KMCP1_HUMAN
ID KMCP1_HUMAN Reviewed; 291 AA.
AC Q5SVS4; B2RN96; B4DZK3; F5H8H8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Kidney mitochondrial carrier protein 1;
DE AltName: Full=Solute carrier family 25 member 30;
GN Name=SLC25A30; Synonyms=KMCP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP INTERACTION WITH VDAC1.
RX PubMed=26387735; DOI=10.1016/j.molcel.2015.08.009;
RA Shanmughapriya S., Rajan S., Hoffman N.E., Higgins A.M., Tomar D.,
RA Nemani N., Hines K.J., Smith D.J., Eguchi A., Vallem S., Shaikh F.,
RA Cheung M., Leonard N.J., Stolakis R.S., Wolfers M.P., Ibetti J.,
RA Chuprun J.K., Jog N.R., Houser S.R., Koch W.J., Elrod J.W., Madesh M.;
RT "SPG7 is an essential and conserved component of the mitochondrial
RT permeability transition pore.";
RL Mol. Cell 60:47-62(2015).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Probable transporter. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VDAC1. {ECO:0000269|PubMed:26387735}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SVS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SVS4-2; Sequence=VSP_053984;
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; AK302967; BAG64115.1; -; mRNA.
DR EMBL; AL627107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132739; AAI32740.1; -; mRNA.
DR EMBL; BC136760; AAI36761.1; -; mRNA.
DR CCDS; CCDS31967.1; -. [Q5SVS4-1]
DR CCDS; CCDS66539.1; -. [Q5SVS4-2]
DR RefSeq; NP_001010875.1; NM_001010875.3. [Q5SVS4-1]
DR RefSeq; NP_001273735.1; NM_001286806.1. [Q5SVS4-2]
DR RefSeq; XP_016876013.1; XM_017020524.1. [Q5SVS4-1]
DR AlphaFoldDB; Q5SVS4; -.
DR SMR; Q5SVS4; -.
DR BioGRID; 128971; 40.
DR IntAct; Q5SVS4; 10.
DR STRING; 9606.ENSP00000429168; -.
DR TCDB; 2.A.29.24.4; the mitochondrial carrier (mc) family.
DR GlyGen; Q5SVS4; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q5SVS4; -.
DR PhosphoSitePlus; Q5SVS4; -.
DR BioMuta; SLC25A30; -.
DR DMDM; 74743890; -.
DR EPD; Q5SVS4; -.
DR jPOST; Q5SVS4; -.
DR MassIVE; Q5SVS4; -.
DR MaxQB; Q5SVS4; -.
DR PaxDb; Q5SVS4; -.
DR PeptideAtlas; Q5SVS4; -.
DR PRIDE; Q5SVS4; -.
DR ProteomicsDB; 27787; -.
DR ProteomicsDB; 63953; -. [Q5SVS4-1]
DR Antibodypedia; 49461; 15 antibodies from 6 providers.
DR DNASU; 253512; -.
DR Ensembl; ENST00000519676.6; ENSP00000429168.1; ENSG00000174032.17. [Q5SVS4-1]
DR Ensembl; ENST00000539591.5; ENSP00000443542.1; ENSG00000174032.17. [Q5SVS4-2]
DR GeneID; 253512; -.
DR KEGG; hsa:253512; -.
DR MANE-Select; ENST00000519676.6; ENSP00000429168.1; NM_001010875.4; NP_001010875.1.
DR UCSC; uc001vag.5; human. [Q5SVS4-1]
DR CTD; 253512; -.
DR DisGeNET; 253512; -.
DR GeneCards; SLC25A30; -.
DR HGNC; HGNC:27371; SLC25A30.
DR HPA; ENSG00000174032; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MIM; 610793; gene.
DR neXtProt; NX_Q5SVS4; -.
DR OpenTargets; ENSG00000174032; -.
DR PharmGKB; PA134931353; -.
DR VEuPathDB; HostDB:ENSG00000174032; -.
DR eggNOG; KOG0753; Eukaryota.
DR GeneTree; ENSGT00940000158961; -.
DR HOGENOM; CLU_015166_14_2_1; -.
DR InParanoid; Q5SVS4; -.
DR OMA; KRMFVEH; -.
DR OrthoDB; 1126848at2759; -.
DR PhylomeDB; Q5SVS4; -.
DR TreeFam; TF323211; -.
DR PathwayCommons; Q5SVS4; -.
DR SignaLink; Q5SVS4; -.
DR BioGRID-ORCS; 253512; 9 hits in 1035 CRISPR screens.
DR ChiTaRS; SLC25A30; human.
DR GenomeRNAi; 253512; -.
DR Pharos; Q5SVS4; Tdark.
DR PRO; PR:Q5SVS4; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5SVS4; protein.
DR Bgee; ENSG00000174032; Expressed in biceps brachii and 166 other tissues.
DR ExpressionAtlas; Q5SVS4; baseline and differential.
DR Genevisible; Q5SVS4; HS.
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: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:0006839; P:mitochondrial transport; IEA:InterPro.
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; IPR002030; Mit_uncoupling_UCP-like.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00784; MTUNCOUPLING.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..291
FT /note="Kidney mitochondrial carrier protein 1"
FT /id="PRO_0000288916"
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 105..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:0007744|PubMed:25944712"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053984"
FT CONFLICT 204
FT /note="F -> L (in Ref. 1; BAG64115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32475 MW; 76A8A6F087454B7F CRC64;
MSALNWKPFV YGGLASITAE CGTFPIDLTK TRLQIQGQTN DAKFKEIRYR GMLHALVRIG
REEGLKALYS GIAPAMLRQA SYGTIKIGTY QSLKRLFIER PEDETLPINV ICGILSGVIS
STIANPTDVL KIRMQAQSNT IQGGMIGNFM NIYQQEGTRG LWKGVSLTAQ RAAIVVGVEL
PVYDITKKHL ILSGLMGDTV YTHFLSSFTC GLAGALASNP VDVVRTRMMN QRVLRDGRCS
GYTGTLDCLL QTWKNEGFFA LYKGFWPNWL RLGPWNIIFF VTYEQLKKLD L
