S2541_MOUSE
ID S2541_MOUSE Reviewed; 312 AA.
AC Q8BVN7; B8ZHC8; Q14BV4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Calcium-independent mitochondrial carrier protein SCaMC-3L {ECO:0000305};
DE AltName: Full=Mitochondrial ATP-Mg/Pi carrier protein SLC25A41 {ECO:0000305};
DE AltName: Full=Small calcium-binding mitochondrial carrier protein 3-like;
DE Short=SCaMC-3-like {ECO:0000303|PubMed:18928449};
DE Short=SCaMC-3L {ECO:0000303|PubMed:18928449};
DE AltName: Full=Solute carrier family 25 member 41;
GN Name=Slc25a41 {ECO:0000312|MGI:MGI:2144215}; Synonyms=SCaMC3L;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, FUNCTION, AND TRANSPORTER ACTIVITY.
RC TISSUE=Testis;
RX PubMed=18928449; DOI=10.1042/bj20081262;
RA Traba J., Satrustegui J., del Arco A.;
RT "Characterization of SCaMC-3-like/slc25a41, a novel calcium-independent
RT mitochondrial ATP-Mg/Pi carrier.";
RL Biochem. J. 418:125-133(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC36618.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36618.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC36618.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI15590.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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-independent ATP-Mg/Pi exchanger that catalyzes the
CC electroneutral exchange of Mg-ATP or free ADP against an
CC hydrogenphosphate and participates in the net transport of adenine
CC nucleotides across the mitochondria inner membrane.
CC {ECO:0000269|PubMed:18928449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in)
CC + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000269|PubMed:18928449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(out) + phosphate(in) = ADP(in) + phosphate(out);
CC Xref=Rhea:RHEA:65844, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:18928449};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for ATP {ECO:0000269|PubMed:18928449};
CC KM=0.9 mM for ADP {ECO:0000269|PubMed:18928449};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18928449}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O94502}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q8BVN7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8BVN7-2; Sequence=VSP_052684;
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis and at lesser levels in
CC brain. {ECO:0000269|PubMed:18928449}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM165286; CAQ63319.1; -; mRNA.
DR EMBL; AK077111; BAC36618.1; -; mRNA.
DR EMBL; BC115588; AAI15589.1; -; mRNA.
DR EMBL; BC115589; AAI15590.1; -; mRNA.
DR CCDS; CCDS37668.1; -. [Q8BVN7-1]
DR CCDS; CCDS84326.1; -. [Q8BVN7-2]
DR RefSeq; NP_001333456.1; NM_001346527.1. [Q8BVN7-2]
DR RefSeq; NP_780542.1; NM_175333.3. [Q8BVN7-1]
DR AlphaFoldDB; Q8BVN7; -.
DR SMR; Q8BVN7; -.
DR STRING; 10090.ENSMUSP00000058877; -.
DR PhosphoSitePlus; Q8BVN7; -.
DR MaxQB; Q8BVN7; -.
DR PaxDb; Q8BVN7; -.
DR PRIDE; Q8BVN7; -.
DR ProteomicsDB; 256669; -. [Q8BVN7-1]
DR ProteomicsDB; 256670; -. [Q8BVN7-2]
DR Antibodypedia; 49970; 21 antibodies from 10 providers.
DR DNASU; 103775; -.
DR Ensembl; ENSMUST00000058661; ENSMUSP00000058877; ENSMUSG00000011486. [Q8BVN7-1]
DR Ensembl; ENSMUST00000169012; ENSMUSP00000130857; ENSMUSG00000011486. [Q8BVN7-2]
DR GeneID; 103775; -.
DR KEGG; mmu:103775; -.
DR UCSC; uc008dds.1; mouse. [Q8BVN7-1]
DR CTD; 284427; -.
DR MGI; MGI:2144215; Slc25a41.
DR VEuPathDB; HostDB:ENSMUSG00000011486; -.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000162419; -.
DR HOGENOM; CLU_015166_10_2_1; -.
DR InParanoid; Q8BVN7; -.
DR OMA; VHESPPF; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; Q8BVN7; -.
DR TreeFam; TF313492; -.
DR BioGRID-ORCS; 103775; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BVN7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BVN7; protein.
DR Bgee; ENSMUSG00000011486; Expressed in spermatid and 16 other tissues.
DR ExpressionAtlas; Q8BVN7; baseline and differential.
DR Genevisible; Q8BVN7; MM.
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:UniProtKB.
DR GO; GO:0015217; F:ADP transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015866; P:ADP transport; IMP:UniProtKB.
DR GO; GO:0015867; P:ATP transport; IMP:UniProtKB.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IMP:UniProtKB.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IMP:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..312
FT /note="Calcium-independent mitochondrial carrier protein
FT SCaMC-3L"
FT /id="PRO_0000319991"
FT TRANSMEM 33..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..107
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..200
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 27..113
FT /note="Solcar 1"
FT /evidence="ECO:0000255"
FT REPEAT 121..206
FT /note="Solcar 2"
FT /evidence="ECO:0000255"
FT REPEAT 217..304
FT /note="Solcar 3"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052684"
SQ SEQUENCE 312 AA; 34505 MW; D20226711BA6877C CRC64;
MGVHLEVLDT GEQLMVPVDV LEEENKGTLW KFLLSGAMAG AVSRTGTAPL DRARVYMQVY
SSKSNFRNLL SGLRSLVQEG GVRSLWRGNG INVLKIAPEY AIKFSVCEQS KNFFYGVHSS
QLFQERVVAG SLAVAVSQTL INPMEVLKTR LTLRFTGQYK GLLDCARQIL ERDGTRALYR
GYLPNMLGII PYACTDLAVY ELLQCLWQKL GRDMKDPSGL VSLSSVTLST TCGQMASYPL
TLVRTRMQAQ DTVEGSNPTM QGVFKRILSQ QGWPGLYRGM TPTLLKVLPA GGISYLVYEA
MKKTLGVQVL SR
