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GDIA_HUMAN
ID   GDIA_HUMAN              Reviewed;         447 AA.
AC   P31150; P50394; Q6FG50; Q7Z2G6; Q7Z2G9; Q7Z2H5; Q7Z2I6;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 213.
DE   RecName: Full=Rab GDP dissociation inhibitor alpha;
DE            Short=Rab GDI alpha;
DE   AltName: Full=Guanosine diphosphate dissociation inhibitor 1;
DE            Short=GDI-1;
DE   AltName: Full=Oligophrenin-2;
DE   AltName: Full=Protein XAP-4;
GN   Name=GDI1; Synonyms=GDIL, OPHN2, RABGDIA, XAP4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=7849400; DOI=10.1007/bf00411459;
RA   Sedlacek Z., Konecki D.S., Korn B., Klauck S.M., Poustka A.;
RT   "Evolutionary conservation and genomic organization of XAP-4, an Xq28
RT   located gene coding for a human rab GDP-dissociation inhibitor (GDI).";
RL   Mamm. Genome 5:633-639(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=7585614;
RA   Nishimura N., Goji J., Nakamura H., Orita S., Takai Y., Sano K.;
RT   "Cloning of a brain-type isoform of human Rab GDI and its expression in
RT   human neuroblastoma cell lines and tumor specimens.";
RL   Cancer Res. 55:5445-5450(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA   Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L.,
RA   Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.;
RT   "Long-range sequence analysis in Xq28: thirteen known and six candidate
RT   genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.";
RL   Hum. Mol. Genet. 5:659-668(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Feng Z., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=12777533; DOI=10.1093/molbev/msg134;
RA   Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT   "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT   chimpanzees.";
RL   Mol. Biol. Evol. 20:1281-1289(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Lung;
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   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-181.
RA   Hochgeschwender U.;
RT   "Rapid identification of gene sequences for transcriptional map assembly by
RT   direct cDNA screening of genomic reference libraries.";
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   PROTEIN SEQUENCE OF 143-156; 174-193 AND 222-240, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 328-436.
RA   Bhat K.S.;
RL   Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   PROTEIN SEQUENCE OF 349-361.
RC   TISSUE=Keratinocyte;
RX   PubMed=1286667; DOI=10.1002/elps.11501301199;
RA   Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA   Vandekerckhove J.;
RT   "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT   database of normal human epidermal keratinocytes.";
RL   Electrophoresis 13:960-969(1992).
RN   [15]
RP   TISSUE SPECIFICITY.
RX   PubMed=7543319; DOI=10.1093/hmg/4.4.701;
RA   Bachner D., Sedlacek Z., Korn B., Hameister H., Poustka A.;
RT   "Expression patterns of two human genes coding for different rab GDP-
RT   dissociation inhibitors (GDIs), extremely conserved proteins involved in
RT   cellular transport.";
RL   Hum. Mol. Genet. 4:701-708(1995).
RN   [16]
RP   INTERACTION WITH RHOH.
RX   PubMed=11809807; DOI=10.1128/mcb.22.4.1158-1171.2002;
RA   Li X., Bu X., Lu B., Avraham H., Flavell R.A., Lim B.;
RT   "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient
RT   and modulates activities of other Rho GTPases by an inhibitory function.";
RL   Mol. Cell. Biol. 22:1158-1171(2002).
RN   [17]
RP   INTERACTION WITH RAB10, AND SUBCELLULAR LOCATION.
RX   PubMed=19570034; DOI=10.1042/bj20090624;
RA   Chen Y., Deng Y., Zhang J., Yang L., Xie X., Xu T.;
RT   "GDI-1 preferably interacts with Rab10 in insulin-stimulated GLUT4
RT   translocation.";
RL   Biochem. J. 422:229-235(2009).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   INTERACTION WITH RAB1A AND RAB5A, AND FUNCTION.
RX   PubMed=23815289; DOI=10.3109/09687688.2013.818725;
RA   Kirsten M.L., Baron R.A., Seabra M.C., Ces O.;
RT   "Rab1a and Rab5a preferentially bind to binary lipid compositions with
RT   higher stored curvature elastic energy.";
RL   Mol. Membr. Biol. 30:303-314(2013).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB8A; RAB10 AND
RP   RAB12.
