1-1"
FT                   /id="PRO_0000402277"
FT   TRANSMEM        231..248
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..326
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..368
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..428
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..475
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          11..46
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          80..115
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          120..155
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          156..191
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REPEAT          225..332
FT                   /note="Solcar 1"
FT   REPEAT          345..434
FT                   /note="Solcar 2"
FT   REPEAT          452..494
FT                   /note="Solcar 3; truncated"
FT   BINDING         65
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         99
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="V -> M (in Ref. 3; DAA10462)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  55715 MW;  0AB408E1CED63946 CRC64;
     MLLKNCETDK QRDIRYACLF KELDVKGNGQ VTLDNLISAF EKNDHPLKGN DEAIKMLFTA
     MDVNKDSVVD LSDFKKYASN AESQIWNGFQ RIDLDHDGKI GINEINRYLS DLDNQSICNN
     ELNHELSNEK VNKFSRFFEW AFPKRKANIA LRGQASHKKN TDNDRSKKTT DSDLYVTYDQ
     WRDFLLLVPR KQGSRLHTAY SYFYLFNEDV DLSSEGDVTL INDFIRGFGF FIAGGISGVI
     SRTCTAPFDR LKVFLIARTD LSSILLNSKT DLLAKNPNAD INKISSPLAK AVKSLYRQGG
     IKAFYVGNGL NVIKVFPESS IKFGSFEVTK KIMTKLEGCR DTKDLSKFST YIAGGLAGMA
     AQFSVYPIDT LKFRVQCAPL DTKLKGNNLL FQTAKDMFRE GGGQIILQRC HSRYSGHISL
     CCIRFGDFFC LKKMVYCQTG KDPEPTTRSG HSKQPGCTSN GCIQWNCRSF CCLSNQSFKN
     KTTSPRNICT SLCV
 
 
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