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G-protein-signaling modulator 1 (Activator of G-protein signaling 3)

 GPSM1_RAT               Reviewed;         673 AA.
Q9R080; Q8K3E2;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 2.
05-DEC-2018, entry version 133.
RecName: Full=G-protein-signaling modulator 1;
AltName: Full=Activator of G-protein signaling 3;
Name=Gpsm1; Synonyms=Ags3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH
GNAI2 AND GNAI3, AND MUTAGENESIS OF PHE-631; GLN-639 AND ARG-647.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=10559191; DOI=10.1074/jbc.274.47.33202;
Takesono A., Cismowski M.J., Ribas C., Bernard M., Chung P.,
Hazard S. III, Duzic E., Lanier S.M.;
"Receptor-independent activators of heterotrimeric G-protein signaling
pathways.";
J. Biol. Chem. 274:33202-33205(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley; TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Brown Norway; TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168 (ISOFORM 1).
TISSUE=Spinal ganglion;
Amgen EST program;
"Amgen rat EST program.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, INTERACTION WITH GNAI1; GNAI2; GNAI3 AND GNAO1, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=11121039; DOI=10.1073/pnas.97.26.14364;
de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B.,
Siderovski D.P., Farquhar M.G.;
"Activator of G protein signaling 3 is a guanine dissociation
inhibitor for Galpha i subunits.";
Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GNAI1; GNAI2 AND
GNAI3.
PubMed=11042168; DOI=10.1074/jbc.M005291200;
Bernard M.L., Peterson Y.K., Chung P., Jourdan J., Lanier S.M.;
"Selective interaction of AGS3 with G-proteins and the influence of
AGS3 on the activation state of G-proteins.";
J. Biol. Chem. 276:1585-1593(2001).
[7]
ALTERNATIVE SPLICING (ISOFORMS 2; 3 AND 4), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=11278352; DOI=10.1074/jbc.M007573200;
Pizzinat N., Takesono A., Lanier S.M.;
"Identification of a truncated form of the G-protein regulator AGS3 in
heart that lacks the tetratricopeptide repeat domains.";
J. Biol. Chem. 276:16601-16610(2001).
[8]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
PubMed=11832491; DOI=10.1074/jbc.M112185200;
Blumer J.B., Chandler L.J., Lanier S.M.;
"Expression analysis and subcellular distribution of the two G-protein
regulators AGS3 and LGN indicate distinct functionality. Localization
of LGN to the midbody during cytokinesis.";
J. Biol. Chem. 277:15897-15903(2002).
[9]
FUNCTION.
PubMed=12834360; DOI=10.1021/bi034561p;
Ma H., Peterson Y.K., Bernard M.L., Lanier S.M., Graber S.G.;
"Influence of cytosolic AGS3 on receptor-G protein coupling.";
Biochemistry 42:8085-8093(2003).
[10]
INTERACTION WITH STK11/LKB1 AND MACF1.
PubMed=12719437; DOI=10.1074/jbc.C200686200;
Blumer J.B., Bernard M.L., Peterson Y.K., Nezu J., Chung P.,
Dunican D.J., Knoblich J.A., Lanier S.M.;
"Interaction of activator of G-protein signaling 3 (AGS3) with LKB1, a
serine/threonine kinase involved in cell polarity and cell cycle
progression: phosphorylation of the G-protein regulatory (GPR) motif
as a regulatory mechanism for the interaction of GPR motifs with Gi
alpha.";
J. Biol. Chem. 278:23217-23220(2003).
[11]
FUNCTION, AND MUTAGENESIS OF ISOFORM 2.
PubMed=14726514; DOI=10.1074/jbc.M312660200;
Sato M., Gettys T.W., Lanier S.M.;
"AGS3 and signal integration by Galpha(s)- and Galpha(i)-coupled
receptors: AGS3 blocks the sensitization of adenylyl cyclase following
prolonged stimulation of a Galpha(i)-coupled receptor by influencing
processing of Galpha(i).";
J. Biol. Chem. 279:13375-13382(2004).
[12]
FUNCTION, AND INDUCTION.
PubMed=15091342; DOI=10.1016/S0896-6273(04)00159-X;
Bowers M.S., McFarland K., Lake R.W., Peterson Y.K., Lapish C.C.,
Gregory M.L., Lanier S.M., Kalivas P.W.;
"Activator of G protein signaling 3: a gatekeeper of cocaine
sensitization and drug seeking.";
Neuron 42:269-281(2004).
[13]
FUNCTION.
PubMed=15937104; DOI=10.1073/pnas.0503419102;
Yao L., McFarland K., Fan P., Jiang Z., Inoue Y., Diamond I.;
"Activator of G protein signaling 3 regulates opiate activation of
protein kinase A signaling and relapse of heroin-seeking behavior.";
Proc. Natl. Acad. Sci. U.S.A. 102:8746-8751(2005).
[14]
TISSUE SPECIFICITY.