RX   PubMed=26824392; DOI=10.7554/elife.12813;
RA   Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S.,
RA   Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J.,
RA   Morrow J.A., Reith A.D., Alessi D.R., Mann M.;
RT   "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates
RT   a subset of Rab GTPases.";
RL   Elife 5:0-0(2016).
RN   [22]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB3A; RAB5A;
RP   RAB5B; RAB5C; RAB8A; RAB8B; RAB10; RAB35 AND RAB43.
RX   PubMed=29125462; DOI=10.7554/elife.31012;
RA   Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA   Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA   Mann M.;
RT   "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT   establishes a connection to ciliogenesis.";
RL   Elife 6:0-0(2017).
RN   [23]
RP   VARIANT XLID41 PRO-92.
RX   PubMed=9620768; DOI=10.1038/487;
RA   D'Adamo P., Menegon A., Lo Nigro C., Grasso M., Gulisano M., Tamanini F.,
RA   Bienvenu T., Gedeon A.K., Oostra B., Wu S.-K., Tandon A., Valtorta F.,
RA   Balch W.E., Chelly J., Toniolo D.;
RT   "Mutations in GDI1 are responsible for X-linked non-specific mental
RT   retardation.";
RL   Nat. Genet. 19:134-139(1998).
RN   [24]
RP   VARIANT XLID41 PRO-423.
RX   PubMed=9668174; DOI=10.1093/hmg/7.8.1311;
RA   Bienvenu T., Des Portes V., Saint Martin A., McDonell N., Billuart P.,
RA   Carrie A., Vinet M.-C., Couvert P., Toniolo D., Ropers H.-H., Moraine C.,
RA   van Bokhoven H., Fryns J.-P., Kahn A., Beldjord C., Chelly J.;
RT   "Non-specific X-linked semidominant mental retardation by mutations in a
RT   Rab GDP-dissociation inhibitor.";
RL   Hum. Mol. Genet. 7:1311-1315(1998).
CC   -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab proteins
CC       by inhibiting the dissociation of GDP from them, and the subsequent
CC       binding of GTP to them. Promotes the dissociation of GDP-bound Rab
CC       proteins from the membrane and inhibits their activation. Promotes the
CC       dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes.
CC       {ECO:0000269|PubMed:23815289}.
CC   -!- SUBUNIT: Interacts with RHOH (PubMed:11809807). Interacts with the non-
CC       phosphorylated forms of RAB1A, RAB3A, RAB5A, RAB5B, RAB5C, RAB8A,
CC       RAB8B, RAB10, RAB12, RAB35, and RAB43 (PubMed:19570034,
CC       PubMed:23815289, PubMed:26824392, PubMed:29125462).
CC       {ECO:0000269|PubMed:11809807, ECO:0000269|PubMed:19570034,
CC       ECO:0000269|PubMed:23815289, ECO:0000269|PubMed:26824392,
CC       ECO:0000269|PubMed:29125462}.
CC   -!- INTERACTION:
CC       P31150; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-946999, EBI-739832;
CC       P31150; P62820: RAB1A; NbExp=3; IntAct=EBI-946999, EBI-716845;
CC       P31150; P20338: RAB4A; NbExp=4; IntAct=EBI-946999, EBI-722284;
CC       P31150; P61027: Rab10; Xeno; NbExp=3; IntAct=EBI-946999, EBI-911581;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19570034}. Golgi
CC       apparatus, trans-Golgi network {ECO:0000269|PubMed:19570034}.
CC   -!- TISSUE SPECIFICITY: Brain; predominant in neural and sensory tissues.
CC       {ECO:0000269|PubMed:7543319}.
CC   -!- DISEASE: Intellectual developmental disorder, X-linked 41 (XLID41)
CC       [MIM:300849]: A disorder characterized by significantly below average
CC       general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period.
CC       Intellectual deficiency is the only primary symptom of non-syndromic X-
CC       linked forms, while syndromic forms present with associated physical,
CC       neurological and/or psychiatric manifestations.
CC       {ECO:0000269|PubMed:9620768, ECO:0000269|PubMed:9668174}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR   EMBL; X79353; CAA55908.1; -; mRNA.
DR   EMBL; X79354; CAA55909.1; -; Genomic_DNA.
DR   EMBL; X79355; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79356; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79357; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79358; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79359; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79360; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79364; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79361; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79362; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; X79363; CAA55909.1; JOINED; Genomic_DNA.
