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Database: UniProt
Entry: A0A6J1R484_9HYME
LinkDB: A0A6J1R484_9HYME
Original site: A0A6J1R484_9HYME 
ID   A0A6J1R484_9HYME        Unreviewed;       852 AA.
AC   A0A6J1R484;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   SubName: Full=Regulator of G-protein signaling 9 isoform X4 {ECO:0000313|RefSeq:XP_024888988.1};
GN   Name=LOC112465603 {ECO:0000313|RefSeq:XP_024888988.1};
OS   Temnothorax curvispinosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Temnothorax.
OX   NCBI_TaxID=300111 {ECO:0000313|Proteomes:UP000504618, ECO:0000313|RefSeq:XP_024888988.1};
RN   [1] {ECO:0000313|RefSeq:XP_024888988.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole body {ECO:0000313|RefSeq:XP_024888988.1};
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
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DR   RefSeq; XP_024888988.1; XM_025033220.1.
DR   AlphaFoldDB; A0A6J1R484; -.
DR   GeneID; 112465603; -.
DR   Proteomes; UP000504618; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:TreeGrafter.
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:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd04450; DEP_RGS7-like; 1.
DR   CDD; cd00068; GGL; 1.
DR   CDD; cd08705; RGS_R7-like; 1.
DR   Gene3D; 1.10.1240.60; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR047016; RGS6/7/9/11.
DR   InterPro; IPR047017; RGS6/7/9/11_DHEX_sf.
DR   InterPro; IPR040759; RGS_DHEX.
DR   InterPro; IPR034483; RGS_Egl-10.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45746; LP21163P; 1.
DR   PANTHER; PTHR45746:SF5; REGULATOR OF G-PROTEIN SIGNALING 7; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   Pfam; PF18148; RGS_DHEX; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000504618};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700}.
FT   DOMAIN          35..110
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          311..427
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   REGION          450..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..460
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..634
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..772
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  95729 MW;  142F469E18E66963 CRC64;
     MEASSNQQQK EKEPRVHRPY AFDKMEGLVR EMQDPERGVP VRSQKQFLTS IPSAFMGYDL
     IEWLMDRLAI EESEAVHIAN QLCQYGYFFP VNDSKTLTVK DDSSLYRFQT PYYWPWQHRT
     PDNVEYAIYL AKRTLRNKQR HALEDYEIEA LNSLRKNLQN KWDIIQLQAE EQVRLSKERK
     KGDKIVSDSQ ERAFWRVYRP PPGCLSSLEV VPVPTRFRPG LPRPPSRKRT LTDLQREVAL
     LRNSLTRTRI KVSTAIENFK SYFETYVEYD PMFVQPQPSN PWITDDHMFW QLNSPLVEVP
     TEKRVKRWAL SMEELMSDPT GLQEFTNYLR KEYSHENIRF WLAVKDLRHS FQAQIPDKVN
     EIFREFLAPG APCEINIDGK TMEKVHQEMK NPSRFTFDSA AEHVYTLLLK KDCYPRFIRS
     DQYRNLLAAG VQPLQKKRFF GFGGQAKKKV SSTSTPTSST LQHANIGGGS GGGRRRGSDR
     SLSGSAHELA ICGVRDVTSA PRVPHSHSQS NLTDIPYRDA GATEVVVRPM DDVCPWEAVP
     GPSTEPGGTG DTASSGRTAS ADQTRHVWDS GGYSTTTYSA EAARASRKNS AQLDSCSSSS
     DVSLAIADVS ERLRKSCSLQ HSGSVGTSTS GPSTITRNYS TCSASGRIRL AEIGRASVSS
     CNYPSPQQSF EYSHAVVERV VEKLEERSSL EKIVPEEETV AEAIVEKESQ SSPKTTAKAP
     LISISAIVGD LPSDNSTMEN IDEDGSESCT AKDAGEIVAE EKLKGEDSRA DTGADVSPVA
     EEPATTEELP EETQVMPVWE PDAQQEDRPA VAQAVPREKR DNNVNEVCPW EDEENCRVDA
     PYVKTYATLG YL
//
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