GNAZ_HUMAN
ID GNAZ_HUMAN Reviewed; 355 AA.
AC P19086; B2R6C1; Q4QRJ6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Guanine nucleotide-binding protein G(z) subunit alpha;
DE AltName: Full=G(x) alpha chain;
DE AltName: Full=Gz-alpha;
GN Name=GNAZ;
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=3129724; DOI=10.1073/pnas.85.9.3066;
RA Fong H.K.W., Yoshimoto K.K., Eversole-Cire P., Simon M.I.;
RT "Identification of a GTP-binding protein alpha subunit that lacks an
RT apparent ADP-ribosylation site for pertussis toxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3066-3070(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2115889; DOI=10.1016/s0021-9258(19)38287-0;
RA Matsuoka M., Itoh H., Kaziro Y.;
RT "Characterization of the human gene for Gx alpha, a pertussis toxin-
RT insensitive regulatory GTP-binding protein.";
RL J. Biol. Chem. 265:13215-13220(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1908722;
RA Gagnon A.W., Manning D.R., Catani L., Gewirtz A., Poncz M., Brass L.F.;
RT "Identification of Gz alpha as a pertussis toxin-insensitive G protein in
RT human platelets and megakaryocytes.";
RL Blood 78:1247-1253(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PNS;
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 [9]
RP INTERACTION WITH ADGRB2.
RX PubMed=28891236; DOI=10.1002/humu.23336;
RA Purcell R.H., Toro C., Gahl W.A., Hall R.A.;
RT "A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2) increases
RT receptor signaling activity.";
RL Hum. Mutat. 38:1751-1760(2017).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G-proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Interacts
CC with ADGRB2 (PubMed:28891236). {ECO:0000269|PubMed:28891236}.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; J03260; AAA52580.1; -; mRNA.
DR EMBL; D90150; BAA14180.1; -; Genomic_DNA.
DR EMBL; AF493899; AAM12613.1; -; mRNA.
DR EMBL; CR456495; CAG30381.1; -; mRNA.
DR EMBL; AK312519; BAG35418.1; -; mRNA.
DR EMBL; CH471095; EAW59559.1; -; Genomic_DNA.
DR EMBL; BC078163; AAH78163.1; -; mRNA.
DR EMBL; BC096828; AAH96828.1; -; mRNA.
DR CCDS; CCDS13804.1; -.
DR PIR; A36628; RGHUGX.
DR RefSeq; NP_002064.1; NM_002073.3.
DR AlphaFoldDB; P19086; -.
DR SMR; P19086; -.
DR BioGRID; 109043; 79.
DR ELM; P19086; -.
DR IntAct; P19086; 39.
DR MINT; P19086; -.
DR STRING; 9606.ENSP00000478892; -.
DR iPTMnet; P19086; -.
DR PhosphoSitePlus; P19086; -.
DR SwissPalm; P19086; -.
DR BioMuta; GNAZ; -.
DR DMDM; 121005; -.
DR jPOST; P19086; -.
DR MassIVE; P19086; -.
DR MaxQB; P19086; -.
DR PaxDb; P19086; -.
DR PeptideAtlas; P19086; -.
DR PRIDE; P19086; -.
DR ProteomicsDB; 53630; -.
DR Antibodypedia; 222; 340 antibodies from 30 providers.
DR DNASU; 2781; -.
DR Ensembl; ENST00000615612.2; ENSP00000478892.1; ENSG00000128266.9.
DR GeneID; 2781; -.
DR KEGG; hsa:2781; -.
DR MANE-Select; ENST00000615612.2; ENSP00000478892.1; NM_002073.4; NP_002064.1.
DR UCSC; uc002zwu.2; human.
DR CTD; 2781; -.
DR DisGeNET; 2781; -.
DR GeneCards; GNAZ; -.
DR HGNC; HGNC:4395; GNAZ.
DR HPA; ENSG00000128266; Tissue enhanced (brain).
DR MIM; 139160; gene.
DR neXtProt; NX_P19086; -.
DR OpenTargets; ENSG00000128266; -.
DR PharmGKB; PA28775; -.
DR VEuPathDB; HostDB:ENSG00000128266; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000160353; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P19086; -.
DR OMA; TMGCRQS; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P19086; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; P19086; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P19086; -.
DR SIGNOR; P19086; -.
DR BioGRID-ORCS; 2781; 16 hits in 1067 CRISPR screens.
DR ChiTaRS; GNAZ; human.
DR GeneWiki; GNAZ; -.
DR GenomeRNAi; 2781; -.
DR Pharos; P19086; Tbio.
DR PRO; PR:P19086; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P19086; protein.
DR Bgee; ENSG00000128266; Expressed in cortical plate and 141 other tissues.
DR Genevisible; P19086; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IEA:Ensembl.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; IEA:Ensembl.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Myristate; Nucleotide-binding; Palmitate;
KW Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..355
FT /note="Guanine nucleotide-binding protein G(z) subunit
FT alpha"
FT /id="PRO_0000203696"
FT DOMAIN 32..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="ADP-ribosylarginine; by cholera toxin"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 132
FT /note="W -> Y (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="G -> A (in Ref. 2; BAA14180)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="D -> N (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 40924 MW; E868FAE7CD2873EB CRC64;
MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG
FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR AYDAVQLFAL TGPAESKGEI
TPELLGVMRR LWADPGAQAC FSRSSEYHLE DNAAYYLNDL ERIAAADYIP TVEDILRSRD
MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ
TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA
AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC
