ID C3XW70_BRAFL Unreviewed; 743 AA. AC C3XW70; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 07-SEP-2016, entry version 43. DE RecName: Full=Guanine nucleotide-binding protein subunit gamma {ECO:0000256|RuleBase:RU004973}; GN ORFNames=BRAFLDRAFT_117155 {ECO:0000313|EMBL:EEN67604.1}; OS Branchiostoma floridae (Florida lancelet) (Amphioxus). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Branchiostomidae; OC Branchiostoma. OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554}; RN [1] {ECO:0000313|EMBL:EEN67604.1, ECO:0000313|Proteomes:UP000001554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67604.1, RC ECO:0000313|Proteomes:UP000001554}; RC TISSUE=Testes {ECO:0000313|EMBL:EEN67604.1}; RX PubMed=18563158; DOI=10.1038/nature06967; RG US DOE Joint Genome Institute (JGI-PGF); RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., RA Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., RA Jurka J., Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., RA Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., RA Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., RA Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., RA Satoh N., Rokhsar D.S.; RT "The amphioxus genome and the evolution of the chordate karyotype."; RL Nature 453:1064-1071(2008). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are CC involved as a modulator or transducer in various transmembrane CC signaling systems. The beta and gamma chains are required for the CC GTPase activity, for replacement of GDP by GTP, and for G protein- CC effector interaction. {ECO:0000256|RuleBase:RU004973}. CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and CC gamma. {ECO:0000256|SAAS:SAAS00551442}. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and CC gamma. {ECO:0000256|RuleBase:RU004973}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000256|RuleBase:RU004973}; Lipid-anchor CC {ECO:0000256|RuleBase:RU004973}; Cytoplasmic side CC {ECO:0000256|RuleBase:RU004973}. CC -!- SIMILARITY: Belongs to the G protein gamma family. CC {ECO:0000256|RuleBase:RU004973}. 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; GG666471; EEN67604.1; -; Genomic_DNA. DR RefSeq; XP_002611594.1; XM_002611548.1. DR STRING; 7739.JGI117155; -. DR GeneID; 7207805; -. DR KEGG; bfo:BRAFLDRAFT_117155; -. DR eggNOG; KOG4119; Eukaryota. DR eggNOG; KOG4171; Eukaryota. DR eggNOG; COG2114; LUCA. DR InParanoid; C3XW70; -. DR KO; K12319; -. DR OMA; QPGRINI; -. DR Proteomes; UP000001554; Partially assembled WGS sequence. DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd00068; GGL; 1. DR Gene3D; 3.30.70.1230; -; 1. DR Gene3D; 4.10.260.10; -; 1. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR015898; G-protein_gamma-like_dom. DR InterPro; IPR001770; Gprotein-gamma. DR InterPro; IPR011644; Heme_NO-bd. DR InterPro; IPR011645; HNOB_dom_associated. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR029787; Nucleotide_cyclase. DR Pfam; PF00631; G-gamma; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF07700; HNOB; 1. DR Pfam; PF07701; HNOBA; 1. DR PRINTS; PR00321; GPROTEING. DR SMART; SM00044; CYCc; 1. DR SMART; SM00224; GGL; 1. DR SUPFAM; SSF111126; SSF111126; 1. DR SUPFAM; SSF48670; SSF48670; 1. DR SUPFAM; SSF55073; SSF55073; 2. DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU004973}; KW Complete proteome {ECO:0000313|Proteomes:UP000001554}; KW Lipoprotein {ECO:0000256|RuleBase:RU004973}; KW Membrane {ECO:0000256|RuleBase:RU004973}; KW Reference proteome {ECO:0000313|Proteomes:UP000001554}; KW Transducer {ECO:0000256|RuleBase:RU004973, KW ECO:0000256|SAAS:SAAS00551443}. FT DOMAIN 1 47 G protein gamma. {ECO:0000259|PROSITE: FT PS50058}. FT DOMAIN 570 727 Guanylate cyclase. {ECO:0000259|PROSITE: FT PS50125}. SQ SEQUENCE 743 AA; 83147 MW; C4C42EBCFD8B532A CRC64; MSNSIAQAHK TVDQLRFEAQ IERIRVSKAA ADLQAYCEQH ARDDPLLDSA AEVETKIVVL QRRYAPQQQE VTTITVESAG NKSWYRTRVF YWDVPAENSG DISREVDVEE HVTSRRVILI FNFAENQTFV RVHPLCAGGS GGSWLRRVDM AAHRKIGMTS QRVVRMKRKA ERFAKFVGFA PTHGGANVHQ ISREAVLESM GEHFVRYCIE FGFGSLLRVL GGSLKDFLCN LDSLHEHLAS TYPGIRSPSF CCTEGPDDTL FLHYYSERSG LYPIVKGLVR MIAKEFFNVS VAVDVVSEER ELTSCQGQVV TFSIRHLSCN GDPPGDEKRL SSGTICPTTS SDPKDLPLSV DTFNDIFPFH VMLDRDLKVV QMGRSLKRLL KSNVTSAELR FQDIFEIIRP KVESLFSDIV RHLNTIYVVR TVQGIINKGK DCTAQACEGA SNSASVDVEE STLRLKGEMV FVTESDMLLF LCSPRVKDLS EFLRKGLYFS DTPLHDSSRD VLMVNYLRRR ERDLLDKIED VGNQLRKLQG RLSEDKRRTE ELLHSILPSN AVQSLVSNSP VEAEAHPVVS ILFSDIVNFT GICERVEPMD IVRMLNKLYT SFDVLSKLNE LYKVETIGDA YMVAGGIPEK VDDHADRVVT MAVGMMDVSR TVTSPDGDKP ISIRVPETLS RYLAYECVQN TLLSSMSLPF QIRVGVHSGP CMAGVVGTTM PRYCLFGNTV SLASKMESCS QPGKINISDA TKM //