DR   EMBL; D45021; BAA08078.1; -; mRNA.
DR   EMBL; L44140; AAA92648.1; -; Genomic_DNA.
DR   EMBL; AF400433; AAK92482.1; -; mRNA.
DR   EMBL; AB101741; BAC80330.1; -; Genomic_DNA.
DR   EMBL; AB101742; BAC80331.1; -; Genomic_DNA.
DR   EMBL; AB101743; BAC80332.1; -; Genomic_DNA.
DR   EMBL; AB101744; BAC80333.1; -; Genomic_DNA.
DR   EMBL; AB101745; BAC80334.1; -; Genomic_DNA.
DR   EMBL; AB101746; BAC80335.1; -; Genomic_DNA.
DR   EMBL; AB101747; BAC80336.1; -; Genomic_DNA.
DR   EMBL; AB101748; BAC80337.1; -; Genomic_DNA.
DR   EMBL; AB101749; BAC80338.1; -; Genomic_DNA.
DR   EMBL; AB101750; BAC80339.1; -; Genomic_DNA.
DR   EMBL; AB101751; BAC80340.1; -; Genomic_DNA.
DR   EMBL; AB101752; BAC80341.1; -; Genomic_DNA.
DR   EMBL; AB101753; BAC80342.1; -; Genomic_DNA.
DR   EMBL; AB101754; BAC80343.1; -; Genomic_DNA.
DR   EMBL; AB101755; BAC80344.1; -; Genomic_DNA.
DR   EMBL; AB101756; BAC80345.1; -; Genomic_DNA.
DR   EMBL; AB101757; BAC80346.1; -; Genomic_DNA.
DR   EMBL; AB101758; BAC80347.1; -; Genomic_DNA.
DR   EMBL; AB101759; BAC80348.1; -; Genomic_DNA.
DR   EMBL; AB101760; BAC80349.1; -; Genomic_DNA.
DR   EMBL; AB101771; BAC80360.1; -; Genomic_DNA.
DR   EMBL; AB101772; BAC80361.1; -; Genomic_DNA.
DR   EMBL; AB101773; BAC80362.1; -; Genomic_DNA.
DR   EMBL; AB101774; BAC80363.1; -; Genomic_DNA.
DR   EMBL; AB101775; BAC80364.1; -; Genomic_DNA.
DR   EMBL; AB101776; BAC80365.1; -; Genomic_DNA.
DR   EMBL; AB101777; BAC80366.1; -; Genomic_DNA.
DR   EMBL; AB101778; BAC80367.1; -; Genomic_DNA.
DR   EMBL; AB101779; BAC80368.1; -; Genomic_DNA.
DR   EMBL; AB101780; BAC80369.1; -; Genomic_DNA.
DR   EMBL; AB101781; BAC80370.1; -; Genomic_DNA.
DR   EMBL; AB101782; BAC80371.1; -; Genomic_DNA.
DR   EMBL; AB101783; BAC80372.1; -; Genomic_DNA.
DR   EMBL; AB101784; BAC80373.1; -; Genomic_DNA.
DR   EMBL; AB101785; BAC80374.1; -; Genomic_DNA.
DR   EMBL; AB101786; BAC80375.1; -; Genomic_DNA.
DR   EMBL; AB101787; BAC80376.1; -; Genomic_DNA.
DR   EMBL; AB101788; BAC80377.1; -; Genomic_DNA.
DR   EMBL; AB101789; BAC80378.1; -; Genomic_DNA.
DR   EMBL; AB101790; BAC80379.1; -; Genomic_DNA.
DR   EMBL; AB101801; BAC80390.1; -; Genomic_DNA.
DR   EMBL; AB101802; BAC80391.1; -; Genomic_DNA.
DR   EMBL; AB101803; BAC80392.1; -; Genomic_DNA.
DR   EMBL; AB101804; BAC80393.1; -; Genomic_DNA.
DR   EMBL; AB101805; BAC80394.1; -; Genomic_DNA.
DR   EMBL; AB101806; BAC80395.1; -; Genomic_DNA.
DR   EMBL; AB101807; BAC80396.1; -; Genomic_DNA.
DR   EMBL; AB101808; BAC80397.1; -; Genomic_DNA.
