SCMC2_HUMAN
ID SCMC2_HUMAN Reviewed; 469 AA.
AC Q6KCM7; Q5SYW7; Q5SYW8; Q5SYX3; Q5VWU2; Q5VWU3; Q5VWU4; Q6KCM4; Q6KCM6;
AC Q6UX48; Q705K2; Q96PZ1; Q9BSA6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-2;
DE AltName: Full=Mitochondrial ATP-Mg/Pi carrier protein 3;
DE AltName: Full=Mitochondrial Ca(2+)-dependent solute carrier protein 3;
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 2;
DE AltName: Full=Solute carrier family 25 member 25;
GN Name=SLC25A25; Synonyms=APC3, KIAA1896, MCSC3, SCAMC2;
GN ORFNames=UNQ549/PRO1106;
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] (ISOFORMS 1; 2; 4 AND 6), SUBCELLULAR LOCATION,
RP AND TISSUE 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 4), FUNCTION, SUBCELLULAR LOCATION, AND
RP 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 [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Teratocarcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Chondrosarcoma, and Muscle;
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).
CC -!- FUNCTION: Calcium-dependent mitochondrial solute carrier. Mitochondrial
CC solute carriers shuttle metabolites, nucleotides, and cofactors through
CC the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that
CC mediates the transport of Mg-ATP in exchange for phosphate, catalyzing
CC the net uptake or efflux of adenine nucleotides into or from the
CC mitochondria. {ECO:0000269|PubMed:15123600}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15054102,
CC ECO:0000269|PubMed:15123600}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=SCaMC-2a;
CC IsoId=Q6KCM7-1; Sequence=Displayed;
CC Name=2; Synonyms=SCaMC-2b;
CC IsoId=Q6KCM7-2; Sequence=VSP_031069;
CC Name=3;
CC IsoId=Q6KCM7-3; Sequence=VSP_031069, VSP_031070;
CC Name=4; Synonyms=SCaMC-2c;
CC IsoId=Q6KCM7-4; Sequence=VSP_031068;
CC Name=5;
CC IsoId=Q6KCM7-5; Sequence=VSP_031068, VSP_031070;
CC Name=6; Synonyms=SCaMC-2d;
CC IsoId=Q6KCM7-6; Sequence=VSP_031067;
CC -!- TISSUE SPECIFICITY: Present in various cell lines (at protein level).
CC Widely expressed. Expressed in fetal and adult liver, skeletal muscle,
CC testis, ovary, hippocampus and caudate nucleus. Isoform 1 is present in
CC all tissues tested. Isoform 2 expression is restricted to kidney and
CC lung. {ECO:0000269|PubMed:15054102, ECO:0000269|PubMed:15123600}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB67789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ619989; CAF04495.1; -; mRNA.
DR EMBL; AJ619990; CAF04496.1; -; mRNA.
DR EMBL; AJ619991; CAF04497.1; -; mRNA.
DR EMBL; AJ619992; CAF04498.1; -; mRNA.
DR EMBL; AJ619963; CAF04060.1; -; mRNA.
DR EMBL; AB067483; BAB67789.1; ALT_INIT; mRNA.
DR EMBL; AY358515; AAQ88879.1; -; mRNA.
DR EMBL; AK290705; BAF83394.1; -; mRNA.
DR EMBL; AK290991; BAF83680.1; -; mRNA.
DR EMBL; CH471090; EAW87739.1; -; Genomic_DNA.
DR EMBL; AL360268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005163; AAH05163.2; -; mRNA.
DR EMBL; BC089448; AAH89448.1; -; mRNA.
DR EMBL; BC103930; AAI03931.1; -; mRNA.
DR EMBL; BC103931; AAI03932.1; -; mRNA.
DR EMBL; BC103932; AAI03933.1; -; mRNA.
DR EMBL; BC103933; AAI03934.1; -; mRNA.
DR CCDS; CCDS35151.1; -. [Q6KCM7-2]
DR CCDS; CCDS48031.1; -. [Q6KCM7-4]
DR CCDS; CCDS59146.1; -. [Q6KCM7-5]
DR CCDS; CCDS6890.1; -. [Q6KCM7-1]
DR CCDS; CCDS83420.1; -. [Q6KCM7-3]
DR RefSeq; NP_001006642.1; NM_001006641.3. [Q6KCM7-2]
DR RefSeq; NP_001006643.1; NM_001006642.3. [Q6KCM7-4]
DR RefSeq; NP_001252543.1; NM_001265614.2. [Q6KCM7-5]
DR RefSeq; NP_001317917.1; NM_001330988.1. [Q6KCM7-3]
DR RefSeq; NP_443133.2; NM_052901.4. [Q6KCM7-1]
DR RefSeq; XP_005251746.1; XM_005251689.4.
DR AlphaFoldDB; Q6KCM7; -.
DR SMR; Q6KCM7; -.
DR BioGRID; 125351; 56.
DR IntAct; Q6KCM7; 18.
DR MINT; Q6KCM7; -.
DR STRING; 9606.ENSP00000362159; -.
DR TCDB; 2.A.29.23.1; the mitochondrial carrier (mc) family.
DR iPTMnet; Q6KCM7; -.
DR PhosphoSitePlus; Q6KCM7; -.
DR BioMuta; SLC25A25; -.
DR DMDM; 74758042; -.
DR EPD; Q6KCM7; -.
DR jPOST; Q6KCM7; -.
DR MassIVE; Q6KCM7; -.
DR MaxQB; Q6KCM7; -.
DR PaxDb; Q6KCM7; -.
DR PeptideAtlas; Q6KCM7; -.
DR PRIDE; Q6KCM7; -.
