LOCUS       NP_653346                673 aa            linear   ROD 24-JUN-2024
DEFINITION  G-protein-signaling modulator 1 isoform a [Rattus norvegicus].
ACCESSION   NP_653346
VERSION     NP_653346.2
DBSOURCE    REFSEQ: accession NM_144745.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Conley,J.M. and Watts,V.J.
  TITLE     Differential effects of AGS3 expression on D(2L) dopamine
            receptor-mediated adenylyl cyclase signaling
  JOURNAL   Cell Mol Neurobiol 33 (4), 551-558 (2013)
   PUBMED   23504261
  REMARK    GeneRIF: AGS3 reduced D(2L)DR-mediated sensitization of AC1 and
            AC2.
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Wang,W., Li,Q., Zou,F., Yu,Z., Wang,Y., Lu,T., Hu,T. and Cui,G.
  TITLE     Increased expression of AGS3 in rat brain cortex after traumatic
            brain injury
  JOURNAL   J Neurosci Res 91 (5), 726-736 (2013)
   PUBMED   23404409
  REMARK    GeneRIF: This study demonistrated that the ags3 expression
            increassing in rat brain cortex after traumatic brain injury.
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Yuzawa,S., Kamakura,S., Iwakiri,Y., Hayase,J. and Sumimoto,H.
  TITLE     Structural basis for interaction between the conserved cell
            polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched
            protein (LGN)
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19210-19215 (2011)
   PUBMED   22074847
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Regner,K.R., Nozu,K., Lanier,S.M., Blumer,J.B., Avner,E.D.,
            Sweeney,W.E. Jr. and Park,F.
  TITLE     Loss of activator of G-protein signaling 3 impairs renal tubular
            regeneration following acute kidney injury in rodents
  JOURNAL   FASEB J 25 (6), 1844-1855 (2011)
   PUBMED   21343176
  REMARK    GeneRIF: These data suggest that Gpsm1 acts through a novel
            receptor-independent mechanism to facilitate renal tubular
            epithelial cell proliferation and renal tubular regeneration.
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Xu,Z., Xia,B., Gong,Q., Bailey,J., Groves,B., Radeke,M., Wood,S.A.,
            Szumlinski,K.K. and Ma,D.
  TITLE     Identification of a deubiquitinating enzyme as a novel
            AGS3-interacting protein
  JOURNAL   PLoS One 5 (3), e9725 (2010)
   PUBMED   20305814
  REMARK    GeneRIF: levels of AGS3 and USP9x are co-regulated in the
            prefrontal cortex of rats withdrawn from repeated cocaine treatment
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Bernard,M.L., Peterson,Y.K., Chung,P., Jourdan,J. and Lanier,S.M.
  TITLE     Selective interaction of AGS3 with G-proteins and the influence of
            AGS3 on the activation state of G-proteins
  JOURNAL   J Biol Chem 276 (2), 1585-1593 (2001)
   PUBMED   11042168
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Natochin,M., Lester,B., Peterson,Y.K., Bernard,M.L., Lanier,S.M.
            and Artemyev,N.O.
  TITLE     AGS3 inhibits GDP dissociation from galpha subunits of the Gi
            family and rhodopsin-dependent activation of transducin
  JOURNAL   J Biol Chem 275 (52), 40981-40985 (2000)
   PUBMED   11024022
REFERENCE   8  (residues 1 to 673)
  AUTHORS   De Vries,L., Fischer,T., Tronchere,H., Brothers,G.M.,
            Strockbine,B., Siderovski,D.P. and Farquhar,M.G.
  TITLE     Activator of G protein signaling 3 is a guanine dissociation
            inhibitor for Galpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 97 (26), 14364-14369 (2000)
   PUBMED   11121039
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Peterson,Y.K., Bernard,M.L., Ma,H., Hazard,S. 3rd, Graber,S.G. and
            Lanier,S.M.
  TITLE     Stabilization of the GDP-bound conformation of Gialpha by a peptide
            derived from the G-protein regulatory motif of AGS3
  JOURNAL   J Biol Chem 275 (43), 33193-33196 (2000)
   PUBMED   10969064
  REMARK    GeneRIF: The GPR motif in this protein and other proteins is
            actually associated with activity as a GDI - guanine nucleotide
            dissociation inhibitor and not GTPase activator as initially
            suggested.
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Takesono,A., Cismowski,M.J., Ribas,C., Bernard,M., Chung,P.,
            Hazard,S. 3rd, Duzic,E. and Lanier,S.M.
  TITLE     Receptor-independent activators of heterotrimeric G-protein
            signaling pathways
  JOURNAL   J Biol Chem 274 (47), 33202-33205 (1999)
   PUBMED   10559191
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB743977.1, AF107723.1, CB615566.1, BC105302.1 and BF408282.1.
            
            On Feb 28, 2009 this sequence version replaced NP_653346.1.
            
            Transcript Variant: This variant (1, also known as AGS3-LONG)
            represents the longer transcript and encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMD00132262,
                              SAMD00132263 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..673
                     /product="G-protein-signaling modulator 1 isoform a"
                     /note="activator of G-protein signaling 3; G-protein
                     signalling modulator 1 (AGS3-like, C. elegans); G-protein
                     signaling modulator 1 (AGS3-like, C. elegans)"
                     /calculated_mol_wt=74309
     Region          1..507
                     /region_name="Mediates association with membranes"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          31..56
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          68..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          69..322
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Site            order(70..71,74..75,77,107,110..111,114..115,117..118,147,
                     150..151,154..155,158)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          105..135
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(207,210..211,214..215,217,247,250..251,254..255,
                     257..258,287,290..291,294..295,298)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          207..234
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          239..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          286..313
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          290..358
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          320..354
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          361..485
                     /region_name="Interaction with STK11/LKB1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            418
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6IR34; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          420..477
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86YR5; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          494..515
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          510..544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          547..567
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          595..615
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          609..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Region          629..650
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          645..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9R080.2)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q9R080.2)"
     CDS             1..673
                     /gene="Gpsm1"
                     /gene_synonym="Ags3"
                     /coded_by="NM_144745.2:119..2140"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:246254"
                     /db_xref="RGD:628682"
ORIGIN      
        1 maspappaae elpgpaarrl ysrmeascle lalegerlck agdfkagvaf feaavqvgte
       61 dlktlsaiys qlgnayfylk eyaralqfhk hdlllartig drmgeakasg nlgntlkvlg
      121 rfdeaivccq rhldiaqeqg dkvgearaly nignvyhakg kqlswnaaqd pghlppdvre
      181 tlhrasefye rnlslvkelg draaqgrayg nlgnthyllg nfteattfhk erlaiakefg
      241 dkaaerrays nlgnahiflg rfdvaaehyk ktlqlsrqlr dqaveaqacy slgntytllq
      301 dyeraaeyhl rhlviaqela drvgegracw slgnayvsmg spaqaltfak khlqisqeig
      361 drngeltarm niahlqlalg rltspaaaek pdlagyeaqg arpkrtqrls aetwdllrlp
      421 ldreqngeth htgdwrgpsr dslplpmrsr kyqegpdaie rrpregshsp ldsadvrvqv
      481 prtgipraps sdeecffdll skfqssrmdd qrcpleegqa gaaeataapt leeraaqpsv
      541 taspqteeff dliassqsrr lddqrasvgs lpglritlnn vghlrgdgdp qepgdeffnm
      601 likyqssrid dqrcpppdvl prgptmpded ffsliqrvqa krmdeqrvdl agspdqeasg
      661 lpdprqqcpp gas
//
