Q9BV35 (SCMC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcium-binding mitochondrial carrier protein SCaMC-3

Alternative name(s):
Mitochondrial ATP-Mg/Pi carrier protein 2
Mitochondrial Ca(2+)-dependent solute carrier protein 2
Small calcium-binding mitochondrial carrier protein 3
Solute carrier family 25 member 23

Gene names

Name:	SLC25A23
Synonyms:	APC2, MCSC2, SCAMC3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria. Ref.2
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein Ref.1 Ref.2 Ref.3.
Tissue specificity	Present in various cell lines (at protein level). Expressed at low levels in most tissues examined, with highest expression in brain, skeletal muscle and pancreas. Ref.1 Ref.2 Ref.3
Sequence similarities	Belongs to the mitochondrial carrier (TC 2.A.29) family. [View classification] Contains 3 EF-hand domains. Contains 3 Solcar repeats.
Biophysicochemical properties	Kinetic parameters: KM=1.3 mM for AMP Ref.2 KM=0.54 mM for ADP KM=0.31 mM for ATP KM=0.22 mM for ATP-Mg KM=1.4 mM for Pi Vmax=68 µmol/min/g enzyme with AMP as substrate Vmax=73 µmol/min/g enzyme with ADP as substrate Vmax=65 µmol/min/g enzyme with ATP as substrate Vmax=79 µmol/min/g enzyme with ATP-Mg as substrate Vmax=70 µmol/min/g enzyme with Pi as substrate
Sequence caution	The sequence BAB70825.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAC11071.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transmembrane transport Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BV35-1)

Also known as: SCaMC-3a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BV35-2)

Also known as: SCaMC-3b;

The sequence of this isoform differs from the canonical sequence as follows:
     408-468: ASIEGGPQLS...MKQALGVTSR → DVSVYKTDTVPTLIELTGRRGRKMLNKSFWN

Isoform 3 (identifier: Q9BV35-3)

Also known as: SCaMC-3c;

The sequence of this isoform differs from the canonical sequence as follows:
     161-161: T → TLSSAGFSAWIKDSTAEQNRSKTTVLARRSGSHLKSQHFGRPKWADHE
     408-468: ASIEGGPQLS...MKQALGVTSR → GWSTVARFQITATSAFQVQAILLPQPPE

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 4 (identifier: Q9BV35-4)

Also known as: SCaMC-3d;

The sequence of this isoform differs from the canonical sequence as follows:
     408-468: ASIEGGPQLS...MKQALGVTSR → GWSTVARFQITATSAFQVQAILLPQPPE

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	Calcium-binding mitochondrial carrier protein SCaMC-3		PRO_0000317609
Regions
	Topological domain	1 – 188	188	Mitochondrial intermembrane Potential
	Transmembrane	189 – 206	18	Helical; Name=1; Potential
	Topological domain	207 – 243	37	Mitochondrial matrix Potential
	Transmembrane	244 – 263	20	Helical; Name=2; Potential
	Topological domain	264 – 286	23	Mitochondrial intermembrane Potential
	Transmembrane	287 – 300	14	Helical; Name=3; Potential
	Topological domain	301 – 336	36	Mitochondrial matrix Potential
	Transmembrane	337 – 356	20	Helical; Name=4; Potential
	Topological domain	357 – 379	23	Mitochondrial intermembrane Potential
	Transmembrane	380 – 397	18	Helical; Name=5; Potential
	Topological domain	398 – 436	39	Mitochondrial matrix Potential
	Transmembrane	437 – 456	20	Helical; Name=6; Potential
	Topological domain	457 – 468	12	Mitochondrial intermembrane Potential
	Domain	9 – 44	36	EF-hand 1
	Domain	77 – 112	36	EF-hand 2
	Domain	113 – 148	36	EF-hand 3
	Repeat	183 – 269	87	Solcar 1
	Repeat	277 – 362	86	Solcar 2
	Repeat	374 – 462	89	Solcar 3
	Calcium binding	22 – 33	12	1 Potential
	Calcium binding	90 – 101	12	2 Potential
Natural variations
	Alternative sequence	161	1	T → TLSSAGFSAWIKDSTAEQNR SKTTVLARRSGSHLKSQHFG RPKWADHE in isoform 3.		VSP_031074
	Alternative sequence	408 – 468	61	ASIEG…GVTSR → DVSVYKTDTVPTLIELTGRR GRKMLNKSFWN in isoform 2.		VSP_031075
	Alternative sequence	408 – 468	61	ASIEG…GVTSR → GWSTVARFQITATSAFQVQA ILLPQPPE in isoform 3 and isoform 4.		VSP_031076

