S238B_DANRE
ID S238B_DANRE Reviewed; 287 AA.
AC P0CAT2; I3IT61;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Mitochondrial glycine transporter B {ECO:0000255|HAMAP-Rule:MF_03064};
DE AltName: Full=Solute carrier family 25 member 38-B {ECO:0000255|HAMAP-Rule:MF_03064};
GN Name=slc25a38b;
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 DISRUPTION PHENOTYPE.
RX PubMed=19412178; DOI=10.1038/ng.359;
RA Guernsey D.L., Jiang H., Campagna D.R., Evans S.C., Ferguson M.,
RA Kellogg M.D., Lachance M., Matsuoka M., Nightingale M., Rideout A.,
RA Saint-Amant L., Schmidt P.J., Orr A., Bottomley S.S., Fleming M.D.,
RA Ludman M., Dyack S., Fernandez C.V., Samuels M.E.;
RT "Mutations in mitochondrial carrier family gene SLC25A38 cause nonsyndromic
RT autosomal recessive congenital sideroblastic anemia.";
RL Nat. Genet. 41:651-653(2009).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=26821380; DOI=10.1371/journal.pgen.1005783;
RA Fernandez-Murray J.P., Prykhozhij S.V., Dufay J.N., Steele S.L., Gaston D.,
RA Nasrallah G.K., Coombs A.J., Liwski R.S., Fernandez C.V., Berman J.N.,
RA McMaster C.R.;
RT "Glycine and folate ameliorate models of congenital sideroblastic anemia.";
RL PLoS Genet. 12:E1005783-E1005783(2016).
CC -!- FUNCTION: Mitochondrial glycine transporter that imports glycine into
CC the mitochondrial matrix. Plays an important role in providing glycine
CC for the first enzymatic step in heme biosynthesis, the condensation of
CC glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the
CC mitochondrial matrix. Required during erythropoiesis.
CC {ECO:0000255|HAMAP-Rule:MF_03064}.
CC -!- FUNCTION: May play a role as pro-apoptotic protein that induces
CC caspase-dependent apoptosis. {ECO:0000250|UniProtKB:Q91XD8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) = glycine(out); Xref=Rhea:RHEA:70715,
CC ChEBI:CHEBI:57305; Evidence={ECO:0000250|UniProtKB:Q96DW6};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03064}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03064}.
CC -!- TISSUE SPECIFICITY: At 24 hours post-fertilization, expressed
CC predominantly in posterior blood island, posterior cardinal vein and
CC circulating blood. At 34 hours post-fertilization, becomes restricted
CC to posterior blood island and circulating blood.
CC {ECO:0000269|PubMed:26821380}.
CC -!- DISRUPTION PHENOTYPE: Fishes lacking both slc25a38a and slc25a38b
CC display anemia. {ECO:0000269|PubMed:19412178}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC SLC25A38 subfamily. {ECO:0000255|HAMAP-Rule:MF_03064}.
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DR EMBL; CR925711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001189387.1; NM_001202458.1.
DR AlphaFoldDB; P0CAT2; -.
DR SMR; P0CAT2; -.
DR STRING; 7955.ENSDARP00000106419; -.
DR PaxDb; P0CAT2; -.
DR Ensembl; ENSDART00000151545; ENSDARP00000126117; ENSDARG00000074533.
DR GeneID; 571961; -.
DR KEGG; dre:571961; -.
DR CTD; 571961; -.
DR ZFIN; ZDB-GENE-110214-1; slc25a38b.
DR eggNOG; KOG0766; Eukaryota.
DR GeneTree; ENSGT00550000075117; -.
DR HOGENOM; CLU_015166_0_3_1; -.
DR InParanoid; P0CAT2; -.
DR PRO; PR:P0CAT2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000074533; Expressed in cleaving embryo and 28 other tissues.
DR ExpressionAtlas; P0CAT2; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:1904983; P:glycine import into mitochondrion; IBA:GO_Central.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; IGI:ZFIN.
DR GO; GO:0020027; P:hemoglobin metabolic process; IGI:ZFIN.
DR Gene3D; 1.50.40.10; -; 1.
DR HAMAP; MF_03064; SLC25A38; 1.
DR InterPro; IPR030847; Hem25/SLC25A38.
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..287
FT /note="Mitochondrial glycine transporter B"
FT /id="PRO_0000378921"
FT TRANSMEM 13..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 72..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 110..135
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 163..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 202..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT TRANSMEM 257..275
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 7..97
FT /note="Solcar 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 104..188
FT /note="Solcar 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT REPEAT 198..282
FT /note="Solcar 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
SQ SEQUENCE 287 AA; 30986 MW; DAD41466C96E5540 CRC64;
MEVALAHPAL KAFMCGSLSG TCSTLLFQPL DLVKTRLQTL QNNMHPGAPK VGMITVLFNV
IRTEKLLGLW KGVSPSFMRC IPGVGIYFST FYSLKQHYFQ EGSPSAGEAV LLGAGARCVA
GVAMLPFTVI KTRFESGRYN YISVAGALKS VCQNEGPKAL YSGLTATLLR DAPFSGIYVM
FYSQAKKALP QEISSSSIAP LVNFGCGVVA GILASLATQP ADVIKTHMQV SPALYPKTSD
AMRHVYVKHG LSGFFRGAVP RSLRRTLMAA MAWTVYEQLM ARMGLKS
