ID A0A093I599_STRCA Unreviewed; 1355 AA.
AC A0A093I599;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Regulator of G-protein signaling 12 {ECO:0000313|EMBL:KFV87030.1};
DE Flags: Fragment;
GN ORFNames=N308_14031 {ECO:0000313|EMBL:KFV87030.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV87030.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV87030.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV87030.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL206928; KFV87030.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000021633; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd13162; PTB_RGS12; 1.
DR CDD; cd17136; RBD1_RGS12; 1.
DR CDD; cd17138; RBD2_RGS12; 1.
DR CDD; cd08742; RGS_RGS12; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR046995; RGS10/12/14-like.
DR InterPro; IPR037880; RGS12_RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45945:SF1; REGULATOR OF G-PROTEIN SIGNALING 12; 1.
DR PANTHER; PTHR45945; REGULATOR OF G-PROTEIN SIGNALING LOCO; 1.
DR Pfam; PF02188; GoLoco; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF02196; RBD; 1.
DR Pfam; PF00615; RGS; 1.
DR Pfam; PF16613; RGS12_us1; 1.
DR Pfam; PF16611; RGS12_us2; 1.
DR Pfam; PF16612; RGS12_usC; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00390; GoLoco; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00455; RBD; 2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50898; RBD; 2.
DR PROSITE; PS50132; RGS; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 22..99
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 226..338
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 708..825
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 957..1027
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 1029..1099
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT REGION 832..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1355
FT /evidence="ECO:0000313|EMBL:KFV87030.1"
SQ SEQUENCE 1355 AA; 149562 MW; 3A8A648A8062B3C9 CRC64;
MYRPGETVKR RLNVHAPPRI RSVEVARGRA GYGFTLSGQA PCILSCVMKG SPADYVGLKA
GDQIFAVNEI NVKKASHEDV VKLIGKCSGV LHMVIAEGIS HIDSCSSDEE VGFYDGKGWL
KPKPDSKALG INRAEKVVEE MQSGGIFNMI FEHPALCAGN SETSTPKQRS FSDSAAIKFE
TGNESMTNPN LLSKEEVSKV LNDDSVFRIG LESAEDFGLD ASILNVAMIV GYLGSIELPS
TTSNLENESL QAIRGCMRRL RAEQKIHSLV MMKIMHDCIQ LCSDKSGVVA EYPAEKLAFS
AVCPDDRRFF GLVTMQTNDD ASLAQEDEGV LRTSCHVFMV DPELFHHKIH QGIARRFGLE
CTADPDTNGC LEFPTSSLPV LQFISVLYRD MGELIEGMRA RAFLDGDADA HQNNSTSSNS
DSGIGNFNQE EKNNRVLVVD LGSNPSKHIP NSIWENPVGR GQNQSVSHWN GFCHEPEGNV
PLEVIQSDKS QNLSKHLSPS ARIEVPLVSA RNSVPPSKKS AAGIGNQRWL PVHVLQEWQH
GNASDQESYT DSTDGWSSVN CGTLPPPMSK IPADRYRVDG SFGQPQLKSH KNEWSKKMFC
MQNKFGPQHI IRKSKEEKKG AKFGHAVGLT QAPPQRSSVR RSFGRSKRFS ITRSLDDLES
ATVSDGELNS TDLKDCVSEN SLSSNASLPS VQSCRRLRER RVASWAVSFE RLLQDPVGIK
YFSEFLRKEF SEENILFWQA CEYFNHVPAH DKKELSYRAR EIFSKFLCSK ATTPVNIDSQ
AQLADDILNS PHPDMFKEQQ LQIFNLMKFD SYTRFLKSPL YQECILAEVE GRPLPDPQRV
PSSPTSKHSI SSEKSNISTP KKLSGKSKSG RSLNEESGEE DAEKKKRGTF FSWSRSKSLG
KSQKRKENGD YQNDSIQPNG LSYRRESQGS MSSAASLDLS EASRLPAFVP DKEKSPKYCS
VNLPDGSSSK MVVKSGFSIK EMLCGLCEKH GINIAAVDLF LVGGDKPLVL HQDSSILESR
DLRLEKRTLF RLDLVPINRS VGLKAKPTKP VTEVLRPVVA KYGLNLTELV ARLNGEQEPL
DLGVPISNLD GQRVVLDEKE PTKGRVFTDK QKGASVKQSA AVTSSSRNQV STGEGRALGK
SNSIKMKGEN GKNARDVRLS KREDSIAKIG KKKSQKINLD EAEEFFELIS KAQSNRADDQ
RGLLRKEDLI LPDFLRLPPT GPEPSSSTPA GLKGLNKRVS KNDGKDGCAS PSEKLESVQN
YNENSVKKMG YLENKHKSAL TTVNSQKTCS VPFNTTLSPI PHAQENSTTI WKRQSRELHA
EGIQMVDDEN VADLTLVAEG DISSPNSTLL PPPPP
//