PubMed=16154268; DOI=10.1016/j.neulet.2005.08.043;
Taymans J.-M., Kia H.K., Langlois X.;
"Activator of G protein signaling type 3 mRNA is widely distributed in
the rat brain and is particularly abundant in the subventricular zone-
olfactory bulb system of neural precursor cell proliferation,
migration and differentiation.";
Neurosci. Lett. 391:116-121(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-543; SER-567
AND SER-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which
functions as a receptor-independent activator of heterotrimeric G-
protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound
form thus uncoupling heterotrimeric G-proteins signaling from G
protein-coupled receptors. Controls spindle orientation and
asymmetric cell fate of cerebral cortical progenitors. May also be
involved in macroautophagy in intestinal cells. May play a role in
drug addiction. {ECO:0000269|PubMed:10559191,
ECO:0000269|PubMed:11042168, ECO:0000269|PubMed:11121039,
ECO:0000269|PubMed:12834360, ECO:0000269|PubMed:14726514,
ECO:0000269|PubMed:15091342, ECO:0000269|PubMed:15937104}.
-!- SUBUNIT: Interacts with INSC/inscuteable and FRMPD1 (By
similarity). Interacts with GNAI1, GNAI2 and GNAI3 preferentially
in their GDP-bound state. May also interact with GNAO1. Interacts
with STK11/LKB1 and MACF1. {ECO:0000250,
ECO:0000269|PubMed:10559191, ECO:0000269|PubMed:11042168,
ECO:0000269|PubMed:11121039, ECO:0000269|PubMed:12719437}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein; Cytoplasmic side. Golgi apparatus membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Cytoplasm, cytosol. Note=Isoform 2 is not
associated with membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=1;
IsoId=Q9R080-1; Sequence=Displayed;
Name=2; Synonyms=Short-1;
IsoId=Q9R080-2; Sequence=VSP_039034;
Note=Produced by initiation at Met-62 of isoform 3. Mutagenesis
of Met-1 into Gly prevents expression of this isoform. Combined
mutagenesis of Gln-57, Gln-105 and Gln-129 into Ala alters the
function of the GoLoco domains.;
Name=3; Synonyms=Short-2;
IsoId=Q9R080-3; Sequence=VSP_039035;
Note=Minor isoform. Mutagenesis of Met-1 into Gly leads to
expression of isoform 2.;
Name=4; Synonyms=Long;
IsoId=Q9R080-4; Sequence=VSP_039036;
Note=Produced by alternative splicing.;
-!- TISSUE SPECIFICITY: Isoform 4 is specifically expressed in brain
by neurons and also detected in testis, liver, kidney, heart and
pancreas (at protein level). Highly expressed in cerebellum and
subventricular zone-olfactory bulb system. Isoform 2 and isoform 3
are specifically expressed in heart and are also detected in
brain. {ECO:0000269|PubMed:11121039, ECO:0000269|PubMed:11278352,
ECO:0000269|PubMed:11832491, ECO:0000269|PubMed:16154268}.
-!- DEVELOPMENTAL STAGE: Expression reaches a maximum at postnatal day
7 before to significantly decrease. {ECO:0000269|PubMed:11832491}.
-!- INDUCTION: Up-regulated in prefrontal cortex and core region of
nucleus accumbens during late withdrawal from chronic cocaine
administration. {ECO:0000269|PubMed:15091342}.
-!- DOMAIN: The GoLoco domains mediate interaction with G(i/o) alpha.
The GoLoco domains are essential for the GDI activity toward
G(i/o) alpha.
-!- PTM: Phosphorylation regulates interaction with G(i/o) alpha.
{ECO:0000250}.
-!- MISCELLANEOUS: Responsible for altered neurotransmission and
altered behavior like drug seeking associated with cocaine
addiction. Depletion in prefrontal cortex reverses the behavioral
consequences of cocaine addiction while overexpression in drug-
naive animals induces addictive behavior upon acute cocaine
injection.
-!- SIMILARITY: Belongs to the GPSM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF107723; AAF08683.1; -; mRNA.
EMBL; AY136742; AAN01268.1; -; mRNA.
EMBL; BC086535; AAH86535.1; -; mRNA.
EMBL; CB583569; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; NP_001138941.1; NM_001145469.1. [Q9R080-2]
RefSeq; NP_653346.2; NM_144745.2.
RefSeq; XP_008759842.1; XM_008761620.2. [Q9R080-3]
UniGene; Rn.53933; -.
ProteinModelPortal; Q9R080; -.
SMR; Q9R080; -.
BioGrid; 251555; 1.
CORUM; Q9R080; -.
STRING; 10116.ENSRNOP00000062075; -.
iPTMnet; Q9R080; -.
PhosphoSitePlus; Q9R080; -.
PaxDb; Q9R080; -.
PRIDE; Q9R080; -.
Ensembl; ENSRNOT00000084567; ENSRNOP00000070079; ENSRNOG00000018666. [Q9R080-2]
GeneID; 246254; -.
