ID ZNG1A_HUMAN Reviewed; 395 AA. AC Q9BRT8; A2RU55; A8K3N3; B0AZR4; Q49AJ1; Q5VVK2; Q6VBU6; Q7Z5Z0; Q7Z652; AC Q9BY38; Q9NYD0; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 166. DE RecName: Full=Zinc-regulated GTPase metalloprotein activator 1A {ECO:0000303|PubMed:35584702}; DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q8VEH6}; DE AltName: Full=Cobalamin synthase W domain-containing protein 1 {ECO:0000305}; DE Short=COBW domain-containing protein 1 {ECO:0000305}; DE AltName: Full=NPC-A-6 COBW domain-containing protein 1; DE Short=NPC-A-6; GN Name=ZNG1A {ECO:0000303|PubMed:35584702, ECO:0000312|HGNC:HGNC:17134}; GN Synonyms=CBWD1 {ECO:0000303|PubMed:31862704, GN ECO:0000312|HGNC:HGNC:17134}; 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 [MRNA] (ISOFORM 1), AND INDUCTION. RC TISSUE=Brain; RX PubMed=11489251; DOI=10.1016/s0006-8993(01)02393-9; RA Shi J., Cai W., Chen X., Ying K., Zhang K., Xie Y.; RT "Identification of dopamine responsive mRNAs in glial cells by suppression RT subtractive hybridization."; RL Brain Res. 910:29-37(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP VAL-8. RX PubMed=15233989; DOI=10.1016/j.ygeno.2004.03.001; RA Wong A., Vallender E.J., Heretis K., Ilkin Y., Lahn B.T., Lese Martin C., RA Ledbetter D.H.; RT "Diverse fates of paralogs following segmental duplication of telomeric RT genes."; RL Genomics 84:239-247(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Nasopharyngeal carcinoma; RA Shu J., Li G., He X.; RT "Construction of cDNA expression library from nasopharyngeal carcinoma RT tissue and screening of antigenic genes."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Embryo, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP VAL-8. RC TISSUE=Bone marrow, and Kidney; 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 [8] RP INDUCTION. RX PubMed=22902622; DOI=10.1074/jbc.m112.397000; RA Coneyworth L.J., Jackson K.A., Tyson J., Bosomworth H.J., van der Hagen E., RA Hann G.M., Ogo O.A., Swann D.C., Mathers J.C., Valentine R.A., Ford D.; RT "Identification of the human zinc transcriptional regulatory element RT (ZTRE): a palindromic protein-binding DNA sequence responsible for zinc- RT induced transcriptional repression."; RL J. Biol. Chem. 287:36567-36581(2012). RN [9] RP INDUCTION. RX PubMed=25582195; DOI=10.1128/mcb.01298-14; RA Ogo O.A., Tyson J., Cockell S.J., Howard A., Valentine R.A., Ford D.; RT "The zinc finger protein ZNF658 regulates the transcription of genes RT involved in zinc homeostasis and affects ribosome biogenesis through the RT zinc transcriptional regulatory element."; RL Mol. Cell. Biol. 35:977-987(2015). RN [10] RP POSSIBLE INVOLVEMENT IN CONGENITAL ANOMALIES OF THE KIDNEY AND URINARY RP TRACT. RX PubMed=31862704; DOI=10.1681/asn.2019040398; RA Kanda S., Ohmuraya M., Akagawa H., Horita S., Yoshida Y., Kaneko N., RA Sugawara N., Ishizuka K., Miura K., Harita Y., Yamamoto T., Oka A., RA Araki K., Furukawa T., Hattori M.; RT "Deletion in the Cobalamin Synthetase W Domain-Containing Protein 1 Gene Is RT associated with Congenital Anomalies of the Kidney and Urinary Tract."; RL J. Am. Soc. Nephrol. 