S2544_MOUSE
ID S2544_MOUSE Reviewed; 314 AA.
AC Q8BGF9; Q7TSU9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Solute carrier family 25 member 44 {ECO:0000305};
GN Name=Slc25a44 {ECO:0000303|PubMed:31435015, ECO:0000312|MGI:MGI:2444391};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Hippocampus, and Wolffian duct;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY COLD, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=31435015; DOI=10.1038/s41586-019-1503-x;
RA Yoneshiro T., Wang Q., Tajima K., Matsushita M., Maki H., Igarashi K.,
RA Dai Z., White P.J., McGarrah R.W., Ilkayeva O.R., Deleye Y., Oguri Y.,
RA Kuroda M., Ikeda K., Li H., Ueno A., Ohishi M., Ishikawa T., Kim K.,
RA Chen Y., Sponton C.H., Pradhan R.N., Majd H., Greiner V.J., Yoneshiro M.,
RA Brown Z., Chondronikola M., Takahashi H., Goto T., Kawada T., Sidossis L.,
RA Szoka F.C., McManus M.T., Saito M., Soga T., Kajimura S.;
RT "BCAA catabolism in brown fat controls energy homeostasis through
RT SLC25A44.";
RL Nature 572:614-619(2019).
CC -!- FUNCTION: Mitochondrial solute transporter which transports branched-
CC chain amino acid (BCAA; valine, leucine and isoleucine) into
CC mitochondria in brown adipose tissue (BAT) (PubMed:31435015). BAT is
CC involved in BCAA catabolism and actively utilizes BCAA in the
CC mitochondria for thermogenesis (PubMed:31435015).
CC {ECO:0000269|PubMed:31435015}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000305|PubMed:31435015}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brown adipose tissues compared
CC with other metabolic organs. {ECO:0000269|PubMed:31435015}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during adipogenesis.
CC {ECO:0000269|PubMed:31435015}.
CC -!- INDUCTION: Induction by cold exposure in brown adipose tissues.
CC {ECO:0000269|PubMed:31435015}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000255}.
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DR EMBL; AK032960; BAC28100.1; -; mRNA.
DR EMBL; AK046586; BAC32798.1; -; mRNA.
DR EMBL; AK083273; BAC38838.1; -; mRNA.
DR EMBL; AK083470; BAC38927.1; -; mRNA.
DR EMBL; BC052771; AAH52771.2; -; mRNA.
DR CCDS; CCDS79943.1; -.
DR RefSeq; NP_001139348.1; NM_001145876.2.
DR RefSeq; NP_001139349.1; NM_001145877.2.
DR RefSeq; NP_001268724.1; NM_001281795.1.
DR AlphaFoldDB; Q8BGF9; -.
DR SMR; Q8BGF9; -.
DR STRING; 10090.ENSMUSP00000057871; -.
DR iPTMnet; Q8BGF9; -.
DR PhosphoSitePlus; Q8BGF9; -.
DR MaxQB; Q8BGF9; -.
DR PaxDb; Q8BGF9; -.
DR PRIDE; Q8BGF9; -.
DR ProteomicsDB; 260765; -.
DR Antibodypedia; 47042; 26 antibodies from 11 providers.
DR DNASU; 229517; -.
DR Ensembl; ENSMUST00000193433; ENSMUSP00000141465; ENSMUSG00000050144.
DR Ensembl; ENSMUST00000195657; ENSMUSP00000141780; ENSMUSG00000050144.
DR GeneID; 229517; -.
DR KEGG; mmu:229517; -.
DR UCSC; uc008pvc.3; mouse.
DR CTD; 9673; -.
DR MGI; MGI:2444391; Slc25a44.
DR VEuPathDB; HostDB:ENSMUSG00000050144; -.
DR eggNOG; KOG0765; Eukaryota.
DR GeneTree; ENSGT00940000155399; -.
DR InParanoid; Q8BGF9; -.
DR PhylomeDB; Q8BGF9; -.
DR BioGRID-ORCS; 229517; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Slc25a44; mouse.
DR PRO; PR:Q8BGF9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BGF9; protein.
DR Bgee; ENSMUSG00000050144; Expressed in dentate gyrus of hippocampal formation granule cell and 251 other tissues.
DR ExpressionAtlas; Q8BGF9; baseline and differential.
DR Genevisible; Q8BGF9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0015658; F:branched-chain amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IMP:UniProtKB.
DR GO; GO:0015803; P:branched-chain amino acid transport; IDA:UniProtKB.
DR GO; GO:0120161; P:regulation of cold-induced thermogenesis; IMP:UniProtKB.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR042164; SLC25A44.
DR PANTHER; PTHR46314; PTHR46314; 1.
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 Amino-acid transport; Membrane; Mitochondrion; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..314
FT /note="Solute carrier family 25 member 44"
FT /id="PRO_0000253065"
FT TRANSMEM 20..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..201
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..296
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 18..100
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 107..210
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 220..302
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 314 AA; 35339 MW; 9CA4C54D7C23A2AE CRC64;
MEDKRNIQII EWEHLDKKKF YVFGVAMTMM IRVSVYPFTL IRTRLQVQKG KSLYHGTFDA
FVKILRADGV AGLYRGFLVN TFTLISGQCY VTTYELTRKF VADYSQSNTV KSLVAGGSAS
LVAQSITVPI DVVSQHLMMQ RKGEKMGRFQ VHGNLEGQGV IAFGQTKDII RQILRADGLR
GFYRGYVASL LTYIPNSAVW WPFYHFYAEQ LSRLCPQECP HIVFQAISGP LAAATASILT
NPMDVIRTRV QVEGKSSIVL TFRQLMAEEG PWGLMKGLSA RIISATPSTI VIVVGYESLK
KLSLRPELVD SRHW
