GPR2_CAEEL
ID GPR2_CAEEL Reviewed; 525 AA.
AC Q03569;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=G-protein regulator 2;
GN Name=gpr-2; ORFNames=C38C10.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14534135; DOI=10.1242/dev.00790;
RA Tsou M.-F.B., Hayashi A., Rose L.S.;
RT "LET-99 opposes Galpha/GPR signaling to generate asymmetry for spindle
RT positioning in response to PAR and MES-1/SRC-1 signaling.";
RL Development 130:5717-5730(2003).
RN [4]
RP FUNCTION, INTERACTION WITH GPR-1, AND SUBCELLULAR LOCATION.
RX PubMed=12730122; DOI=10.1101/gad.1081203;
RA Srinivasan D.G., Fisk R.M., Xu H., van den Heuvel S.;
RT "A complex of LIN-5 and GPR proteins regulates G protein signaling and
RT spindle function in C elegans.";
RL Genes Dev. 17:1225-1239(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18694560; DOI=10.1016/j.devcel.2008.06.002;
RA Panbianco C., Weinkove D., Zanin E., Jones D., Divecha N., Gotta M.,
RA Ahringer J.;
RT "A casein kinase 1 and PAR proteins regulate asymmetry of a PIP(2)
RT synthesis enzyme for asymmetric spindle positioning.";
RL Dev. Cell 15:198-208(2008).
CC -!- FUNCTION: In the 1-cell embryo, probably together with gpr-1, controls
CC nuclear rotation and spindle elongation during mitosis
CC (PubMed:14534135). Complex of gpr-1 and gpr-2, in association with lin-
CC 5, activates G-protein signaling to affect mitotic spindle force
CC (PubMed:12730122). Polarity determinants (par genes) may regulate lin-
CC 5/gpr-1/gpr-2/goa-1 locally to create the asymmetric forces that drive
CC spindle movement (PubMed:12730122). {ECO:0000269|PubMed:12730122,
CC ECO:0000269|PubMed:14534135}.
CC -!- SUBUNIT: Interacts with gpr-1; gpr-1 forms a complex with lin-5 and
CC GDP-bound goa-1. {ECO:0000269|PubMed:12730122}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:12730122}. Note=Located to
CC the spindle and cell cortex when in complex with lin-5 and gpr-1
CC (PubMed:12730122). During early embryogenesis, cortical localization
CC changes with the cell cycle. In one-cell embryo, uniform cortical
CC localization from prophase to metaphase and posterior enrichment during
CC anaphase. In the 2-cell embryo, uniform cortical localization in AB
CC blastomere and posterior cortical enrichment in P1 blastomere during
CC interphase. In P1, uniform cortical localization from prophase to early
CC anaphase and then posterior cortical enrichment during late anaphase
CC and telophase (PubMed:14534135, PubMed:12730122). Cortical localization
CC and asymmetrical distribution is regulated by the csnk-1-mediated
CC regulation of pkk-1 (PubMed:18694560). Enriched at the contact site
CC between EMS and P2 from prophase to prometaphase (PubMed:14534135).
CC {ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135,
CC ECO:0000269|PubMed:18694560}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous RNAi-mediated knockdown of both gpr-
CC 1 and gpr-2 causes, in the 1-cell embryo, a decrease in nuclear and
CC spindle movements during prophase, reduced asymmetric spindle
CC elongation during anaphase and mispositioning of nuclei after cell
CC division. {ECO:0000269|PubMed:14534135}.
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DR EMBL; Z19153; CAA79548.1; -; Genomic_DNA.
DR PIR; S28288; S28288.
DR RefSeq; NP_499066.1; NM_066665.5.
DR AlphaFoldDB; Q03569; -.
DR SMR; Q03569; -.
DR BioGRID; 41516; 5.
DR ComplexPortal; CPX-4027; gpr-1-gpr-2-lin-5 complex.
DR STRING; 6239.C38C10.4; -.
DR EPD; Q03569; -.
DR PaxDb; Q03569; -.
DR PeptideAtlas; Q03569; -.
DR EnsemblMetazoa; C38C10.4.1; C38C10.4.1; WBGene00001689.
DR GeneID; 176318; -.
DR KEGG; cel:CELE_C38C10.4; -.
DR UCSC; C38C10.4; c. elegans.
DR CTD; 176318; -.
DR WormBase; C38C10.4; CE00107; WBGene00001689; gpr-2.
DR eggNOG; ENOG502TGM6; Eukaryota.
DR GeneTree; ENSGT00970000196587; -.
DR HOGENOM; CLU_517044_0_0_1; -.
DR InParanoid; Q03569; -.
DR OrthoDB; 962799at2759; -.
DR PRO; PR:Q03569; -.
DR Proteomes; UP000001940; Chromosome III.
DR GO; GO:0005818; C:aster; IDA:WormBase.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:ComplexPortal.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IC:ComplexPortal.
DR GO; GO:0000022; P:mitotic spindle elongation; IC:ComplexPortal.
DR GO; GO:0007097; P:nuclear migration; IC:ComplexPortal.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SMART; SM00390; GoLoco; 1.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50877; GOLOCO; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Reference proteome.
FT CHAIN 1..525
FT /note="G-protein regulator 2"
FT /id="PRO_0000087563"
FT DOMAIN 424..445
FT /note="GoLoco"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 489..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 60129 MW; 00912EA46E390B7E CRC64;
MDVSYYDGPK DEVIEAMLKS AVTAMKLGQY EDGKGRLEDT MEFGTSNFQL LGTIYMYYGR
VCRHLNHDAK ALEFFEHELN MFKLIFNYPE ACDSTRRIVQ QALKMEKFSK ARRFAEDLID
YTSNKKNGEK YIGQARILFA SVCLEGCERD VESNQDEKKK LLSICAEQIA AVKLFNENNT
EGAVSETKIM LIEAKCLSLD EKYEESRRKY QECIDFAIKT DQFEAVHIAY YDKALYAETY
LLFFIIRDLR SALFYATKFG KERDVVKYKS KLSEEMLRNG EFHEAYLYGL EALVSIRKLG
LNEHIGDVLL TIAKCLIALG KRRQAAYFII LGSVLTINQS SFKLFYEQID VAMNQERSET
ATDQDACLAI DSSPDPTSSN DMINKFVVKL EHATNVETWE MIVNGIIEDQ KKPVAIEKKE
NEEPVDMMDL IFSMSSRMDD QRTELSAARF IPPRPVSSAS KKTTKSHRIL PGLRANWTKV
QSMKFDGHTM NRILKRSKKS KSSLDSTNSI QGDDTRSDDV TMTSK
