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GPR1_CAEEL
ID   GPR1_CAEEL              Reviewed;         525 AA.
AC   Q95QJ7; P34408;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=G-protein regulator 1;
GN   Name=gpr-1; ORFNames=F22B7.13;
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; LIN-5 AND GOA-1, AND SUBCELLULAR
RP   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-2, 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, lin-5 and GDP-bound goa-1.
CC       {ECO:0000269|PubMed:12730122}.
CC   -!- INTERACTION:
CC       Q95QJ7; Q9N2V6: gpa-16; NbExp=2; IntAct=EBI-316069, EBI-1005005;
CC       Q95QJ7; O01488: kxd-1; NbExp=5; IntAct=EBI-316069, EBI-320537;
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-2
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; FO080222; CCD62140.1; -; Genomic_DNA.
DR   PIR; S44636; S44636.
DR   RefSeq; NP_498900.1; NM_066499.3.
DR   AlphaFoldDB; Q95QJ7; -.
DR   SMR; Q95QJ7; -.
DR   BioGRID; 41414; 12.
DR   ComplexPortal; CPX-4027; gpr-1-gpr-2-lin-5 complex.
DR   DIP; DIP-26900N; -.
DR   IntAct; Q95QJ7; 6.
DR   STRING; 6239.F22B7.13; -.
DR   EPD; Q95QJ7; -.
DR   PaxDb; Q95QJ7; -.
DR   PeptideAtlas; Q95QJ7; -.
DR   EnsemblMetazoa; F22B7.13.1; F22B7.13.1; WBGene00001688.
DR   GeneID; 176210; -.
DR   KEGG; cel:CELE_F22B7.13; -.
DR   UCSC; F22B7.13; c. elegans.
DR   CTD; 176210; -.
DR   WormBase; F22B7.13; CE24910; WBGene00001688; gpr-1.
DR   eggNOG; ENOG502TGM6; Eukaryota.
DR   GeneTree; ENSGT00970000196587; -.
DR   HOGENOM; CLU_517044_0_0_1; -.
DR   InParanoid; Q95QJ7; -.
DR   OMA; MNSRMDD; -.
DR   OrthoDB; 962799at2759; -.
DR   PRO; PR:Q95QJ7; -.
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:0001965; F:G-protein alpha-subunit binding; IPI:WormBase.
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; 1.
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 1"
FT                   /id="PRO_0000087562"
FT   DOMAIN          424..445
FT                   /note="GoLoco"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT   REGION          488..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;  60128 MW;  EC68F930E3622AB5 CRC64;
     MDVSYYDGPK DEVAEAMLKS AVTAMRLGQY EDGKGRLEEI MEFGTSNFQL LGTIYMYYGR
     VCRHLNHDAK ALEFFEHELN MFKLIFNYPE ACDSTRRIVE QALKMGKFPK ARRFAEDLID
     YTSNKKNGEK YIGQARILFA SVCLEGCERD VESNQDEKKK LLSICAEQIA AVKLFNENNT
     EGAVSETKIM LLEAKCLSLD EKYEESRRKY QECIDFAIKT DQFEAVHIAY YDKALYAETD
     LLFFIIRDLR SALFYATKFG KERDVVKYKS KLSEEMLRNG EFHEAYLYGL EALVSIRKLG
     LNEYIGDVLL TIAKCLIALG KRRQAAYFII LGSVLTINQN SFKLFYEQID VAMNQERSET
     ATDQDVCLAI DSSPDPTSSN DMINKFVVEL EHATNVETWE MIVNGIIDDQ KKPVAIEKKE
     NEEPVDMMDL IFSMSSRMDD QRTELPAARF IPPRPVSSAS KKTTKSHRIL PGLRANWTKV
     QSMKFDGHTM NRILKRSKKS KSSLDSTNSM QGDDTRSDDV TMTSK
 
 
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