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S2538_PICGU
ID   S2538_PICGU             Reviewed;         317 AA.
AC   A5D9W9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Mitochondrial glycine transporter {ECO:0000255|HAMAP-Rule:MF_03064};
DE   AltName: Full=Solute carrier family 25 member 38 homolog {ECO:0000255|HAMAP-Rule:MF_03064};
GN   ORFNames=PGUG_00074;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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. {ECO:0000255|HAMAP-Rule:MF_03064}.
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   -!- 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; CH408155; EDK35976.2; -; Genomic_DNA.
DR   RefSeq; XP_001486697.1; XM_001486647.1.
DR   AlphaFoldDB; A5D9W9; -.
DR   SMR; A5D9W9; -.
DR   STRING; 4929.XP_001486697.1; -.
DR   EnsemblFungi; EDK35976; EDK35976; PGUG_00074.
DR   GeneID; 5128750; -.
DR   KEGG; pgu:PGUG_00074; -.
DR   VEuPathDB; FungiDB:PGUG_00074; -.
DR   eggNOG; KOG0766; Eukaryota.
DR   HOGENOM; CLU_015166_0_3_1; -.
DR   InParanoid; A5D9W9; -.
DR   OMA; IRDAPYA; -.
DR   OrthoDB; 1531343at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015187; F:glycine transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1904983; P:glycine import into mitochondrion; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.50.40.10; -; 2.
DR   HAMAP; MF_03064; SLC25A38; 1.
DR   InterPro; IPR030847; Hem25/SLC25A38.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   Pfam; PF00153; Mito_carr; 3.
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; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..317
FT                   /note="Mitochondrial glycine transporter"
FT                   /id="PRO_0000378941"
FT   TRANSMEM        16..41
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        70..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        123..148
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        180..203
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        226..252
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   TRANSMEM        284..302
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   REPEAT          10..95
FT                   /note="Solcar 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   REPEAT          117..205
FT                   /note="Solcar 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
FT   REPEAT          222..309
FT                   /note="Solcar 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03064"
SQ   SEQUENCE   317 AA;  35092 MW;  2BAEA7F710DABBDD CRC64;
     MASTTPEVKP GTTLHLLAGS SAGLISAFTL QPFDLLKTRL QQQQRANVGY RSSISRELKK
     LARFKDLWRG ALPSTLRTSV GAGLYFTILS QTRTYVAQLR ARTDKLPHSQ TSVLPKLSAL
     DNLSAGFVVR AVVGFITMPI TIIKTRFESN MYNYNSMYEG VEGIYLDGKE KGSLRNFFKG
     TIATLARDCP YAGLYVLFYE SMKNEFVPKT LILFDQQEQL ENSTLVNSSA AVVASSLATT
     ITAPFDAIKT RLQLDSHTVG GNSIMSVTKQ LLKEDGGVRN LFRGLSLRFG RKGLSAAISW
     CIYEELLKSG RLQRLLH
 
 
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