SCMC3_HUMAN
ID SCMC3_HUMAN Reviewed; 468 AA.
AC Q9BV35; B4DGB6; Q4LBC2; Q705K3; Q86Y43; Q8N2N4; Q96NQ4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-3;
DE AltName: Full=Mitochondrial ATP-Mg/Pi carrier protein 2;
DE AltName: Full=Mitochondrial Ca(2+)-dependent solute carrier protein 2;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 3;
DE AltName: Full=Solute carrier family 25 member 23;
GN Name=SLC25A23; Synonyms=APC2, MCSC2, SCAMC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15054102; DOI=10.1074/jbc.m401417200;
RA del Arco A., Satrustegui J.;
RT "Identification of a novel human subfamily of mitochondrial carriers with
RT calcium-binding domains.";
RL J. Biol. Chem. 279:24701-24713(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15123600; DOI=10.1074/jbc.m400445200;
RA Fiermonte G., De Leonardis F., Todisco S., Palmieri L., Lasorsa F.M.,
RA Palmieri F.;
RT "Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial
RT expression, reconstitution, functional characterization, and tissue
RT distribution.";
RL J. Biol. Chem. 279:30722-30730(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP CALCIUM-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=15716113; DOI=10.1016/j.gene.2004.11.028;
RA Bassi M.T., Manzoni M., Bresciani R., Pizzo M.T., Della Monica A.,
RA Barlati S., Monti E., Borsani G.;
RT "Cellular expression and alternative splicing of SLC25A23, a member of the
RT mitochondrial Ca2+-dependent solute carrier gene family.";
RL Gene 345:173-182(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala, Cerebellum, and Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 413-468 (ISOFORM 4), AND ALTERNATIVE
RP SPLICING.
RX PubMed=15801905; DOI=10.1042/bj20050283;
RA Del Arco A.;
RT "Novel variants of human SCaMC-3, an isoform of the ATP-Mg/P(i)
RT mitochondrial carrier, generated by alternative splicing from 3'-flanking
RT transposable elements.";
RL Biochem. J. 389:647-655(2005).
RN [8]
RP FUNCTION, INTERACTION WITH MCU AND MICU1, AND MUTAGENESIS OF ASP-22;
RP GLU-33; ASP-90 AND GLU-101.
RX PubMed=24430870; DOI=10.1091/mbc.e13-08-0502;
RA Hoffman N.E., Chandramoorthy H.C., Shanmughapriya S., Zhang X.Q.,
RA Vallem S., Doonan P.J., Malliankaraman K., Guo S., Rajan S., Elrod J.W.,
RA Koch W.J., Cheung J.Y., Madesh M.;
RT "SLC25A23 augments mitochondrial Ca(2+) uptake, interacts with MCU, and
RT induces oxidative stress-mediated cell death.";
RL Mol. Biol. Cell 25:936-947(2014).
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial
CC solute carriers shuttle metabolites, nucleotides, and cofactors through
CC the mitochondrial inner membrane (PubMed:15123600). May act as a ATP-
CC Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for
CC phosphate, catalyzing the net uptake or efflux of adenine nucleotides
CC into or from the mitochondria (PubMed:15123600). Acts as a regulator of
CC mitochondrial calcium uptake via interaction with MCU and MICU1
CC (PubMed:24430870). {ECO:0000269|PubMed:15123600,
CC ECO:0000269|PubMed:24430870}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for AMP {ECO:0000269|PubMed:15123600};
CC KM=0.54 mM for ADP {ECO:0000269|PubMed:15123600};
CC KM=0.31 mM for ATP {ECO:0000269|PubMed:15123600};
CC KM=0.22 mM for ATP-Mg {ECO:0000269|PubMed:15123600};
CC KM=1.4 mM for Pi {ECO:0000269|PubMed:15123600};
CC Vmax=68 umol/min/g enzyme with AMP as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=73 umol/min/g enzyme with ADP as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=65 umol/min/g enzyme with ATP as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=79 umol/min/g enzyme with ATP-Mg as substrate
CC {ECO:0000269|PubMed:15123600};
CC Vmax=70 umol/min/g enzyme with Pi as substrate
CC {ECO:0000269|PubMed:15123600};
CC -!- SUBUNIT: Interacts with MCU (PubMed:24430870). Interacts with MICU1
CC (PubMed:24430870). {ECO:0000269|PubMed:24430870}.