31:139-147(2020). RN [11] RP NOMENCLATURE. RX PubMed=35584702; DOI=10.1016/j.cell.2022.04.011; RA Weiss A., Murdoch C.C., Edmonds K.A., Jordan M.R., Monteith A.J., RA Perera Y.R., Rodriguez Nassif A.M., Petoletti A.M., Beavers W.N., RA Munneke M.J., Drury S.L., Krystofiak E.S., Thalluri K., Wu H., RA Kruse A.R.S., DiMarchi R.D., Caprioli R.M., Spraggins J.M., Chazin W.J., RA Giedroc D.P., Skaar E.P.; RT "Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc RT homeostasis."; RL Cell 185:2148-2163(2022). CC -!- FUNCTION: Zinc chaperone that directly transfers zinc cofactor to CC target metalloproteins, thereby activating them. Catalyzes zinc CC insertion into the active site of methionine aminopeptidase METAP1, CC which function to cleave the initiator methionine from polypeptides CC during or after protein translation. Mechanistically, the N-terminal CC psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of CC METAP1. After formation of the docked complex, zinc is transferred from CC the CXCC motif in the GTPase domain of ZNG1A to the zinc binding site CC in the peptidase domain of METAP1 in a process requiring GTP CC hydrolysis. GTP/GDP exchange is required for release of active METAP1. CC {ECO:0000250|UniProtKB:Q8VEH6}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:Q8VEH6}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:Q8VEH6}; CC -!- INTERACTION: CC Q9BRT8; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-1054417, EBI-2837444; CC Q9BRT8; O75460-2: ERN1; NbExp=3; IntAct=EBI-1054417, EBI-25852368; CC Q9BRT8; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-1054417, EBI-10226858; CC Q9BRT8; P01100: FOS; NbExp=3; IntAct=EBI-1054417, EBI-852851; CC Q9BRT8; P62993: GRB2; NbExp=3; IntAct=EBI-1054417, EBI-401755; CC Q9BRT8; Q99909: SSX3; NbExp=3; IntAct=EBI-1054417, EBI-10295431; CC Q9BRT8; P31930: UQCRC1; NbExp=3; IntAct=EBI-1054417, EBI-1052596; CC Q9BRT8; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-1054417, EBI-746595; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VEH6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9BRT8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BRT8-2; Sequence=VSP_019731, VSP_019732; CC Name=3; CC IsoId=Q9BRT8-3; Sequence=VSP_019734; CC Name=4; CC IsoId=Q9BRT8-4; Sequence=VSP_019733; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Up-regulated in cultured CC astrocytes treated with dopamine. {ECO:0000269|PubMed:15233989}. CC -!- INDUCTION: Down-regulated in response to zinc: repressed by ZNF658 in CC response to zinc by binding to the zinc transcriptional regulatory CC element (ZTRE) (5'-C[AC]C[TAG]CC[TC]-N(0-50)-[GA]G[ATC]G[TG]G-3') found CC in the promoter region of CBWD1 (PubMed:22902622, PubMed:25582195). CC Increased expression in response to dopamine treatment CC (PubMed:11489251). {ECO:0000269|PubMed:11489251, CC ECO:0000269|PubMed:22902622, ECO:0000269|PubMed:25582195}. CC -!