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GDAP1_MOUSE
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   03-AUG-2022, entry version 156.
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   AlphaFoldDB; O88741; -.
DR   SMR; O88741; -.
DR   BioGRID; 199873; 4.
DR   STRING; 10090.ENSMUSP00000026879; -.
DR   iPTMnet; O88741; -.
DR   PhosphoSitePlus; O88741; -.
DR   MaxQB; O88741; -.
DR   PaxDb; O88741; -.
DR   PeptideAtlas; O88741; -.
DR   PRIDE; O88741; -.
DR   ProteomicsDB; 267425; -. [O88741-1]
DR   ProteomicsDB; 267426; -. [O88741-2]
DR   Antibodypedia; 2988; 126 antibodies from 23 providers.
DR   DNASU; 14545; -.
DR   Ensembl; ENSMUST00000026879; ENSMUSP00000026879; ENSMUSG00000025777. [O88741-1]
DR   GeneID; 14545; -.
DR   KEGG; mmu:14545; -.
DR   UCSC; uc007akb.2; mouse. [O88741-2]
DR   UCSC; uc007akc.2; mouse. [O88741-1]
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; 1011771at2759; -.
DR   PhylomeDB; O88741; -.
DR   TreeFam; TF327072; -.
DR   Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR   BioGRID-ORCS; 14545; 1 hit in 73 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 161 other tissues.
DR   ExpressionAtlas; O88741; baseline and differential.
DR   Genevisible; O88741; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031307; C:integral component of 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:0006749; P:glutathione metabolic process; IEA:InterPro.
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   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   1: Evidence at protein level;
KW   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
 
 
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