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Database: UniProt
Entry: A0A286XJR1_CAVPO
LinkDB: A0A286XJR1_CAVPO
Original site: A0A286XJR1_CAVPO 
ID   A0A286XJR1_CAVPO        Unreviewed;      1431 AA.
AC   A0A286XJR1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Regulator of G protein signaling 12 {ECO:0000313|Ensembl:ENSCPOP00000025553.1};
GN   Name=RGS12 {ECO:0000313|Ensembl:ENSCPOP00000025553.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000025553.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000025553.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000025553.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC       {ECO:0000256|ARBA:ARBA00004279}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; AAKN02055219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_013013129.1; XM_013157675.1.
DR   STRING; 10141.ENSCPOP00000025553; -.
DR   Ensembl; ENSCPOT00000033635.1; ENSCPOP00000025553.1; ENSCPOG00000005334.4.
DR   GeneID; 100713051; -.
DR   KEGG; cpoc:100713051; -.
DR   CTD; 6002; -.
DR   VEuPathDB; HostDB:ENSCPOG00000005334; -.
DR   eggNOG; KOG3589; Eukaryota.
DR   GeneTree; ENSGT00940000159741; -.
DR   InParanoid; A0A286XJR1; -.
DR   OMA; HKSEWSK; -.
DR   OrthoDB; 22856at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000005334; Expressed in frontal cortex and 13 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProt.
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; 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; 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   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          23..100
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          226..338
FT                   /note="PID"
FT                   /evidence="ECO:0000259|PROSITE:PS01179"
FT   DOMAIN          714..831
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          962..1032
FT                   /note="RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50898"
FT   DOMAIN          1034..1104
FT                   /note="RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50898"
FT   REGION          159..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1238..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1391..1431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..896
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..942
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1154..1168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1313..1334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1346..1360
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1397..1412
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1431 AA;  154875 MW;  E4555EBB7CEF78BB CRC64;
     MMYRAGEPVK RPPLGPVPPR LRSVEVARGR AGYGFTLAGQ APCVLSGVIR GSPADFVGLR
     AGDQIFTINE INVKKASHED VVKLIGKCSG VLRLVIGEGA GHPEACSSDD EGGLCEGKGW
     LRPKLDSKAL GINRAERVVE EMQSGGIFSM IFENPSLCMS TPEPSQGKQR SLSESASVRL
     EGSPNAVQTG LLSKEELVRV IHDDSVFSAG PENLDSFALD ASILNVAMVV GYLGSIELPS
     TSCNLESDSL QAIRGCMRRL RAEQKIHSLV TMKVMHDRVL LCSDKACVVA EYPAEKLAFS
     AVCPDDRRFF GLVTMQTNDD GSLAQGEEGA LRTSCHVFMV DPDLFHHKIH QGIARRFGFM
     CTADPDTSGC LEFPASSLPV LQFISILYRD MGEFIEGVRA RAFLDGDADA HQNNSTSSNS
     DSGIGNFNQE EKSNRVLVVD LGGGLSRHGP GSSASWEGAG ARSSQSWAAS WSRSFCHSPE
     GCASFEAGPQ ADRLRDLSKH LGPASHTEGT PASLWSSVPP SKRGSASTSC GLSQRWLPVH
     VLQEWQCGHA SDQESYTDST DGWSSVNCGT LPPPMSKIPA DRYRVEGSFM QAPLSAQKRD
     WARKAFGMQN LFGPSRNVRR TKEDKKGSKF GRGIGLAQTS QRSSARRSFR RSKRFSITRS
     LDDLESATVS DGELTGADLK DCVSSNSLSS NASLPSVQSC RRLRERRVAS WAVSFERLLQ
     DPVGIRYFSD FLRKEFSEEN ILFWQACEYF NHVPAHDKKE LSHRAREIFS KFLCSKATTP
     VNIDSQAQLA DDILNAPHPD MFKEQQLQIF NLMKFDSYTR FLKSQLYQEC ILAEVEGRAL
     PDAQQVPSSP ASKHSIGSDH SSTSTPKKLS GKSKSGRSLN EDAGDEDSEK KRKGAFFSWS
     RSRSTGRSQK KKEPGDHGQD TLPTNGGLCR RRESQGSVSS AGSLDLPEAC RTLVPEKDKA
     VKHCCIYLPD GATCVVAVKS GFSIKEILAG LCERHGINGA AVDLFLVGGD KPLVLHQDSS
     ILASRDLRLE KRTLFRLDLV PINRSVGLKA KPTKPVTEVL RPVVAKYGLD LGSLLVRLSG
     EKEPLDLGAP ISSLDGQRVV LEERDPARGR APTDKQKGAL AKPSAAASSR PRDRSATGEE
     RTLGKSNSIK IKGENGKNAR DPRLSKREES IAKIGKKKYQ KINLDEAEEF FELISKAQSN
     RADDQRGLLT KEDLVLPEFL RLPPGSTKLP LCTLAAGKGF SKRPETTGHS REKASLPSDS
     PATSPGSTQS TSSAQSPGSA QSPGSAHSPS GPRGASPLGQ KVQEGPTQVW RRRQSQEVED
     GGIQTEDESR ADLTLVGEGD ISSPNSTLLP PPPSPQDAPG PLRPGGRARG SQGLPVNRIF
     DVDLAAGMAP RVWPGPRRAR PMRPPASDCP GQSPSPGEPK AKLSTHHATF V
//
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