ID GDAP1_MOUSE Reviewed; 358 AA.
AC O88741; Q8C7Q5; Q9CTN2;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=Ganglioside-induced differentiation-associated protein 1;
DE Short=GDAP1;
GN Name=Gdap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10217254; DOI=10.1046/j.1471-4159.1999.0721781.x;
RA Liu H., Nakagawa T., Kanematsu T., Uchida T., Tsuji S.;
RT "Isolation of 10 differentially expressed cDNAs in differentiated Neuro2a
RT cells induced through controlled expression of the GD3 synthase gene.";
RL J. Neurochem. 72:1781-1790(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, Spinal cord, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 162-172; 215-225 AND 292-310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16172208; DOI=10.1083/jcb.200507087;
RA Niemann A., Ruegg M., La Padula V., Schenone A., Suter U.;
RT "Ganglioside-induced differentiation associated protein 1 is a regulator of
RT the mitochondrial network: new implications for Charcot-Marie-Tooth
RT disease.";
RL J. Cell Biol. 170:1067-1078(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates the mitochondrial network by promoting
CC mitochondrial fission. {ECO:0000250, ECO:0000269|PubMed:16172208}.
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:0000269|PubMed:16172208}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88741-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88741-2; Sequence=VSP_008791, VSP_008792;
CC -!- TISSUE SPECIFICITY: Expressed in brain, spinal cord, muscles and
CC intestinal villi. In the central nervous system expressed most
CC prominently in the cortex, cerebellum, thalamus, olfactory bulb, and
CC spinal cord. Expressed also in sciatic nerves and in dorsal root
CC ganglia. {ECO:0000269|PubMed:16172208}.
CC -!- DEVELOPMENTAL STAGE: First expressed at embryonic stage 13 dpc. Levels
CC then increase gradually to reach maximum levels at adulthood.
CC -!- INDUCTION: Increased expression during neural differentiation.
CC {ECO:0000269|PubMed:10217254}.
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; Y17850; CAA76893.1; -; mRNA.
DR EMBL; AK020988; BAB32270.1; -; mRNA.
DR EMBL; AK045460; BAC32380.1; -; mRNA.
DR EMBL; AK049655; BAC33861.1; -; mRNA.
DR EMBL; AK083814; BAC39027.1; -; mRNA.
DR EMBL; BC048177; AAH48177.1; -; mRNA.
DR EMBL; BC051135; AAH51135.1; -; mRNA.
DR CCDS; CCDS14834.1; -. [O88741-1]
DR RefSeq; NP_034397.1; NM_010267.3. [O88741-1]
DR PDB; 8EXZ; X-ray; 2.82 A; A/B=1-358.
DR PDBsum; 8EXZ; -.
DR AlphaFoldDB; O88741; -.
DR SMR; O88741; -.
DR BioGRID; 199873; 4.
DR STRING; 10090.ENSMUSP00000026879; -.
DR iPTMnet; O88741; -.
DR PhosphoSitePlus; O88741; -.
DR SwissPalm; O88741; -.
DR MaxQB; O88741; -.
DR PaxDb; 10090-ENSMUSP00000026879; -.
DR PeptideAtlas; O88741; -.
DR ProteomicsDB; 267425; -. [O88741-1]
DR ProteomicsDB; 267426; -. [O88741-2]
DR Antibodypedia; 2988; 141 antibodies from 23 providers.
DR DNASU; 14545; -.
DR Ensembl; ENSMUST00000026879.8; ENSMUSP00000026879.8; ENSMUSG00000025777.9. [O88741-1]
DR GeneID; 14545; -.
DR KEGG; mmu:14545; -.
DR UCSC; uc007akb.2; mouse. [O88741-2]
DR UCSC; uc007akc.2; mouse. [O88741-1]
DR AGR; MGI:1338002; -.
DR CTD; 54332; -.
DR MGI; MGI:1338002; Gdap1.
DR VEuPathDB; HostDB:ENSMUSG00000025777; -.
DR eggNOG; KOG4420; Eukaryota.
DR GeneTree; ENSGT00940000159124; -.
DR HOGENOM; CLU_049129_0_0_1; -.
DR InParanoid; O88741; -.
DR OMA; LHCEEYD; -.
DR OrthoDB; 803504at2759; -.
DR PhylomeDB; O88741; -.
DR TreeFam; TF327072; -.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 14545; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Gdap1; mouse.
DR PRO; PR:O88741; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O88741; Protein.
DR Bgee; ENSMUSG00000025777; Expressed in barrel cortex and 164 other cell types or tissues.
DR ExpressionAtlas; O88741; baseline and differential.
DR Genevisible; O88741; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISO:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
DR CDD; cd10303; GST_C_GDAP1; 1.
DR CDD; cd03052; GST_N_GDAP1; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; IPR034336; GST_C_GDAP1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44188:SF3; GANGLIOSIDE-INDUCED DIFFERENTIATION-ASSOCIATED PROTEIN 1; 1.
DR PANTHER; PTHR44188; GDAP1, ISOFORM A; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..358
FT /note="Ganglioside-induced differentiation-associated
FT protein 1"
FT /id="PRO_0000186039"
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"
FT VAR_SEQ 163
FT /note="Q -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008791"
FT VAR_SEQ 164..358
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008792"
SQ SEQUENCE 358 AA; 41311 MW; 7B533CB34138891F CRC64;
MARRQDEARA GVPLRVEGPP DKEVHLILYH WTHSFSSQKV RLVIAEKALK CEEHDVSLPL
SEHNEPWFMR LNSAGEVPVL VHGENIICEA TQIIDYLEQT FLDERTPRLM PDEGSMYYPR
VQHYRELLDS LPMDAYTHGC ILHPELTVDS MIPAYATTRI RSQIGNTESE LKKLAEENPD
LQEAYIAKQK RLKSKLLDHD NVKYLKKILD ELEKVLDQVE TELQRRNEET PEEGNQPWLC
GESFTLADVS LAVTLHRLKF LGFARRNWGH GKRPNLETYY ERVLKRKTFN KVLGHVNNIL
ISAVLPTAFR VAKKRAPKVL GSTLVVGLLV GMGYFAFMLF RRRLGSMILA LRPRPNYF
//
