ID   GRP1_CAEEL              Reviewed;         393 AA.
AC   P34512;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=GTP exchange factor for ARFs 1;
GN   Name=grp-1; ORFNames=K06H7.4;
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.
RX   PubMed=22801495; DOI=10.1038/nature11240;
RA   Denning D.P., Hatch V., Horvitz H.R.;
RT   "Programmed elimination of cells by caspase-independent cell extrusion in
RT   C. elegans.";
RL   Nature 488:226-230(2012).
CC   -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF. Promotes the
CC       activation of ARF through replacement of GDP with GTP (By similarity).
CC       Plays a role in cell shedding during embryogenesis, probably by
CC       promoting the endocytosis of cell adhesion molecules (PubMed:22801495).
CC       {ECO:0000250, ECO:0000269|PubMed:22801495}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO080533; CCD64454.1; -; Genomic_DNA.
DR   PIR; S44844; S44844.
DR   RefSeq; NP_498764.1; NM_066363.3.
DR   AlphaFoldDB; P34512; -.
DR   SMR; P34512; -.
DR   BioGRID; 41346; 1.
DR   IntAct; P34512; 1.
DR   STRING; 6239.K06H7.4; -.
DR   EPD; P34512; -.
DR   PaxDb; P34512; -.
DR   PeptideAtlas; P34512; -.
DR   EnsemblMetazoa; K06H7.4.1; K06H7.4.1; WBGene00001743.
DR   GeneID; 176140; -.
DR   KEGG; cel:CELE_K06H7.4; -.
DR   UCSC; K06H7.4.1; c. elegans.
DR   CTD; 176140; -.
DR   WormBase; K06H7.4; CE26942; WBGene00001743; grp-1.
DR   eggNOG; KOG0930; Eukaryota.
DR   GeneTree; ENSGT00940000160865; -.
DR   HOGENOM; CLU_032820_3_0_1; -.
DR   InParanoid; P34512; -.
DR   OMA; PDTCYVL; -.
DR   OrthoDB; 657055at2759; -.
DR   PhylomeDB; P34512; -.
DR   PRO; PR:P34512; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   GO; GO:0030496; C:midbody; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   CDD; cd00171; Sec7; 1.
DR   Gene3D; 1.10.1000.11; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; SSF48425; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Guanine-nucleotide releasing factor; Reference proteome.
FT   CHAIN           1..393
FT                   /note="GTP exchange factor for ARFs 1"
FT                   /id="PRO_0000120220"
FT   DOMAIN          53..239
FT                   /note="SEC7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT   DOMAIN          261..377
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          12..54
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   393 AA;  45082 MW;  4466B2D5859C8F4A CRC64;
     MSSRYSERNG LSETEKMTLP KVRKRKAQLV DEIEALKNEV REVDEELDQV YYTHPKSKEY
     HKIVVNGRKK FNQDPWKALD WLASRNVVAK DPQALALWMK AGEGLSKSAI GEILGDNRPF
     ALETLDRFTK EHKLHDVPIV PALRQYLFSF RLPGESQKIN RILEKFAEVY ANQNPSYGNA
     DQAHTVAYSC IMVNTLLHNP NVKDKPSLEK YIEMNEQLLE KGAITIEQLT EVYESVSVTQ
     FKIPDEVSTS GKGTVNDILL HAEREGWLFK QSSNPLFSGA LSWKKRWFVL SENCLYYFDQ
     MTDKEPKGII TLANVGIRKV EAPSRPFMFE IFSLSDGQIK ACKTEQDGRL VEGRHSIYKI
     CAVNDEDMRS WINAISRMMA PQQHLLARPK STH