KMCP1_MOUSE
ID KMCP1_MOUSE Reviewed; 291 AA.
AC Q9CR58; Q3UAD0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Kidney mitochondrial carrier protein 1;
DE AltName: Full=Solute carrier family 25 member 30;
GN Name=Slc25a30; Synonyms=Kmcp1;
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=Bone marrow, and Testis;
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 SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15809292; DOI=10.1074/jbc.m412136200;
RA Haguenauer A., Raimbault S., Masscheleyn S., del Mar Gonzalez-Barroso M.,
RA Criscuolo F., Plamondon J., Miroux B., Ricquier D., Richard D.,
RA Bouillaud F., Pecqueur C.;
RT "A new renal mitochondrial carrier, KMCP1, is up-regulated during tubular
RT cell regeneration and induction of antioxidant enzymes.";
RL J. Biol. Chem. 280:22036-22043(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Testis;
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).
CC -!- FUNCTION: Probable transporter. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VDAC1. {ECO:0000250|UniProtKB:Q5SVS4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15809292}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15809292}.
CC -!- TISSUE SPECIFICITY: Present in kidney (at protein level). Expressed
CC predominantly within the kidney cortex in the proximal and distal
CC tubules and at lower levels in the testis and white adipose tissue.
CC {ECO:0000269|PubMed:15809292}.
CC -!- INDUCTION: Up-regulated during fasting and in the regenerative phase
CC following renal tubular injury. {ECO:0000269|PubMed:15809292}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AK015679; BAB29928.1; -; mRNA.
DR EMBL; AK017035; BAB30563.1; -; mRNA.
DR EMBL; AK151334; BAE30312.1; -; mRNA.
DR EMBL; AK151420; BAE30385.1; -; mRNA.
DR EMBL; AK159122; BAE34837.1; -; mRNA.
DR EMBL; AK159732; BAE35326.1; -; mRNA.
DR CCDS; CCDS27281.1; -.
DR RefSeq; NP_080508.1; NM_026232.3.
DR AlphaFoldDB; Q9CR58; -.
DR SMR; Q9CR58; -.
DR BioGRID; 212273; 1.
DR STRING; 10090.ENSMUSP00000022580; -.
DR TCDB; 2.A.29.24.2; the mitochondrial carrier (mc) family.
DR PhosphoSitePlus; Q9CR58; -.
DR EPD; Q9CR58; -.
DR MaxQB; Q9CR58; -.
DR PaxDb; Q9CR58; -.
DR PRIDE; Q9CR58; -.
DR ProteomicsDB; 264785; -.
DR Antibodypedia; 49461; 15 antibodies from 6 providers.
DR DNASU; 67554; -.
DR Ensembl; ENSMUST00000022580; ENSMUSP00000022580; ENSMUSG00000022003.
DR GeneID; 67554; -.
DR KEGG; mmu:67554; -.
DR UCSC; uc007uqx.1; mouse.
DR CTD; 253512; -.
DR MGI; MGI:1914804; Slc25a30.
DR VEuPathDB; HostDB:ENSMUSG00000022003; -.
DR eggNOG; KOG0753; Eukaryota.
DR GeneTree; ENSGT00940000158961; -.
DR HOGENOM; CLU_015166_14_2_1; -.
DR InParanoid; Q9CR58; -.
DR OMA; KRMFVEH; -.
DR OrthoDB; 1126848at2759; -.
DR PhylomeDB; Q9CR58; -.
DR TreeFam; TF323211; -.
DR BioGRID-ORCS; 67554; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Slc25a30; mouse.
DR PRO; PR:Q9CR58; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CR58; protein.
DR Bgee; ENSMUSG00000022003; Expressed in cumulus cell and 246 other tissues.
DR ExpressionAtlas; Q9CR58; baseline and differential.
DR Genevisible; Q9CR58; 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:BHF-UCL.
DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
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 Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5SVS4"
FT CHAIN 2..291
FT /note="Kidney mitochondrial carrier protein 1"
FT /id="PRO_0000288918"
FT TRANSMEM 9..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..283
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 7..96
FT /note="Solcar 1"
FT REPEAT 104..189
FT /note="Solcar 2"
FT REPEAT 198..289
FT /note="Solcar 3"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SVS4"
FT CONFLICT 17
FT /note="I -> M (in Ref. 1; BAE30385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32282 MW; 1CD3138F9FF27B99 CRC64;
MSALNWKPFV YGGLASITAE CGTFPIDLTK TRLQIQGQTN DANFREIRYR GMLHALMRIG
REEGLKALYS GIAPAMLRQA SYGTIKIGTY QSLKRLAVER PEDETLLVNV VCGILSGVIS
SAIANPTDVL KIRMQAQNSA VQGGMIDSFM SIYQQEGTRG LWKGVSLTAQ RAAIVVGVEL
PVYDITKKHL ILSGLMGDTV ATHFLSSFTC GLVGALASNP VDVVRTRMMN QRALRDGRCA
GYKGTLDCLL QTWKNEGFFA LYKGFWPNWL RLGPWNIIFF LTYEQLKKLD L