CC -!- INTERACTION:
CC Q9BV35; Q92624: APPBP2; NbExp=3; IntAct=EBI-2933255, EBI-743771;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600,
CC ECO:0000269|PubMed:15716113}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600,
CC ECO:0000269|PubMed:15716113}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=SCaMC-3a;
CC IsoId=Q9BV35-1; Sequence=Displayed;
CC Name=2; Synonyms=SCaMC-3b;
CC IsoId=Q9BV35-2; Sequence=VSP_031075;
CC Name=3; Synonyms=SCaMC-3c;
CC IsoId=Q9BV35-3; Sequence=VSP_031074, VSP_031076;
CC Name=4; Synonyms=SCaMC-3d;
CC IsoId=Q9BV35-4; Sequence=VSP_031076;
CC -!- TISSUE SPECIFICITY: Present in various cell lines (at protein level).
CC Expressed at low levels in most tissues examined, with highest
CC expression in brain, skeletal muscle and pancreas.
CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600,
CC ECO:0000269|PubMed:15716113}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70825.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11071.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ619988; CAF04494.1; -; mRNA.
DR EMBL; AJ619962; CAF04059.1; -; mRNA.
DR EMBL; AJ512835; CAD55563.1; -; mRNA.
DR EMBL; AY750170; AAU95077.1; -; mRNA.
DR EMBL; AK054901; BAB70825.1; ALT_INIT; mRNA.
DR EMBL; AK074579; BAC11071.1; ALT_INIT; mRNA.
DR EMBL; AK294514; BAG57727.1; -; mRNA.
DR EMBL; CH471139; EAW69087.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69089.1; -; Genomic_DNA.
DR EMBL; BC001656; AAH01656.1; -; mRNA.
DR EMBL; AJ879082; CAI51684.1; -; mRNA.
DR EMBL; AJ879083; CAI51685.1; -; mRNA.
DR CCDS; CCDS32882.1; -. [Q9BV35-1]
DR RefSeq; NP_077008.2; NM_024103.2. [Q9BV35-1]
DR AlphaFoldDB; Q9BV35; -.
DR SMR; Q9BV35; -.
DR BioGRID; 122533; 34.
DR IntAct; Q9BV35; 20.
DR STRING; 9606.ENSP00000301454; -.
DR TCDB; 2.A.29.23.5; the mitochondrial carrier (mc) family.
DR iPTMnet; Q9BV35; -.
DR PhosphoSitePlus; Q9BV35; -.
DR BioMuta; SLC25A23; -.
DR DMDM; 167016556; -.
DR EPD; Q9BV35; -.
DR jPOST; Q9BV35; -.
DR MassIVE; Q9BV35; -.
DR MaxQB; Q9BV35; -.
DR PaxDb; Q9BV35; -.
DR PeptideAtlas; Q9BV35; -.
DR PRIDE; Q9BV35; -.
DR ProteomicsDB; 79158; -. [Q9BV35-1]
DR ProteomicsDB; 79159; -. [Q9BV35-2]
DR ProteomicsDB; 79160; -. [Q9BV35-3]
DR ProteomicsDB; 79161; -. [Q9BV35-4]
DR Antibodypedia; 24155; 96 antibodies from 19 providers.
DR DNASU; 79085; -.
DR Ensembl; ENST00000264088.8; ENSP00000264088.3; ENSG00000125648.15. [Q9BV35-3]
DR Ensembl; ENST00000301454.9; ENSP00000301454.3; ENSG00000125648.15. [Q9BV35-1]
DR Ensembl; ENST00000334510.9; ENSP00000334537.4; ENSG00000125648.15. [Q9BV35-2]
DR GeneID; 79085; -.
DR KEGG; hsa:79085; -.
DR MANE-Select; ENST00000301454.9; ENSP00000301454.3; NM_024103.3; NP_077008.2.
DR UCSC; uc002mex.2; human. [Q9BV35-1]
DR CTD; 79085; -.
DR DisGeNET; 79085; -.
DR GeneCards; SLC25A23; -.
DR HGNC; HGNC:19375; SLC25A23.
DR HPA; ENSG00000125648; Tissue enhanced (brain).
DR MIM; 608746; gene.
DR neXtProt; NX_Q9BV35; -.
DR OpenTargets; ENSG00000125648; -.
DR PharmGKB; PA134932456; -.
