CMC_DICDI
ID CMC_DICDI Reviewed; 772 AA.
AC Q54RB9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Calcium-binding mitochondrial carrier protein;
DE AltName: Full=Mitochondrial substrate carrier family protein O;
GN Name=mcfO; ORFNames=DDB_G0283329;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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; AAFI02000052; EAL65805.1; -; Genomic_DNA.
DR RefSeq; XP_639128.1; XM_634036.1.
DR AlphaFoldDB; Q54RB9; -.
DR SMR; Q54RB9; -.
DR STRING; 44689.DDB0234089; -.
DR PaxDb; Q54RB9; -.
DR EnsemblProtists; EAL65805; EAL65805; DDB_G0283329.
DR GeneID; 8623999; -.
DR KEGG; ddi:DDB_G0283329; -.
DR dictyBase; DDB_G0283329; mcfO.
DR eggNOG; KOG0751; Eukaryota.
DR HOGENOM; CLU_014931_3_0_1; -.
DR InParanoid; Q54RB9; -.
DR OMA; DWDCEWA; -.
DR PhylomeDB; Q54RB9; -.
DR Reactome; R-DDI-70263; Gluconeogenesis.
DR Reactome; R-DDI-8963693; Aspartate and asparagine metabolism.
DR PRO; PR:Q54RB9; -.
DR Proteomes; UP000002195; Chromosome 4.
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; ISS:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IBA:GO_Central.
DR GO; GO:0043490; P:malate-aspartate shuttle; IBA:GO_Central.
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; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13833; EF-hand_8; 2.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..772
FT /note="Calcium-binding mitochondrial carrier protein"
FT /id="PRO_0000329428"
FT TRANSMEM 442..459
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 501..520
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 545..558
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 591..610
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 630..647
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT TRANSMEM 687..706
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT DOMAIN 132..165
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 166..201
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 235..270
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 347..382
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 436..526
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 535..616
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 624..712
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REGION 1..377
FT /note="N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 378..422
FT /note="Linker loop domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 432..720
FT /note="Carrier domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 721..772
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:O75746"
FT REGION 751..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 772 AA; 85648 MW; C7273988F0EF53FE CRC64;
MFANRVRQAQ KLYQKRFFSL GNNSTISKQQ FKNSSNNNNN KNGGNKNGFY QKAFIATTVA
LTTTLLTATT LLDDNTNSEK EILKSQRQTF EKYASTTLEG ERQMTAEDFL SALTTLESDK
QSGEHEILKA SLDADKFKVL FQMADVDHTG YISFDEYVMF DELMAKPEAE YFLAFKLFDR
DGNGYISKND FKHVITASLD PSIPFNFDCE LVNLYFGDGR TELNYSQFTQ LLKDLQQERI
KQEFKFHDKY NSGYIPRDKF AKVLGSVKLR KIPDHVRDKL ESISELNLLS GHPNEVSYSQ
FVAANDMLLH IPSYGRVLKA AILKNKKDNI NKEEFLTEAR SSTSIEITPL EIDLIFHLFD
LNKDGKLSIS DFEKSTGLNI NKIGGGTNYS DSYPSDSHVT IQNSSTTPSP STPITNTAAA
IALNKKHGKT FAQQVLESIE NFALGSIAGG IGAAAVYPID LVKTRMQNQR AVDPAKRLYV
NSWDCFKKVV KFEGVRGLYK GILPQMVGVA PEKAIKLTVN DLLRDLFGDK SKGEIYFPLE
VLAGGFAGMS QVCVTNPLEI VKIRLQVQST GPKVSAITII KELGLAGLYK GAGACLLRDI
PFSAIYFPTY AKMKTILANE DGKLGPMDLL LAGAVAGIPA ASLVTPADVI KTRLQVKANA
GEQTYTGIRD CFQKILKEEG PRALFKGALA RVFRSSPQFG VTLVSYELLQ KALLPDAEYK
PPTNAPITQK DFDVIRGNTN TVQRVIDMES KFGTLHQTRD NNKSSNGGEN KN
