ID W5MYH0_LEPOC Unreviewed; 567 AA.
AC W5MYH0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Regulator of G protein signaling 14 {ECO:0000313|Ensembl:ENSLOCP00000013429.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013429.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000013429.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01005331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MYH0; -.
DR Ensembl; ENSLOCT00000013458.1; ENSLOCP00000013429.1; ENSLOCG00000010943.1.
DR GeneTree; ENSGT00940000166254; -.
DR OMA; KRTAQYK; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000010943; Expressed in bone element and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd17139; RBD2_RGS14; 1.
DR CDD; cd08706; RGS_R12-like; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR046993; RBD2_RGS14.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR046995; RGS10/12/14-like.
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:SF2; REGULATOR OF G-PROTEIN SIGNALING 14; 1.
DR PANTHER; PTHR45945; REGULATOR OF G-PROTEIN SIGNALING LOCO; 1.
DR Pfam; PF02196; RBD; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00455; RBD; 2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50898; RBD; 2.
DR PROSITE; PS50132; RGS; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..567
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866764"
FT DOMAIN 64..181
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 312..383
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 385..455
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 63429 MW; 496A60AFF5A2EC90 CRC64;
MPKHWNLCCL SVKHITLAVS DGELNVTEGD GHGSTHSLNS NTSLPSVQSG SRRVERSVAS
WAVSFERLLE DPTGVRYFTA FLKSEVSAEN ILFWQACEKF RQIPPSQKDE LLREAREIYV
NYLSSNALHA INIDDTARIE ESLLDNPTPD MFQKAQQQIF KLMKFDSYTR FVRSQLYQKC
MLANVAGQPL PDLWPGSKSP GSILSLIQAK VLLKFKNSST ERERNVEDSS ERKRATLDGR
PSQDKSKRDK RLWNILNDLD CGNGQILVSR RESQSSVTSS TSVELGSFCN KGENGSSCPR
VTDQDKESRA VKYCCVYLPD GTASLAPVRA DLTVRDMLSG ICEKRGILLK DVKIYLKGND
KQPLSLDQES LVLTDQQVLL ETMITFTLEV VFLGKTVGIV AKSSKVLSEA LAPVLRKNEL
RPEEVVATIS GSQEPLNMSI PVMSLAKKKV LLDRIKEIHS ETSFVHQGMS MNLLSSPLNT
DIQTVGNEKV VSHIIILYIE LQSYKRKQVG ILLFKLKNYA LKAASLSSKG LIDLLSKVQN
SRVNDQRGLL CKENLVIPHF LQQPLRE
//