DR VEuPathDB; HostDB:ENSG00000125648; -.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000159428; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; Q9BV35; -.
DR OMA; GHWILDI; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q9BV35; -.
DR TreeFam; TF313492; -.
DR PathwayCommons; Q9BV35; -.
DR SignaLink; Q9BV35; -.
DR BioGRID-ORCS; 79085; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; SLC25A23; human.
DR GenomeRNAi; 79085; -.
DR Pharos; Q9BV35; Tbio.
DR PRO; PR:Q9BV35; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BV35; protein.
DR Bgee; ENSG00000125648; Expressed in nucleus accumbens and 183 other tissues.
DR ExpressionAtlas; Q9BV35; baseline and differential.
DR Genevisible; Q9BV35; HS.
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; IDA:HPA.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0036444; P:calcium import into the mitochondrion; IMP:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IMP:UniProtKB.
DR GO; GO:1900069; P:regulation of cellular hyperosmotic salinity response; IMP:UniProtKB.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IEA:Ensembl.
DR GO; GO:0051282; P:regulation of sequestering of calcium ion; IEA:Ensembl.
DR GO; GO:0097274; P:urea homeostasis; IEA:Ensembl.
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; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 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; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..468
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 3"
FT /id="PRO_0000317609"
FT TOPO_DOM 1..188
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..206
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..243
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..263
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..286
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..300
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..336
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..356
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..379
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..397
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..436
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..456
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..468
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 9..44
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 DOMAIN 113..148
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 183..269
FT /note="Solcar 1"
FT REPEAT 277..362
FT /note="Solcar 2"
FT REPEAT 374..462
FT /note="Solcar 3"
FT REGION 34..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
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"
FT VAR_SEQ 161
FT /note="T -> TLSSAGFSAWIKDSTAEQNRSKTTVLARRSGSHLKSQHFGRPKWADH
FT E (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031074"
FT VAR_SEQ 408..468
FT /note="ASIEGGPQLSMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAVSISYVVYENM
FT KQALGVTSR -> DVSVYKTDTVPTLIELTGRRGRKMLNKSFWN (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15716113"
FT /id="VSP_031075"
FT VAR_SEQ 408..468
FT /note="ASIEGGPQLSMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAVSISYVVYENM
FT KQALGVTSR -> GWSTVARFQITATSAFQVQAILLPQPPE (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15801905"
FT /id="VSP_031076"
FT MUTAGEN 22
FT /note="D->A: Abolishes the ability to regulate
FT mitochondrial calcium uptake; when associated with K-33; A-
FT 90 and K-101."
FT /evidence="ECO:0000269|PubMed:24430870"
FT MUTAGEN 33
FT /note="E->K: Abolishes the ability to regulate
FT mitochondrial calcium uptake; when associated with A-22; A-
FT 90 and K-101."
FT /evidence="ECO:0000269|PubMed:24430870"
FT MUTAGEN 90
FT /note="D->A: Abolishes the ability to regulate
FT mitochondrial calcium uptake; when associated with A-22; K-
FT 33 and K-101."
FT /evidence="ECO:0000269|PubMed:24430870"
FT MUTAGEN 101
FT /note="E->K: Abolishes the ability to regulate
FT mitochondrial calcium uptake; when associated with A-22; K-
FT 33 and A-90."
FT /evidence="ECO:0000269|PubMed:24430870"
SQ SEQUENCE 468 AA; 52378 MW; B2D66A4665C27174 CRC64;
MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISSEGDA
DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISISLEQAEK
ILHSMDRDGT MTIDWQEWRD HFLLHSLENV EDVLYFWKHS TVLDIGECLT VPDEFSKQEK
LTGMWWKQLV AGAVAGAVSR TGTAPLDRLK VFMQVHASKT NRLNILGGLR SMVLEGGIRS
LWRGNGINVL KIAPESAIKF MAYEQIKRAI LGQQETLHVQ ERFVAGSLAG ATAQTIIYPM
EVLKTRLTLR RTGQYKGLLD CARRILEREG PRAFYRGYLP NVLGIIPYAG IDLAVYETLK
NWWLQQYSHD SADPGILVLL ACGTISSTCG QIASYPLALV RTRMQAQASI EGGPQLSMLG
LLRHILSQEG MRGLYRGIAP NFMKVIPAVS ISYVVYENMK QALGVTSR