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SCaMC-3a) [UniParc]. Last modified February 5, 2008. Version 2. Checksum: B2D66A4665C27174	FASTA	468	52,378
	10 20 30 40 50 60 MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISSEGDA 70 80 90 100 110 120 DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISISLEQAEK 130 140 150 160 170 180 ILHSMDRDGT MTIDWQEWRD HFLLHSLENV EDVLYFWKHS TVLDIGECLT VPDEFSKQEK 190 200 210 220 230 240 LTGMWWKQLV AGAVAGAVSR TGTAPLDRLK VFMQVHASKT NRLNILGGLR SMVLEGGIRS 250 260 270 280 290 300 LWRGNGINVL KIAPESAIKF MAYEQIKRAI LGQQETLHVQ ERFVAGSLAG ATAQTIIYPM 310 320 330 340 350 360 EVLKTRLTLR RTGQYKGLLD CARRILEREG PRAFYRGYLP NVLGIIPYAG IDLAVYETLK 370 380 390 400 410 420 NWWLQQYSHD SADPGILVLL ACGTISSTCG QIASYPLALV RTRMQAQASI EGGPQLSMLG 430 440 450 460 LLRHILSQEG MRGLYRGIAP NFMKVIPAVS ISYVVYENMK QALGVTSR
	Isoform 2 (SCaMC-3b) [UniParc]. Checksum: 290DB81E953C5D3F	FASTA	438	49,354
	10 20 30 40 50 60 MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISSEGDA 70 80 90 100 110 120 DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISISLEQAEK 130 140 150 160 170 180 ILHSMDRDGT MTIDWQEWRD HFLLHSLENV EDVLYFWKHS TVLDIGECLT VPDEFSKQEK 190 200 210 220 230 240 LTGMWWKQLV AGAVAGAVSR TGTAPLDRLK VFMQVHASKT NRLNILGGLR SMVLEGGIRS 250 260 270 280 290 300 LWRGNGINVL KIAPESAIKF MAYEQIKRAI LGQQETLHVQ ERFVAGSLAG ATAQTIIYPM 310 320 330 340 350 360 EVLKTRLTLR RTGQYKGLLD CARRILEREG PRAFYRGYLP NVLGIIPYAG IDLAVYETLK 370 380 390 400 410 420 NWWLQQYSHD SADPGILVLL ACGTISSTCG QIASYPLALV RTRMQAQDVS VYKTDTVPTL 430 IELTGRRGRK MLNKSFWN
	Isoform 3 (SCaMC-3c) [UniParc]. Checksum: 8917BEA2BC2FE42B	FASTA	482	54,035
	10 20 30 40 50 60 MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISSEGDA 70 80 90 100 110 120 DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISISLEQAEK 130 140 150 160 170 180 ILHSMDRDGT MTIDWQEWRD HFLLHSLENV EDVLYFWKHS TLSSAGFSAW IKDSTAEQNR 190 200 210 220 230 240 SKTTVLARRS GSHLKSQHFG RPKWADHEVL DIGECLTVPD EFSKQEKLTG MWWKQLVAGA 250 260 270 280 290 300 VAGAVSRTGT APLDRLKVFM QVHASKTNRL NILGGLRSMV LEGGIRSLWR GNGINVLKIA 310 320 330 340 350 360 PESAIKFMAY EQIKRAILGQ QETLHVQERF VAGSLAGATA QTIIYPMEVL KTRLTLRRTG 370 380 390 400 410 420 QYKGLLDCAR RILEREGPRA FYRGYLPNVL GIIPYAGIDL AVYETLKNWW LQQYSHDSAD 430 440 450 460 470 480 PGILVLLACG TISSTCGQIA SYPLALVRTR MQAQGWSTVA RFQITATSAF QVQAILLPQP PE
	Isoform 4 (SCaMC-3d) [UniParc]. Checksum: DEE44DC4C31B7E9F	FASTA	435	48,786
	10 20 30 40 50 60 MRGSPGDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGGGNPDPGA QQGISSEGDA 70 80 90 100 110 120 DPDGGLDLEE FSRYLQEREQ RLLLMFHSLD RNQDGHIDVS EIQQSFRALG ISISLEQAEK 130 140 150 160 170 180 ILHSMDRDGT MTIDWQEWRD HFLLHSLENV EDVLYFWKHS TVLDIGECLT VPDEFSKQEK 190 200 210 220 230 240 LTGMWWKQLV AGAVAGAVSR TGTAPLDRLK VFMQVHASKT NRLNILGGLR SMVLEGGIRS 250 260 270 280 290 300 LWRGNGINVL KIAPESAIKF MAYEQIKRAI LGQQETLHVQ ERFVAGSLAG ATAQTIIYPM 310 320 330 340 350 360 EVLKTRLTLR RTGQYKGLLD CARRILEREG PRAFYRGYLP NVLGIIPYAG IDLAVYETLK 370 380 390 400 410 420 NWWLQQYSHD SADPGILVLL ACGTISSTCG QIASYPLALV RTRMQAQGWS TVARFQITAT 430 SAFQVQAILL PQPPE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel human subfamily of mitochondrial carriers with calcium-binding domains." del Arco A., Satrustegui J. J. Biol. Chem. 279:24701-24713(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution." Fiermonte G., De Leonardis F., Todisco S., Palmieri L., Lasorsa F.M., Palmieri F. J. Biol. Chem. 279:30722-30730(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Brain.
