CMC1_CAEEL
ID CMC1_CAEEL Reviewed; 716 AA.
AC Q21153; L8E976;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Probable calcium-binding mitochondrial carrier K02F3.2;
GN ORFNames=K02F3.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Mitochondrial and calcium-binding carrier that catalyzes the
CC calcium-dependent exchange of cytoplasmic glutamate with mitochondrial
CC aspartate across the mitochondrial inner membrane.
CC {ECO:0000250|UniProtKB:O75746}.
CC -!- SUBUNIT: Homodimer (via N-terminus). {ECO:0000250|UniProtKB:O75746}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O75746}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O75746}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q21153-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q21153-2; Sequence=VSP_053225;
CC -!- DOMAIN: Upon calcium binding, the EF-hand-containing regulatory N-
CC terminal domain binds to the C-terminal domain, opening a vestibule
CC which allows the substrates to be translocated through the carrier
CC domain. In the absence of calcium, the linker loop domain may close the
CC vestibule, which may prevent substrates from entering the carrier
CC domain. {ECO:0000250|UniProtKB:O75746}.
CC -!- MISCELLANEOUS: Binds to one calcium ion with high affinity.
CC {ECO:0000250|UniProtKB:O75746}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; FO080195; CCD61871.2; -; Genomic_DNA.
DR EMBL; FO080195; CCQ25712.1; -; Genomic_DNA.
DR PIR; T16533; T16533.
DR RefSeq; NP_001263698.1; NM_001276769.1. [Q21153-1]
DR RefSeq; NP_497274.3; NM_064873.5. [Q21153-2]
DR AlphaFoldDB; Q21153; -.
DR SMR; Q21153; -.
DR BioGRID; 40511; 9.
DR STRING; 6239.K02F3.2b; -.
DR EPD; Q21153; -.
DR PaxDb; Q21153; -.
DR PeptideAtlas; Q21153; -.
DR EnsemblMetazoa; K02F3.2a.1; K02F3.2a.1; WBGene00019326. [Q21153-2]
DR EnsemblMetazoa; K02F3.2b.1; K02F3.2b.1; WBGene00019326. [Q21153-1]
DR GeneID; 175242; -.
DR KEGG; cel:CELE_K02F3.2; -.
DR UCSC; K02F3.2; c. elegans. [Q21153-1]
DR CTD; 175242; -.
DR WormBase; K02F3.2a; CE48021; WBGene00019326; -. [Q21153-2]
DR WormBase; K02F3.2b; CE48184; WBGene00019326; -. [Q21153-1]
DR eggNOG; KOG0751; Eukaryota.
DR GeneTree; ENSGT00940000155963; -.
DR InParanoid; Q21153; -.
DR OMA; DWDCEWA; -.
DR OrthoDB; 1007928at2759; -.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR Reactome; R-CEL-8963693; Aspartate and asparagine metabolism.
DR PRO; PR:Q21153; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019326; Expressed in larva and 3 other tissues.
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:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015810; P:aspartate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IBA:GO_Central.
DR GO; GO:0043490; P:malate-aspartate shuttle; IBA:GO_Central.
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; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 3.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Alternative splicing; Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..716
FT /note="Probable calcium-binding mitochondrial carrier
FT K02F3.2"
FT /id="PRO_0000090603"
FT TRANSMEM 382..399
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 443..462
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 485..498
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 535..554
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 574..591
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 631..650
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT DOMAIN 93..121
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 127..162
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 165..195
FT /note="EF-hand 3"
FT /evidence="ECO:0000305"
FT DOMAIN 198..233
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 376..468
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 475..560
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 568..656
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REGION 1..345
FT /note="N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 346..362
FT /note="Linker loop domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 372..664
FT /note="Carrier domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 665..716
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 256..263
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_053225"
SQ SEQUENCE 716 AA; 79595 MW; FD9C7DC32D50ADAD CRC64;
MSFDHLLTSS KRRELLQNLG IGHGSDVFST GLFRKAECNA ETAISQRSIP RANPDHLRPI
FDRFATKEIK GKKLMTPEDF IRGYLGLYTE ENYNKETVRL LASAADTTKD GDISFEEFCA
FEALLCSPDA LYLTAFELFD RNASDTISCD EFEAVIRHTQ PLHDQDFDFS SEFIKRYFGA
DKQRNVNYHS FCQLLHDFYE EQGIQAFKRY DKNGNGTISS LDFQQIMTTV KGHLLTDFVR
HNLIAVSGGG ASGHKFSDTR GGFVTFPYYA AFNSLLAKME LIKRVYVSTT RGNLDIEMTK
EEFLHAIQSY TQVTPYEVEI LFHLSELNHP GRKTLCLKDI QAIDPERLKR VSQMDRLINI
KAVHHKDDRG VGTAFLESAY RFLLGSVAGA CGATAVYPID LVKTRMQNQR TSGSFVGEVM
YKNSLDCFKK VVKFEGLLGL YRGLLPQIVG VAPEKAIKLT MNDYMRDKFT KDGKIPLYGE
IIAGGTGGMC QVVFTNPLEI VKIRLQTAGE VQQAGKKIGV FTVLKELGFL GLYKGSRACF
LRDIPFSAIY FPAYAHAKLA SADEDGMNSP GTLFASAFIA GVPAAGLVTP ADVIKTRLQV
AARAGQTTYN GVIDCARKLI KEEGPMSLWK GTAARVCRSS PQFAVTLLTY EVLQRLFYVD
FAGSRPTGSE LATTKTIQDE SSTNPDHVGG YKLAAATFSG IEHKFGLFLP KFETSK