DR   EMBL; AB101809; BAC80398.1; -; Genomic_DNA.
DR   EMBL; AB101810; BAC80399.1; -; Genomic_DNA.
DR   EMBL; AB101811; BAC80400.1; -; Genomic_DNA.
DR   EMBL; AB101812; BAC80401.1; -; Genomic_DNA.
DR   EMBL; AB101813; BAC80402.1; -; Genomic_DNA.
DR   EMBL; AB101814; BAC80403.1; -; Genomic_DNA.
DR   EMBL; AB101815; BAC80404.1; -; Genomic_DNA.
DR   EMBL; AB101816; BAC80405.1; -; Genomic_DNA.
DR   EMBL; AB101817; BAC80406.1; -; Genomic_DNA.
DR   EMBL; AB101818; BAC80407.1; -; Genomic_DNA.
DR   EMBL; AB101819; BAC80408.1; -; Genomic_DNA.
DR   EMBL; AB101820; BAC80409.1; -; Genomic_DNA.
DR   EMBL; AB101831; BAC80420.1; -; Genomic_DNA.
DR   EMBL; AB101832; BAC80421.1; -; Genomic_DNA.
DR   EMBL; AB101833; BAC80422.1; -; Genomic_DNA.
DR   EMBL; AB101834; BAC80423.1; -; Genomic_DNA.
DR   EMBL; AB101835; BAC80424.1; -; Genomic_DNA.
DR   EMBL; AB101836; BAC80425.1; -; Genomic_DNA.
DR   EMBL; AB101837; BAC80426.1; -; Genomic_DNA.
DR   EMBL; AB101838; BAC80427.1; -; Genomic_DNA.
DR   EMBL; AB101839; BAC80428.1; -; Genomic_DNA.
DR   EMBL; AB101840; BAC80429.1; -; Genomic_DNA.
DR   EMBL; AB101841; BAC80430.1; -; Genomic_DNA.
DR   EMBL; AB101842; BAC80431.1; -; Genomic_DNA.
DR   EMBL; AB101843; BAC80432.1; -; Genomic_DNA.
DR   EMBL; AB101844; BAC80433.1; -; Genomic_DNA.
DR   EMBL; AB101845; BAC80434.1; -; Genomic_DNA.
DR   EMBL; AB101846; BAC80435.1; -; Genomic_DNA.
DR   EMBL; AB101847; BAC80436.1; -; Genomic_DNA.
DR   EMBL; AB101848; BAC80437.1; -; Genomic_DNA.
DR   EMBL; AB101849; BAC80438.1; -; Genomic_DNA.
DR   EMBL; AB101850; BAC80439.1; -; Genomic_DNA.
DR   EMBL; AB102647; BAC81116.1; -; mRNA.
DR   EMBL; CR542258; CAG47054.1; -; mRNA.
DR   EMBL; CR542276; CAG47072.1; -; mRNA.
DR   EMBL; BT019884; AAV38687.1; -; mRNA.
DR   EMBL; BX936385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471172; EAW72710.1; -; Genomic_DNA.
DR   EMBL; BC000317; AAH00317.1; -; mRNA.
DR   EMBL; BC012201; AAH12201.1; -; mRNA.
DR   EMBL; U14623; AAA21558.1; -; Genomic_DNA.
DR   EMBL; L05086; AAC15851.1; -; mRNA.
DR   CCDS; CCDS35452.1; -.
DR   PIR; I37082; I37082.
DR   RefSeq; NP_001484.1; NM_001493.2.
DR   AlphaFoldDB; P31150; -.
DR   SMR; P31150; -.
DR   BioGRID; 108932; 102.
DR   IntAct; P31150; 63.
DR   MINT; P31150; -.
DR   STRING; 9606.ENSP00000394071; -.
DR   GlyGen; P31150; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P31150; -.
DR   MetOSite; P31150; -.
DR   PhosphoSitePlus; P31150; -.
DR   SwissPalm; P31150; -.
DR   BioMuta; GDI1; -.
DR   DMDM; 1707886; -.
DR   OGP; P31150; -.
DR   REPRODUCTION-2DPAGE; IPI00010154; -.
DR   UCD-2DPAGE; P31150; -.
DR   EPD; P31150; -.
DR   jPOST; P31150; -.