KEGG; rno:246254; -.
UCSC; RGD:628682; rat. [Q9R080-1]
CTD; 26086; -.
RGD; 628682; Gpsm1.
eggNOG; KOG1130; Eukaryota.
eggNOG; ENOG410XP6N; LUCA.
GeneTree; ENSGT00940000154667; -.
HOGENOM; HOG000231543; -.
HOVERGEN; HBG051823; -.
InParanoid; Q9R080; -.
KO; K15839; -.
PhylomeDB; Q9R080; -.
Reactome; R-RNO-418594; G alpha (i) signalling events.
PRO; PR:Q9R080; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000018666; Expressed in 10 organ(s), highest expression level in heart.
ExpressionAtlas; Q9R080; baseline and differential.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:RGD.
GO; GO:0030695; F:GTPase regulator activity; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:RGD.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR003109; GoLoco_motif.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
Pfam; PF02188; GoLoco; 4.
SMART; SM00390; GoLoco; 4.
SMART; SM00028; TPR; 6.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50877; GOLOCO; 4.
PROSITE; PS50005; TPR; 6.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
Endoplasmic reticulum; Golgi apparatus; Membrane; Methylation;
Neurogenesis; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
CHAIN 1 673 G-protein-signaling modulator 1.
/FTId=PRO_0000252404.
REPEAT 28 61 TPR 1.
REPEAT 66 99 TPR 2.
REPEAT 106 139 TPR 3.
REPEAT 146 178 TPR 4.
REPEAT 180 199 TPR 5.
REPEAT 206 239 TPR 6.
REPEAT 246 279 TPR 7.
REPEAT 286 319 TPR 8.
REPEAT 326 359 TPR 9.
DOMAIN 493 515 GoLoco 1. {ECO:0000255|PROSITE-
ProRule:PRU00097}.
DOMAIN 546 568 GoLoco 2. {ECO:0000255|PROSITE-
ProRule:PRU00097}.
DOMAIN 594 616 GoLoco 3. {ECO:0000255|PROSITE-
ProRule:PRU00097}.
DOMAIN 628 650 GoLoco 4. {ECO:0000255|PROSITE-
ProRule:PRU00097}.
REGION 1 507 Mediates association with membranes.
REGION 361 485 Interaction with STK11/LKB1.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:Q86YR5}.
MOD_RES 418 418 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q6IR34}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000250|UniProtKB:Q86YR5}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000250|UniProtKB:Q86YR5}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:Q86YR5}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000250|UniProtKB:Q86YR5}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 1 507 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_039034.
VAR_SEQ 1 446 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_039035.
VAR_SEQ 1 23 Missing (in isoform 4).
{ECO:0000303|PubMed:10559191}.
/FTId=VSP_039036.
MUTAGEN 631 631 F->R: Loss of interaction with GNAI2 and
GNAI3. {ECO:0000269|PubMed:10559191}.
MUTAGEN 639 639 Q->A: Loss of interaction with GNAI2 and
GNAI3. {ECO:0000269|PubMed:10559191}.
MUTAGEN 647 647 R->F: Loss of interaction with GNAI2 and
GNAI3. {ECO:0000269|PubMed:10559191}.
SEQUENCE 673 AA; 74440 MW; 40BE412E27011C00 CRC64;
MASPAPPAAE ELPGPAARRL YSRMEASCLE LALEGERLCK AGDFKAGVAF FEAAVQVGTE
DLKTLSAIYS QLGNAYFYLK EYARALQFHK HDLLLARTIG DRMGEAKASG NLGNTLKVLG
RFDEAIVCCQ RHLDIAQEQG DKVGEARALY NIGNVYHAKG KQLSWNAAQD PGHLPPDVRE
TLHRASEFYE RNLSLVKELG DRAAQGRAYG NLGNTHYLLG NFTEATTFHK ERLAIAKEFG
DKAAERRAYS NLGNAHIFLG RFDVAAEHYK KTLQLSRQIR DQAVEAQACY SLGNTYTLLQ
DYERAAEYHL RHLVIAQELA DRVGEGRACW SLGNAYVSMG SPAQALTFAK KHLQISQEIG
DRNGELTARM NIAHLQLALG RLTSPAAAEK PDLAGYEAQG ARPKRTQRLS AETWDLLRLP
LDREQNGETH HTGDWRGPSR DSLPLPMRSR KYQEGPDAIE RRPREGSHSP LDSADVRVQV
PRTGIPRAPS SDEECFFDLL SKFQSSRMDD QRCPLEEGQA GAAEATAAPT LEERAAQPSV
TASPQTEEFF DLIASSQSRR LDDQRASVGS LPGLRITLNN VGHLRGDGDP QEPGDEFFNM
LIKYQSSRID DQRCPPPDVL PRGPTMPDED FFSLIQRVQA KRMDEQRVDL AGSPDQEASG
LPDPRQQCPP GAS


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