S2541_RAT
ID S2541_RAT Reviewed; 312 AA.
AC B8ZHC9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 96.
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|RGD:1588585};
GN ORFNames=rCG_45007 {ECO:0000312|EMBL:EDL83587.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q8BVN7}.
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:0000250|UniProtKB:Q8BVN7};
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:0000250|UniProtKB:Q8BVN7};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q8BVN7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O94502}.
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}.
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DR EMBL; FM165287; CAQ63320.1; -; mRNA.
DR EMBL; AABR07066515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474092; EDL83587.1; -; Genomic_DNA.
DR RefSeq; NP_001100344.1; NM_001106874.1.
DR AlphaFoldDB; B8ZHC9; -.
DR SMR; B8ZHC9; -.
DR STRING; 10116.ENSRNOP00000064251; -.
DR PaxDb; B8ZHC9; -.
DR PeptideAtlas; B8ZHC9; -.
DR Ensembl; ENSRNOT00000074117; ENSRNOP00000064251; ENSRNOG00000048853.
DR GeneID; 301114; -.
DR KEGG; rno:301114; -.
DR CTD; 284427; -.
DR RGD; 1588585; Slc25a41.
DR eggNOG; KOG0036; Eukaryota.
DR GeneTree; ENSGT00940000162419; -.
DR HOGENOM; CLU_015166_10_2_1; -.
DR InParanoid; B8ZHC9; -.
DR OMA; VHESPPF; -.
DR OrthoDB; 442523at2759; -.
DR PhylomeDB; B8ZHC9; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Proteomes; UP000234681; Chromosome 9.
DR Bgee; ENSRNOG00000048853; Expressed in testis.
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:UniProtKB.
DR GO; GO:0015217; F:ADP transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015866; P:ADP transport; ISS:UniProtKB.
DR GO; GO:0015867; P:ATP transport; ISS:UniProtKB.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; ISS:UniProtKB.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; ISS: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 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..312
FT /note="Calcium-independent mitochondrial carrier protein
FT SCaMC-3L"
FT /id="PRO_0000451985"
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|PROSITE-ProRule:PRU00282"
FT REPEAT 121..206
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 217..304
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 312 AA; 34557 MW; 1B59EB0B7E9794AA CRC64;
MGVHLEVLDT GEQLMVPGDV LEEENKGTLW KFLLSGAMAG AVSRTGTAPL DRARVYMQVY
SSKSNFRHLL SGLRSLVQEG GIRSLWRGNG INVLKIAPEY AIKFSVFEQS RNFFYGVHTS
PSFQERVVAG SLAVAISQTL INPMEVLKTR LTLRFTGQYK GLLDCARQIL ERDGTRALYR
GYLPNMLGII PYACTDLAVY ELLRCLWQKS GRDMKDPSGL VSLSSVTLST TCGQMASYPL
TLVRTRMQAQ DTVEGSNPTM LGVFKRILNQ QGWPGLYRGM TPTLLKVLPA GGISYLVYEA
MKKTLGVQVL SR
