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GDAP1_BOVIN
ID   GDAP1_BOVIN             Reviewed;         358 AA.
AC   A6QQZ0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Ganglioside-induced differentiation-associated protein 1;
DE            Short=GDAP1;
GN   Name=GDAP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates the mitochondrial network by promoting
CC       mitochondrial fission. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q8TB36}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q8TB36}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O88741}.
CC   -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC       and enhancement of mitophagy. Deubiquitinated by USP30.
CC       {ECO:0000250|UniProtKB:Q8TB36}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC   -!- CAUTION: While belonging to the GST superfamily, it lacks glutathione
CC       transferase activity. {ECO:0000305}.
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DR   EMBL; DAAA02038855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC150048; AAI50049.1; -; mRNA.
DR   RefSeq; NP_001094692.1; NM_001101222.1.
DR   AlphaFoldDB; A6QQZ0; -.
DR   SMR; A6QQZ0; -.
DR   STRING; 9913.ENSBTAP00000016739; -.
DR   PaxDb; A6QQZ0; -.
DR   PRIDE; A6QQZ0; -.
DR   Ensembl; ENSBTAT00000016739; ENSBTAP00000016739; ENSBTAG00000012608.
DR   GeneID; 613472; -.
DR   KEGG; bta:613472; -.
DR   CTD; 54332; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012608; -.
DR   VGNC; VGNC:29295; GDAP1.
DR   eggNOG; KOG4420; Eukaryota.
DR   GeneTree; ENSGT00940000159124; -.
DR   HOGENOM; CLU_049129_0_0_1; -.
DR   InParanoid; A6QQZ0; -.
DR   OMA; LHCEEYD; -.
DR   OrthoDB; 1011771at2759; -.
DR   TreeFam; TF327072; -.
DR   Reactome; R-BTA-9603798; Class I peroxisomal membrane protein import.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000012608; Expressed in occipital lobe and 97 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0008053; P:mitochondrial fusion; IBA:GO_Central.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   InterPro; IPR034336; GDAP1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44188:SF3; PTHR44188:SF3; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Isopeptide bond; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..358
FT                   /note="Ganglioside-induced differentiation-associated
FT                   protein 1"
FT                   /id="PRO_0000418810"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..105
FT                   /note="GST N-terminal"
FT   DOMAIN          153..309
FT                   /note="GST C-terminal"
FT   REGION          320..358
FT                   /note="Required for mitochondrial localization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         203
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        50
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        172
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        173
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        188
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        190
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        203
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        206
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        207
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
FT   CROSSLNK        214
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TB36"
SQ   SEQUENCE   358 AA;  41202 MW;  01806D1D09891F23 CRC64;
     MARRQDEQRG GAPLIAEGKS DAEVKLILYH WTHSFSSQKV RLVIAEKALK CEEHDVSLPL
     SEHNEPWFMR LNSTGEVPVL IHGENIICEA TQIIDYLEQT FLDEKTPRLM PDKGSMYYPR
     VQHYRELLDS LPMDAYTHGC ILHPELTVDS MIPAYATTRI RSQIGNTESE LKKLAEENPD
     LQEAYIAKQK RLKSKLLDHD NVKYLKKILD ELEKVLDQVE TELQRRNEET PEEGRQPWLC
     GESFTLADVS LAVTLHRLKF LGFARRNWGN GKRPNLETYY ERVLKRKTFN KVLGHVNNIL
     ISAVLPTAFR VAKKRAPKVL GTTLVVGLLA GMGYFAFMLF RKRLGSMILA LRPRPNYF
 
 
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