S238A_DANRE
ID S238A_DANRE Reviewed; 287 AA.
AC Q08CI8; F1QG50;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Mitochondrial glycine transporter A {ECO:0000255|HAMAP-Rule:MF_03064};
DE AltName: Full=Solute carrier family 25 member 38-A {ECO:0000255|HAMAP-Rule:MF_03064};
GN Name=slc25a38a; ORFNames=zgc:153036;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Intestine;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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, as well as in somites, brain and retina. At 34 hours
CC post-fertilization, becomes restricted to posterior blood island and
CC circulating blood. {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}.
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; CABZ01034848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01034849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC124222; AAI24223.1; -; mRNA.
DR RefSeq; NP_001070070.1; NM_001076602.1.
DR AlphaFoldDB; Q08CI8; -.
DR SMR; Q08CI8; -.
DR STRING; 7955.ENSDARP00000077967; -.
DR PaxDb; Q08CI8; -.
DR Ensembl; ENSDART00000083532; ENSDARP00000077967; ENSDARG00000059805.
DR GeneID; 767662; -.
DR KEGG; dre:767662; -.
DR CTD; 767662; -.
DR ZFIN; ZDB-GENE-060929-320; slc25a38a.
DR eggNOG; KOG0766; Eukaryota.
DR GeneTree; ENSGT00550000075117; -.
DR HOGENOM; CLU_015166_0_3_1; -.
DR InParanoid; Q08CI8; -.
DR OMA; YMEHGLQ; -.
DR OrthoDB; 1531343at2759; -.
DR PhylomeDB; Q08CI8; -.
DR TreeFam; TF332793; -.
DR PRO; PR:Q08CI8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000059805; Expressed in liver and 23 other tissues.
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 A"
FT /id="PRO_0000291805"
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"
FT CONFLICT 41
FT /note="Q -> H (in Ref. 2; AAI24223)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="R -> H (in Ref. 2; AAI24223)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="H -> N (in Ref. 2; AAI24223)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="I -> M (in Ref. 2; AAI24223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 31161 MW; 1429A9E8EB10C528 CRC64;
MEFSVAHPAV KAFMCGSLSG TCSTLLFQPL DLVKTRLQTL QSGVQPGTGR VGMVTVFVNV
LRTEKLLGLW RGVSPSFVRC IPGVGIYFST YFTLKQRYFS SGAPGPLQAV LLGAGARCVA
GVFMLPVTVI KTRFESGRYR YSGVFGALRS VCQTEGPKAL FSGLMATLLR DAPFSGIYVM
IYSQTKHLLP PEISQSSYAP VANFSCGVLA GVLASVLTQP ADVVKTHIQV SPDVFSRTSD
VVRYIYKEHG LVGFFRGAVP RSLRRTMMAA MAWTVYEQLM AQIGLKS
