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GNAI1_CHICK
ID   GNAI1_CHICK             Reviewed;         354 AA.
AC   P50146;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-1;
DE   AltName: Full=Adenylate cyclase-inhibiting G alpha protein;
GN   Name=GNAI1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7821803; DOI=10.1016/0378-1119(94)90449-9;
RA   Kilbourne E.J., Galper J.B.;
RT   "Cloning of cDNAs coding for the G alpha i1 and G alpha i2 G-proteins from
RT   chick brain.";
RL   Gene 150:341-344(1994).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as
CC       transducers downstream of G protein-coupled receptors (GPCRs) in
CC       numerous signaling cascades. The alpha chain contains the guanine
CC       nucleotide binding site and alternates between an active, GTP-bound
CC       state and an inactive, GDP-bound state. Signaling by an activated GPCR
CC       promotes GDP release and GTP binding. The alpha subunit has a low
CC       GTPase activity that converts bound GTP to GDP, thereby terminating the
CC       signal. Both GDP release and GTP hydrolysis are modulated by numerous
CC       regulatory proteins (By similarity). Signaling is mediated via effector
CC       proteins, such as adenylate cyclase. Inhibits adenylate cyclase
CC       activity, leading to decreased intracellular cAMP levels (By
CC       similarity). Required for cortical dynein-dynactin complex recruitment
CC       during metaphase (By similarity). {ECO:0000250|UniProtKB:P10824,
CC       ECO:0000250|UniProtKB:P63096}.
CC   -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC       and gamma. The alpha chain contains the guanine nucleotide binding
CC       site. Part of a spindle orientation complex. Identified in complex with
CC       the beta subunit GNB1 and the gamma subunit GNG1. Identified in complex
CC       with the beta subunit GNB1 and the gamma subunit GNG2. GTP binding
CC       causes dissociation of the heterotrimer, liberating the individual
CC       subunits so that they can interact with downstream effector proteins
CC       (By similarity). {ECO:0000250|UniProtKB:P10824,
CC       ECO:0000250|UniProtKB:P63096}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P10824}. Cell membrane
CC       {ECO:0000250|UniProtKB:P10824}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:P10824}.
CC       Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Membrane
CC       {ECO:0000250|UniProtKB:P10824}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P10824}.
CC   -!- PTM: Myristoylation at Gly-2 is required for membrane anchoring before
CC       palmitoylation. {ECO:0000250|UniProtKB:P10824}.
CC   -!- PTM: Palmitoylation at Cys-3 varies with membrane lipid composition.
CC       {ECO:0000250|UniProtKB:P10824}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L24548; AAA65066.1; -; mRNA.
DR   PIR; I50237; I50237.
DR   RefSeq; NP_990734.1; NM_205403.1.
DR   AlphaFoldDB; P50146; -.
DR   SMR; P50146; -.
DR   STRING; 9031.ENSGALP00000013640; -.
DR   PaxDb; P50146; -.
DR   GeneID; 396368; -.
DR   KEGG; gga:396368; -.
DR   CTD; 2770; -.
DR   VEuPathDB; HostDB:geneid_396368; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   InParanoid; P50146; -.
DR   OrthoDB; 754573at2759; -.
DR   PhylomeDB; P50146; -.
DR   PRO; PR:P50146; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0099738; C:cell cortex region; ISS:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISS:UniProtKB.
DR   GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:AgBase.
DR   GO; GO:0050805; P:negative regulation of synaptic transmission; ISS:AgBase.
DR   GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR   GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cell membrane; Cytoplasm; Cytoskeleton;
KW   GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Mitosis;
KW   Myristate; Nucleotide-binding; Nucleus; Palmitate; Reference proteome;
KW   Transducer; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63096"
FT   CHAIN           2..354
FT                   /note="Guanine nucleotide-binding protein G(i) subunit
FT                   alpha-1"
FT                   /id="PRO_0000203674"
FT   DOMAIN          32..354
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          35..48
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          173..181
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          196..205
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          265..272
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          324..329
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         43..48
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         150..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         175..178
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         200..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   BINDING         326
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P63096"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P10824"
SQ   SEQUENCE   354 AA;  40378 MW;  CA03F97E4EF534F2 CRC64;
     MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG
     YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDPTR ADDARQLFVL AGAAEEGFMT
     ADVAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQTSYIPT QQDVLRTRVK
     TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
     NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY AGSNTYEEAA
     AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
 
 
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