DR ProteomicsDB; 66541; -. [Q6KCM7-1]
DR ProteomicsDB; 66542; -. [Q6KCM7-2]
DR ProteomicsDB; 66543; -. [Q6KCM7-3]
DR ProteomicsDB; 66544; -. [Q6KCM7-4]
DR ProteomicsDB; 66545; -. [Q6KCM7-5]
DR ProteomicsDB; 66546; -. [Q6KCM7-6]
DR Antibodypedia; 17304; 153 antibodies from 24 providers.
DR DNASU; 114789; -.
DR Ensembl; ENST00000373064.9; ENSP00000362155.5; ENSG00000148339.13. [Q6KCM7-1]
DR Ensembl; ENST00000373066.9; ENSP00000362157.5; ENSG00000148339.13. [Q6KCM7-5]
DR Ensembl; ENST00000373068.6; ENSP00000362159.2; ENSG00000148339.13. [Q6KCM7-2]
DR Ensembl; ENST00000373069.10; ENSP00000362160.5; ENSG00000148339.13. [Q6KCM7-3]
DR Ensembl; ENST00000432073.6; ENSP00000410053.2; ENSG00000148339.13. [Q6KCM7-4]
DR GeneID; 114789; -.
DR KEGG; hsa:114789; -.
DR MANE-Select; ENST00000373069.10; ENSP00000362160.5; NM_001330988.2; NP_001317917.1. [Q6KCM7-3]
DR UCSC; uc004btb.5; human. [Q6KCM7-1]
DR CTD; 114789; -.
DR DisGeNET; 114789; -.
DR GeneCards; SLC25A25; -.
DR HGNC; HGNC:20663; SLC25A25.
DR HPA; ENSG00000148339; Tissue enhanced (liver).
DR MalaCards; SLC25A25; -.
DR MIM; 608745; gene.
DR neXtProt; NX_Q6KCM7; -.
DR OpenTargets; ENSG00000148339; -.
DR PharmGKB; PA134952319; -.
DR VEuPathDB; HostDB:ENSG00000148339; -.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000157207; -.
DR HOGENOM; CLU_015166_2_0_1; -.
DR InParanoid; Q6KCM7; -.
DR OMA; DIWMQEG; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q6KCM7; -.
DR TreeFam; TF313492; -.
DR PathwayCommons; Q6KCM7; -.
DR SignaLink; Q6KCM7; -.
DR BioGRID-ORCS; 114789; 51 hits in 1077 CRISPR screens.
DR ChiTaRS; SLC25A25; human.
DR GenomeRNAi; 114789; -.
DR Pharos; Q6KCM7; Tbio.
DR PRO; PR:Q6KCM7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q6KCM7; protein.
DR Bgee; ENSG00000148339; Expressed in mucosa of stomach and 184 other tissues.
DR ExpressionAtlas; Q6KCM7; baseline and differential.
DR Genevisible; Q6KCM7; 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:0005347; F:ATP transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0045333; P:cellular respiration; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
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; PF13833; EF-hand_8; 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; 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..469
FT /note="Calcium-binding mitochondrial carrier protein SCaMC-
FT 2"
FT /id="PRO_0000317602"
FT TOPO_DOM 1..189
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..207
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..244
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..264
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..287
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..301
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..337
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..357
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..380
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..398
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..437
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..457
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..469
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 47..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..113
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 114..149
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 184..270
FT /note="Solcar 1"
FT REPEAT 278..363
FT /note="Solcar 2"
FT REPEAT 375..463
FT /note="Solcar 3"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15054102"
FT /id="VSP_031067"
FT VAR_SEQ 1..53
FT /note="MLCLCLYVPVIGEAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWK
FT Q -> MLQMLWHFLASFFPRAGCHGSREGDDREVRGTPAPAWRDQMASFLGKQDGRAEA
FT TEKRPTILLVVGPAEQFPK (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11572484,
FT ECO:0000303|PubMed:15054102, ECO:0000303|PubMed:15123600"
FT /id="VSP_031068"
FT VAR_SEQ 1..52
FT /note="MLCLCLYVPVIGEAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWK
FT -> MVSSVLCRCVASPPPDAAATAASSSASSPASVGDPCGGAICGGPDHRLRLWRLFQT
FT LDVNRDGGLCVNDLAVGLRRLGLHRTEGEL (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15054102"
FT /id="VSP_031069"
FT VAR_SEQ 125
FT /note="S -> RIRTGHFWGPVTY (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11572484"
FT /id="VSP_031070"
FT CONFLICT 89
FT /note="S -> I (in Ref. 4; AAQ88879)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="T -> Q (in Ref. 8; AAH05163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 52663 MW; A50825AA95DBD4BE CRC64;
MLCLCLYVPV IGEAQTEFQY FESKGLPAEL KSIFKLSVFI PSQEFSTYRQ WKQKIVQAGD
KDLDGQLDFE EFVHYLQDHE KKLRLVFKSL DKKNDGRIDA QEIMQSLRDL GVKISEQQAE
KILKSMDKNG TMTIDWNEWR DYHLLHPVEN IPEIILYWKH STIFDVGENL TVPDEFTVEE
RQTGMWWRHL VAGGGAGAVS RTCTAPLDRL KVLMQVHASR SNNMGIVGGF TQMIREGGAR
SLWRGNGINV LKIAPESAIK FMAYEQIKRL VGSDQETLRI HERLVAGSLA GAIAQSSIYP
MEVLKTRMAL RKTGQYSGML DCARRILARE GVAAFYKGYV PNMLGIIPYA GIDLAVYETL
KNAWLQHYAV NSADPGVFVL LACGTMSSTC GQLASYPLAL VRTRMQAQAS IEGAPEVTMS
SLFKHILRTE GAFGLYRGLA PNFMKVIPAV SISYVVYENL KITLGVQSR
