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TXTPB_DANRE
ID   TXTPB_DANRE             Reviewed;         317 AA.
AC   F1R4U0;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Tricarboxylate transport protein B, mitochondrial {ECO:0000250|UniProtKB:P53007};
DE   AltName: Full=Citrate transport protein B {ECO:0000250|UniProtKB:P53007};
DE   AltName: Full=Solute carrier family 25 member 1b;
DE   Flags: Precursor;
GN   Name=slc25a1b {ECO:0000312|ZFIN:ZDB-GENE-130114-1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26870663; DOI=10.3233/jnd-140021;
RA   Chaouch A., Porcelli V., Cox D., Edvardson S., Scarcia P., De Grassi A.,
RA   Pierri C.L., Cossins J., Laval S.H., Griffin H., Mueller J.S.,
RA   Evangelista T., Toepf A., Abicht A., Huebner A., von der Hagen M.,
RA   Bushby K., Straub V., Horvath R., Elpeleg O., Palace J., Senderek J.,
RA   Beeson D., Palmieri L., Lochmueller H.;
RT   "Mutations in the mitochondrial citrate carrier SLC25A1 are associated with
RT   impaired neuromuscular transmission.";
RL   J. Neuromuscul. Dis. 1:75-90(2014).
CC   -!- FUNCTION: Citrate transporter that mediates the exchange of
CC       mitochondrial citrate for cytosolic malate (By similarity). Required
CC       for proper neuromuscular junction formation (PubMed:26870663).
CC       {ECO:0000250|UniProtKB:P53007, ECO:0000269|PubMed:26870663}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q8JZU2}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino-injected embryos display altered tail
CC       morphology, impaired swimming and defective touch-evoked escape
CC       responses. Neuromuscular junction development is abnormal and motor
CC       axon terminals show short and erratic outgrowth toward the muscle fiber
CC       with no evidence of complete synapse formation. In addition, knockdown
CC       embryos often show edema of the hindbrain, heart, yolk sac and tail.
CC       {ECO:0000269|PubMed:26870663}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000255, ECO:0000255|RuleBase:RU000488}.
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DR   EMBL; CR450714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001313457.1; NM_001326528.1.
DR   AlphaFoldDB; F1R4U0; -.
DR   SMR; F1R4U0; -.
DR   STRING; 7955.ENSDARP00000104198; -.
DR   PaxDb; F1R4U0; -.
DR   Ensembl; ENSDART00000109131; ENSDARP00000104198; ENSDARG00000076381.
DR   GeneID; 795332; -.
DR   KEGG; dre:795332; -.
DR   CTD; 795332; -.
DR   ZFIN; ZDB-GENE-130114-1; slc25a1b.
DR   eggNOG; KOG0756; Eukaryota.
DR   GeneTree; ENSGT00550000074856; -.
DR   HOGENOM; CLU_015166_5_1_1; -.
DR   InParanoid; F1R4U0; -.
DR   OMA; CPAFIVG; -.
DR   OrthoDB; 1523221at2759; -.
DR   TreeFam; TF105786; -.
DR   Reactome; R-DRE-70263; Gluconeogenesis.
DR   Reactome; R-DRE-75105; Fatty acyl-CoA biosynthesis.
DR   PRO; PR:F1R4U0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 10.
DR   Bgee; ENSDARG00000076381; Expressed in liver and 18 other tissues.
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; IBA:GO_Central.
DR   GO; GO:0071913; F:citrate secondary active transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006843; P:mitochondrial citrate transmembrane transport; IBA:GO_Central.
DR   GO; GO:0007528; P:neuromuscular junction development; IGI:ZFIN.
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   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..317
FT                   /note="Tricarboxylate transport protein B, mitochondrial"
FT                   /id="PRO_0000447227"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          29..117
FT                   /note="Solcar"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          128..214
FT                   /note="Solcar"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          224..309
FT                   /note="Solcar"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   317 AA;  34345 MW;  4E32FCBCF37DC5A1 CRC64;
     MSGSPKFVSP FHRPHCLSAA APAGQAKLTH PGKAILAGGI AGGIEICITF PTEYVKTQLQ
     LDEKANPPRY KGIVDCVKQT VQGHGVKGLY RGLSSLLYGS IPKAAVRFGV FEFLSNQMRD
     ESGKLDSTRG LICGLGAGVA EAVVVVCPME TVKVKFIHDQ TSANPKYRGF FHGVREIVRT
     QGLKGTYQGL TATVLKQGSN QAIRFYVMTA LRNWYKGDNP NKSINPVVTG LFGAVAGAAS
     VFGNTPLDVI KTRMQGLEAH KYKSTVDCAI KIMKYEGPAA FYKGTVPRLG RVCMDVAIVF
     IIYEEVVKVL NKVWKTD
 
 
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