DR   MassIVE; P31150; -.
DR   MaxQB; P31150; -.
DR   PaxDb; P31150; -.
DR   PeptideAtlas; P31150; -.
DR   PRIDE; P31150; -.
DR   ProteomicsDB; 54760; -.
DR   Antibodypedia; 4564; 401 antibodies from 33 providers.
DR   DNASU; 2664; -.
DR   Ensembl; ENST00000447750.7; ENSP00000394071.2; ENSG00000203879.12.
DR   GeneID; 2664; -.
DR   KEGG; hsa:2664; -.
DR   MANE-Select; ENST00000447750.7; ENSP00000394071.2; NM_001493.3; NP_001484.1.
DR   UCSC; uc004fli.5; human.
DR   CTD; 2664; -.
DR   DisGeNET; 2664; -.
DR   GeneCards; GDI1; -.
DR   HGNC; HGNC:4226; GDI1.
DR   HPA; ENSG00000203879; Tissue enhanced (brain).
DR   MalaCards; GDI1; -.
DR   MIM; 300104; gene.
DR   MIM; 300849; phenotype.
DR   neXtProt; NX_P31150; -.
DR   OpenTargets; ENSG00000203879; -.
DR   Orphanet; 777; X-linked non-syndromic intellectual disability.
DR   PharmGKB; PA28641; -.
DR   VEuPathDB; HostDB:ENSG00000203879; -.
DR   eggNOG; KOG1439; Eukaryota.
DR   GeneTree; ENSGT00950000182994; -.
DR   HOGENOM; CLU_021695_0_0_1; -.
DR   InParanoid; P31150; -.
DR   OMA; DHYGGES; -.
DR   OrthoDB; 763627at2759; -.
DR   PhylomeDB; P31150; -.
DR   TreeFam; TF300449; -.
DR   PathwayCommons; P31150; -.
DR   Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   SignaLink; P31150; -.
DR   BioGRID-ORCS; 2664; 11 hits in 707 CRISPR screens.
DR   ChiTaRS; GDI1; human.
DR   GeneWiki; GDI1; -.
DR   GenomeRNAi; 2664; -.
DR   Pharos; P31150; Tbio.
DR   PRO; PR:P31150; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P31150; protein.
DR   Bgee; ENSG00000203879; Expressed in right hemisphere of cerebellum and 205 other tissues.
DR   ExpressionAtlas; P31150; baseline and differential.
DR   Genevisible; P31150; HS.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; TAS:ProtInc.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0090315; P:negative regulation of protein targeting to membrane; IMP:UniProtKB.
DR   GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0032482; P:Rab protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR11787; PTHR11787; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PRINTS; PR00892; RABGDI.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Disease variant; Golgi apparatus;
KW   GTPase activation; Intellectual disability; Reference proteome.
FT   CHAIN           1..447
FT                   /note="Rab GDP dissociation inhibitor alpha"
FT                   /id="PRO_0000056671"
FT   VARIANT         92
FT                   /note="L -> P (in XLID41; causes reduced binding and
FT                   recycling of RAB3A; dbSNP:rs121434607)"
FT                   /evidence="ECO:0000269|PubMed:9620768"
FT                   /id="VAR_008130"
FT   VARIANT         423
FT                   /note="R -> P (in XLID41; dbSNP:rs121434609)"
FT                   /evidence="ECO:0000269|PubMed:9668174"
FT                   /id="VAR_008131"
FT   CONFLICT        34
FT                   /note="D -> G (in Ref. 2; BAA08078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="N -> K (in Ref. 2; BAA08078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149..151
FT                   /note="NFD -> GTY (in Ref. 2; BAA08078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="G -> V (in Ref. 13; AAC15851)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="H -> Q (in Ref. 13; AAC15851)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="D -> G (in Ref. 13; AAC15851)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442
FT                   /note="F -> S (in Ref. 2; BAA08078)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50583 MW;  BC283A445E50A652 CRC64;
     MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQLLE
     GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP
     STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQTTSMRD VYRKFDLGQD
     VIDFTGHALA LYRTDDYLDQ PCLETVNRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VRKAGQVIRI
     ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETT
     DPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGCESQVFC SCSYDATTHF ETTCNDIKDI
     YKRMAGTAFD FENMKRKQND VFGEAEQ
 
 
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