- DISEASE: Note=Congenital anomalies of the kidney and urinary tract CC (CAKUT). A disorder encompassing a broad spectrum of renal and urinary CC tract malformations that include renal agenesis, kidney hypodysplasia, CC multicystic kidney dysplasia, duplex collecting system, posterior CC urethral valves and ureter abnormalities. Congenital anomalies of CC kidney and urinary tract are the commonest cause of chronic kidney CC disease in children (PubMed:31862704). Disease susceptibility may be CC associated with variants affecting the gene represented in this entry CC (PubMed:31862704). {ECO:0000269|PubMed:31862704}. CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF257330; AAF68990.2; -; mRNA. DR EMBL; AY343911; AAQ76869.1; -; mRNA. DR EMBL; AY320414; AAP73813.1; -; mRNA. DR EMBL; AF212253; AAK14935.1; -; mRNA. DR EMBL; AK315855; BAF98746.1; -; mRNA. DR EMBL; AK290648; BAF83337.1; -; mRNA. DR EMBL; AL356244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL449043; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005996; AAH05996.1; -; mRNA. DR EMBL; BC009573; AAH09573.1; -; mRNA. DR EMBL; BC013432; AAH13432.1; -; mRNA. DR EMBL; BC132759; AAI32760.1; -; mRNA. DR CCDS; CCDS47947.1; -. [Q9BRT8-3] DR CCDS; CCDS47948.1; -. [Q9BRT8-2] DR CCDS; CCDS6438.1; -. [Q9BRT8-1] DR CCDS; CCDS94370.1; -. [Q9BRT8-4] DR RefSeq; NP_001138827.1; NM_001145355.1. [Q9BRT8-2] DR RefSeq; NP_001138828.1; NM_001145356.1. [Q9BRT8-3] DR RefSeq; NP_060961.3; NM_018491.3. [Q9BRT8-1] DR AlphaFoldDB; Q9BRT8; -. DR SMR; Q9BRT8; -. DR BioGRID; 120970; 256. DR IntAct; Q9BRT8; 72. DR STRING; 9606.ENSP00000366617; -. DR iPTMnet; Q9BRT8; -. DR PhosphoSitePlus; Q9BRT8; -. DR BioMuta; CBWD1; -. DR DMDM; 74752288; -. DR EPD; Q9BRT8; -. DR jPOST; Q9BRT8; -. DR MassIVE; Q9BRT8; -. DR MaxQB; Q9BRT8; -. DR PaxDb; 9606-ENSP00000366617; -. DR PeptideAtlas; Q9BRT8; -. DR ProteomicsDB; 78831; -. [Q9BRT8-1] DR ProteomicsDB; 78832; -. [Q9BRT8-2] DR ProteomicsDB; 78833; -. [Q9BRT8-3] DR ProteomicsDB; 78834; -. [Q9BRT8-4] DR Pumba; Q9BRT8; -. DR Antibodypedia; 55445; 235 antibodies from 16 providers. DR DNASU; 55871; -. DR Ensembl; ENST00000314367.14; ENSP00000323433.10; ENSG00000172785.19. [Q9BRT8-2] DR Ensembl; ENST00000356521.9; ENSP00000348915.4; ENSG00000172785.19. [Q9BRT8-1] DR Ensembl; ENST00000377400.8; ENSP00000366617.5; ENSG00000172785.19. [Q9BRT8-1] DR Ensembl; ENST00000382393.2; ENSP00000371830.1; ENSG00000172785.19. [Q9BRT8-4] DR Ensembl; ENST00000382447.8; ENSP00000371885.4; ENSG00000172785.19. [Q9BRT8-3] DR GeneID; 55871; -. DR KEGG; hsa:55871; -. DR MANE-Select; ENST00000356521.9; ENSP00000348915.4; NM_018491.5; NP_060961.3. DR UCSC; uc003zga.5; human. [Q9BRT8-1] DR AGR; HGNC:17134; -. DR CTD; 55871; -. DR DisGeNET; 55871; -. DR GeneCards; ZNG1A; -. DR HGNC; HGNC:17134; ZNG1A. DR HPA; ENSG00000172785; Low tissue specificity. DR MIM; 611078; gene. DR neXtProt; NX_Q9BRT8; -. DR OpenTargets; ENSG00000172785; -. DR PharmGKB; PA26124; -. DR VEuPathDB; HostDB:ENSG00000172785; -. DR eggNOG; KOG2743; Eukaryota. DR GeneTree; ENSGT00940000164995; -. DR HOGENOM; CLU_2236423_0_0_1; -. DR InParanoid; Q9BRT8; -. DR OMA; KHVFQGV; -. DR OrthoDB; 1010489at2759; -. DR PhylomeDB; Q9BRT8; -. DR