ID   ZNG1B_HUMAN             Reviewed;         395 AA.
AC   Q8IUF1; Q0VAN3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Zinc-regulated GTPase metalloprotein activator 1B {ECO:0000303|PubMed:35584702};
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:Q8VEH6};
DE   AltName: Full=Cobalamin synthase W domain-containing protein 2 {ECO:0000305};
DE            Short=COBW domain-containing protein 2 {ECO:0000305};
GN   Name=ZNG1B {ECO:0000303|PubMed:35584702, ECO:0000312|HGNC:HGNC:17907};
GN   Synonyms=CBWD2 {ECO:0000312|HGNC:HGNC:17907};
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].
RX   PubMed=12421752; DOI=10.1101/gr.338402;
RA   Fan Y., Newman T., Linardopoulou E., Trask B.J.;
RT   "Gene content and function of the ancestral chromosome fusion site in human
RT   chromosome 2q13-2q14.1 and paralogous regions.";
RL   Genome Res. 12:1663-1672(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 [LARGE SCALE MRNA].
RC   TISSUE=Substantia nigra;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
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 ZNG1B 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VEH6}.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF452722; AAN64907.1; -; mRNA.
DR   EMBL; AY343910; AAQ76868.1; -; mRNA.
DR   EMBL; AK290072; BAF82761.1; -; mRNA.
DR   EMBL; AC016745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL078621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC120991; AAI20992.1; -; mRNA.
DR   EMBL; BC120992; AAI20993.1; -; mRNA.
DR   CCDS; CCDS2116.1; -.
DR   RefSeq; NP_742000.1; NM_172003.3.
DR   AlphaFoldDB; Q8IUF1; -.
DR   SMR; Q8IUF1; -.
DR   BioGRID; 127299; 93.
DR   IntAct; Q8IUF1; 15.
DR   MINT; Q8IUF1; -.
DR   STRING; 9606.ENSP00000259199; -.
DR   iPTMnet; Q8IUF1; -.
DR   PhosphoSitePlus; Q8IUF1; -.
DR   BioMuta; CBWD2; -.
DR   DMDM; 74714301; -.
DR   EPD; Q8IUF1; -.
DR   jPOST; Q8IUF1; -.
DR   MassIVE; Q8IUF1; -.
DR   MaxQB; Q8IUF1; -.
DR   PaxDb; 9606-ENSP00000259199; -.
DR   PeptideAtlas; Q8IUF1; -.
DR   ProteomicsDB; 70557; -.
DR   Pumba; Q8IUF1; -.
DR   Antibodypedia; 59948; 50 antibodies from 12 providers.
DR   DNASU; 150472; -.
DR   Ensembl; ENST00000259199.9; ENSP00000259199.4; ENSG00000136682.16.
DR   GeneID; 150472; -.
DR   KEGG; hsa:150472; -.
DR   MANE-Select; ENST00000259199.9; ENSP00000259199.4; NM_172003.3; NP_742000.1.
DR   UCSC; uc002tju.4; human.
DR   AGR; HGNC:17907; -.
DR   CTD; 150472; -.
DR   GeneCards; ZNG1B; -.
DR   HGNC; HGNC:17907; ZNG1B.
DR   HPA; ENSG00000136682; Low tissue specificity.
DR   MIM; 611079; gene.
DR   neXtProt; NX_Q8IUF1; -.
DR   OpenTargets; ENSG00000136682; -.
DR   PharmGKB; PA26125; -.
DR   VEuPathDB; HostDB:ENSG00000136682; -.
DR   eggNOG; KOG2743; Eukaryota.
DR   GeneTree; ENSGT00940000164995; -.
DR   InParanoid; Q8IUF1; -.
DR   OMA; FEYLHEE; -.
DR   OrthoDB; 1010489at2759; -.
DR   PhylomeDB; Q8IUF1; -.
DR   TreeFam; TF332679; -.
DR   PathwayCommons; Q8IUF1; -.
DR   SignaLink; Q8IUF1; -.
DR   BioGRID-ORCS; 150472; 369 hits in 693 CRISPR screens.
DR   ChiTaRS; CBWD2; human.
DR   GenomeRNAi; 150472; -.
DR   Pharos; Q8IUF1; Tdark.
DR   PRO; PR:Q8IUF1; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8IUF1; Protein.
DR   Bgee; ENSG00000136682; Expressed in monocyte and 97 other cell types or tissues.
DR   ExpressionAtlas; Q8IUF1; 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   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; Q8IUF1; HS.
PE   2: Evidence at transcript level;
KW   Chaperone; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..395
FT                   /note="Zinc-regulated GTPase metalloprotein activator 1B"
FT                   /id="PRO_0000316813"
FT   DOMAIN          274..377
FT                   /note="CobW C-terminal"
FT   REGION          1..36
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   CONFLICT        242
FT                   /note="V -> I (in Ref. 5; AAI20992)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  44034 MW;  D1BAA6864670939F CRC64;
     MLPAVGSADE EEDPAEEDCP ELVPMETTQS EEEEKSGLGA KIPVTIITGY LGAGKTTLLN
     YILTEQHSKR VAVILNEFGE GSALEKSLAV SQGGELYEEW LELRNGCLCC SVKDNGLRAI
     ENLMQKKGKF DYILLETTGL ADPGAVASMF WVDAELGSDI YLDGIITIVD SKYGLKHLAE
     EKPDGLINEA TRQVALADAI LINKTDLVPE EDVKKLRATI RSINGLGQIL ETQRSRVDLS
     NVLDLHAFDS LSGISLQKKL QHVPGTQPHL DQSIVTITFE VPGNAKEEHL NMFIQNLLWE
     KNVRNKDNHC MEVIRLKGLV SIKDKSQQVI VQGVHELYDL EETPVSWKDD TERTNRLVLL
     GRNLDKDILK QLFIATVTET EKQWTTHFKE DQVCT
//