CMC2_CAEEL
ID CMC2_CAEEL Reviewed; 588 AA.
AC Q20799;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putative calcium-binding mitochondrial carrier F55A11.4;
GN ORFNames=F55A11.4;
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:Q9UJS0}.
CC -!- SUBUNIT: Homodimer (via N-terminus). {ECO:0000250|UniProtKB:Q9UJS0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9UJS0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9UJS0}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; Z72511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T22688; T22688.
DR AlphaFoldDB; Q20799; -.
DR SMR; Q20799; -.
DR STRING; 6239.F55A11.4a; -.
DR EPD; Q20799; -.
DR PaxDb; Q20799; -.
DR eggNOG; KOG0036; Eukaryota.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; Q20799; -.
DR Proteomes; UP000001940; Chromosome V.
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:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
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; IPR002167; Graves_DC.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00928; GRAVESDC.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 5: Uncertain;
KW Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..588
FT /note="Putative calcium-binding mitochondrial carrier
FT F55A11.4"
FT /id="PRO_0000090604"
FT TRANSMEM 252..269
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 307..326
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 352..365
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 403..422
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 446..463
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 504..523
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT DOMAIN 73..108
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 109..139
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 140..175
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 176..211
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 246..332
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 342..428
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 440..529
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 588 AA; 66337 MW; 68DDF60923D8697D CRC64;
MINKNEQTES TSGAAEQKED DEEQYVQLSS LGEYKDEVTP LLSPKHVPLV LGKVTKEAAI
ATHSALHGGM SEEKERQIRD IYDRLDIDND GTIDIRDLTL ALKHETPHIP ANLAPVIMSK
MSPDDEGRVD FYSFSSYVLE NEQKLAEMFA DMDRNHDGLV DVVEMKNYCK DIGVPLDDHK
AQHIVNKMDQ TGSASVDLKE FQEFMMLYPS SDLKDIVDFW RHNLIIDIGE DSQIPEDFSQ
QEMQEGIWWR HLVAGGAAGA VSRTCTAPFD RIKVYLQVNS SKTNRLGVMS CLKLLHAEGG
IKSFWRGNGI NVIKIAPESA IKFMCYDQLK RLIQKKKGNE EISTFERLCA GSAAGAISQS
TIYPMEVMKT RLALRKTGQL DRGIIHFAHK MYTKEGIRCF YKGYLPNLIG IIPYAGIDLA
IYETLKRTYV RYYETNSSEP GVLALLACGT CSSTCGQLSS YPFALVRTRL QALSITRYSP
QPDTMFGQFK YILQNEGVTG FYRGITPNFL KVIPAVSISY VVYEKVRTGL GVPVCSRGGL
EDIHQFLPCS IHSIIQFFFF PRTFLLTISG RSLRVKPVWR SHFSKFNK