TreeFam; TF332679; -. DR PathwayCommons; Q9BRT8; -. DR SignaLink; Q9BRT8; -. DR BioGRID-ORCS; 55871; 347 hits in 1028 CRISPR screens. DR ChiTaRS; CBWD1; human. DR GeneWiki; CBWD1; -. DR GenomeRNAi; 55871; -. DR Pharos; Q9BRT8; Tbio. DR PRO; PR:Q9BRT8; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9BRT8; Protein. DR Bgee; ENSG00000172785; Expressed in adrenal tissue and 105 other cell types or tissues. DR ExpressionAtlas; Q9BRT8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001822; P:kidney development; IMP:UniProtKB. DR CDD; cd03112; CobW-like; 1. DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR036627; CobW-likC_sf. DR InterPro; IPR011629; CobW-like_C. DR InterPro; IPR003495; CobW/HypB/UreG_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR13748:SF31; COBW DOMAIN-CONTAINING PROTEIN 1-RELATED; 1. DR PANTHER; PTHR13748; COBW-RELATED; 1. DR Pfam; PF02492; cobW; 1. DR Pfam; PF07683; CobW_C; 1. DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q9BRT8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chaperone; GTP-binding; Hydrolase; Metal-binding; KW Nucleotide-binding; Nucleus; Reference proteome; Zinc. FT CHAIN 1..395 FT /note="Zinc-regulated GTPase metalloprotein activator 1A" FT /id="PRO_0000245523" FT DOMAIN 274..377 FT /note="CobW C-terminal" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 17..24 FT /note="psi-PxLVp motif" FT /evidence="ECO:0000250|UniProtKB:Q8VEH6" FT MOTIF 107..110 FT /note="CXCC motif" FT /evidence="ECO:0000255" FT BINDING 49..56 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8VEH6" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8VEH6" FT BINDING 110..114 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q8VEH6" FT BINDING 203..206 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT VAR_SEQ 1..36 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_019731" FT VAR_SEQ 37..51 FT /note="GLGAKIPVTIITGYL -> MYFKRAARAFPVLLT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_019732" FT VAR_SEQ 114..395 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_019733" FT VAR_SEQ 236..254 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10931946" FT /id="VSP_019734" FT VARIANT 8 FT /note="A -> V (in dbSNP:rs16925054)" FT /evidence="ECO:0000269|PubMed:15233989, FT ECO:0000269|PubMed:15489334" FT /id="VAR_026979" FT CONFLICT 25 FT /note="I -> M (in Ref. 1; AAF68990 and 4; AAK14935)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="S -> N (in Ref. 1; AAF68990)" FT /evidence="ECO:0000305" FT CONFLICT 387..389 FT /note="RFQ -> HFK (in Ref. 4; AAK14935)" FT /evidence="ECO:0000305" SQ SEQUENCE 395 AA; 44068 MW; A3E04537A6698C6E CRC64; MLPAVGSADE EEDPAEEDCP ELVPIETTQS EEEEKSGLGA KIPVTIITGY LGAGKTTLLN YILTEQHSKR VAVILNEFGE GSALEKSLAV SQGGELYEEW LELRNGCLCC SVKDSGLRAI ENLMQKKGKF DYILLETTGL ADPGAVASMF WVDAELGSDI YLDGIITIVD SKYGLKHLTE EKPDGLINEA TRQVALADAI LINKTDLVPE EDVKKLRTTI RSINGLGQIL ETQRSRVDLS NVLDLHAFDS LSGISLQKKL QHVPGTQPHL DQSIVTITFE VPGNAKEEHL NMFIQNLLWE KNVRNKDNHC MEVIRLKGLV SIKDKSQQVI VQGVHELYDL EETPVSWKDD TERTNRLVLL GRNLDKDILK QLFIATVTET EKQWTTRFQE DQVCT //