MCFB_DICDI
ID MCFB_DICDI Reviewed; 434 AA.
AC Q54MZ4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Mitochondrial substrate carrier family protein B;
GN Name=mcfB; ORFNames=DDB_G0285599;
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).
RN [2]
RP REVIEW.
RX PubMed=17442478; DOI=10.1016/j.biochi.2007.03.004;
RA Satre M., Mattei S., Aubry L., Gaudet P., Pelosi L., Brandolin G.,
RA Klein G.;
RT "Mitochondrial carrier family: repertoire and peculiarities of the cellular
RT slime mould Dictyostelium discoideum.";
RL Biochimie 89:1058-1069(2007).
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial
CC solute carriers shuttle metabolites, nucleotides, and cofactors through
CC the mitochondrial inner membrane (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64637.1; -; Genomic_DNA.
DR RefSeq; XP_638149.1; XM_633057.1.
DR AlphaFoldDB; Q54MZ4; -.
DR SMR; Q54MZ4; -.
DR PaxDb; Q54MZ4; -.
DR EnsemblProtists; EAL64637; EAL64637; DDB_G0285599.
DR GeneID; 8625197; -.
DR KEGG; ddi:DDB_G0285599; -.
DR dictyBase; DDB_G0285599; mcfB.
DR eggNOG; KOG0752; Eukaryota.
DR HOGENOM; CLU_015166_2_1_1; -.
DR InParanoid; Q54MZ4; -.
DR OMA; KLPGMWA; -.
DR PhylomeDB; Q54MZ4; -.
DR Reactome; R-DDI-196783; Coenzyme A biosynthesis.
DR PRO; PR:Q54MZ4; -.
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; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; 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; 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; PR00926; MITOCARRIER.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF103506; SSF103506; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
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..434
FT /note="Mitochondrial substrate carrier family protein B"
FT /id="PRO_0000385518"
FT TOPO_DOM 1..141
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..159
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..203
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 204..224
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..244
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 245..265
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..293
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 294..314
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..338
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 339..359
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..402
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 403..423
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..434
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT DOMAIN 40..75
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 77..112
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 136..229
FT /note="Solcar 1"
FT REPEAT 239..325
FT /note="Solcar 2"
FT REPEAT 333..422
FT /note="Solcar 3"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 434 AA; 48684 MW; 40E6C46F905314A3 CRC64;
MSNNNNNNNN NNNNNNNNNN NNNNNNNNDK NNNNNIDSSI KEKKLKEWFD KFDVDKDGSL
DSNELKKGFK LHANIDMKDE QITKMMERAD SNKNHRIEWD EFLKVASDSS SPEIEDIAEH
WLQYSTKPIV HAPADVPSWK LLLSGGVAGA VSRTCTSPLE RLKILNQVGH MNLEQNAPKY
KGRGIIQSLK TMYTTEGFIG FFKGNGTNVI RIAPYSAIQF LSYEKYKNFL LNNNDQTHLT
TYENLFVGGA AGVTSLLCTY PLDLIRSRLT VQVFGNKYNG IADTCKMIIR EEGVAGLYKG
LFASALGVAP YVAINFTTYE NLKKTFIPKD TTPTVVQSLT FGAISGATAQ TLTYPIDLIR
RRLQVQGIGG KDILYNGTFD AFRKIIRDEG VLGLYNGMIP CYLKVIPAIS ISFCVYEVMK
KILKIDSKKI SYQS