[3]	"Cellular expression and alternative splicing of SLC25A23, a member of the mitochondrial Ca2+-dependent solute carrier gene family." Bassi M.T., Manzoni M., Bresciani R., Pizzo M.T., Della Monica A., Barlati S., Monti E., Borsani G. Gene 345:173-182(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, CALCIUM-BINDING, TISSUE SPECIFICITY.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Amygdala, Cerebellum and Embryo.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Eye.
[7]	"Novel variants of human SCaMC-3, an isoform of the ATP-Mg/P(i) mitochondrial carrier, generated by alternative splicing from 3'-flanking transposable elements." Del Arco A. Biochem. J. 389:647-655(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-468 (ISOFORM 4), ALTERNATIVE SPLICING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ619988 mRNA. Translation: CAF04494.1. AJ619962 mRNA. Translation: CAF04059.1. AJ512835 mRNA. Translation: CAD55563.1. AY750170 mRNA. Translation: AAU95077.1. AK054901 mRNA. Translation: BAB70825.1. Different initiation. AK074579 mRNA. Translation: BAC11071.1. Different initiation. AK294514 mRNA. Translation: BAG57727.1. CH471139 Genomic DNA. Translation: EAW69087.1. CH471139 Genomic DNA. Translation: EAW69089.1. BC001656 mRNA. Translation: AAH01656.1. AJ879082 mRNA. Translation: CAI51684.1. AJ879083 mRNA. Translation: CAI51685.1.
IPI	IPI00419997. IPI00479721. IPI00884969. IPI00885199.
RefSeq	NP_077008.2. NM_024103.2.
UniGene	Hs.356231. Hs.732434.
3D structure databases
HSSP	HSSP built from PDB template 1K9U based on UniProtKB O82040.
ProteinModelPortal	Q9BV35.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BV35. 1 interaction.
STRING	9606.ENSP00000301454.
PTM databases
PhosphoSite	Q9BV35.
Polymorphism databases
DMDM	167016556.
Proteomic databases
PaxDb	Q9BV35.
PRIDE	Q9BV35.
Protocols and materials databases
DNASU	79085.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264088; ENSP00000264088; ENSG00000125648. ENST00000301454; ENSP00000301454; ENSG00000125648. ENST00000334510; ENSP00000334537; ENSG00000125648.
GeneID	79085.
KEGG	hsa:79085.
UCSC	uc002mex.1. human.
Organism-specific databases
CTD	79085.
GeneCards	GC19M006436.
H-InvDB	HIX0014698.
HGNC	HGNC:19375. SLC25A23.
HPA	HPA050883.
MIM	608746. gene.
neXtProt	NX_Q9BV35.
PharmGKB	PA134932456.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG316894.
HOVERGEN	HBG108464.
KO	K14684.
OMA	QIKWAIR.
Gene expression databases
ArrayExpress	Q9BV35.
Bgee	Q9BV35.
CleanEx	HS_APC2. HS_SLC25A23.
Genevestigator	Q9BV35.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 1.50.40.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR002067. Mit_carrier. IPR018108. Mitochondrial_sb/sol_carrier. IPR023395. Mt_carrier_dom. [Graphical view]
Pfam	PF13499. EF_hand_5. 2 hits. PF00153. Mito_carr. 3 hits. [Graphical view]
PRINTS	PR00926. MITOCARRIER.
SMART	SM00054. EFh. 3 hits. [Graphical view]
SUPFAM	SSF103506. Mitoch_carrier. 1 hit.
PROSITE	PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 3 hits. PS50920. SOLCAR. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	79085.
NextBio	67901.
SOURCE	Search...

Entry information

Entry name

SCMC3_HUMAN

Accession

Primary (citable) accession number: Q9BV35
Secondary accession number(s): B4DGB6 , Q4LBC2, Q705K3, Q86Y43, Q8N2N4, Q96NQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.