ID A0A1S2ZPI5_ERIEU Unreviewed; 99 AA.
AC A0A1S2ZPI5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Guanine nucleotide-binding protein subunit gamma {ECO:0000256|RuleBase:RU004973};
GN Name=GNG11 {ECO:0000313|RefSeq:XP_007522559.2};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007522559.2};
RN [1] {ECO:0000313|RefSeq:XP_007522559.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction. {ECO:0000256|RuleBase:RU004973}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma.
CC {ECO:0000256|RuleBase:RU004973}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU004973};
CC Lipid-anchor {ECO:0000256|RuleBase:RU004973}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU004973}.
CC -!- SIMILARITY: Belongs to the G protein gamma family.
CC {ECO:0000256|ARBA:ARBA00007431, ECO:0000256|RuleBase:RU004973}.
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DR RefSeq; XP_007522559.2; XM_007522497.2.
DR AlphaFoldDB; A0A1S2ZPI5; -.
DR STRING; 9365.ENSEEUP00000004599; -.
DR CTD; 2791; -.
DR eggNOG; KOG4119; Eukaryota.
DR InParanoid; A0A1S2ZPI5; -.
DR OrthoDB; 5344095at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809:SF1; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-11; 1.
DR PANTHER; PTHR13809; GUANINE NUCLEOTIDE-BINDING PROTEIN GAMMA SUBUNIT; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM01224; G_gamma; 1.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU004973}; Coiled coil {ECO:0000256|SAM:Coils};
KW Lipoprotein {ECO:0000256|RuleBase:RU004973};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004973};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU004973}.
FT DOMAIN 31..99
FT /note="G protein gamma"
FT /evidence="ECO:0000259|PROSITE:PS50058"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..72
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 99 AA; 11251 MW; E285F291147B3603 CRC64;
MDIQRQMCSS SSSTCRTVPG PSSEAKMPAL HIEDLPEKEK LKMEVEQLRK EVKLQRQQVS
KCSEEIKNYI EERSGEDPLV KGIPEDKNPF KEKGSCIIS
//