GBAS1_CAEEL
ID GBAS1_CAEEL Reviewed; 758 AA.
AC Q9TZI4; Q86RS8;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=G-protein alpha subunit activating protein gbas-1 {ECO:0000305};
GN Name=gbas-1 {ECO:0000312|WormBase:F59H5.1};
GN ORFNames=F59H5.1 {ECO:0000312|WormBase:F59H5.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000312|EMBL:AAO27841.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 517-758, AND INTERACTION WITH GOA-1.
RX PubMed=18629017; DOI=10.1002/cfg.318;
RA Cuppen E., van der Linden A.M., Jansen G., Plasterk R.H.;
RT "Proteins interacting with Caenorhabditis elegans Galpha subunits.";
RL Comp. Funct. Genomics 4:479-491(2003).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GOA-1, TISSUE SPECIFICITY, GBA MOTIF, AND
RP MUTAGENESIS OF 337-GLN--ARG-758; 575-LYS--ARG-758; VAL-657; PHE-660 AND
RP LEU-661.
RX PubMed=26659249; DOI=10.1093/molbev/msv336;
RA Coleman B.D., Marivin A., Parag-Sharma K., DiGiacomo V., Kim S.,
RA Pepper J.S., Casler J., Nguyen L.T., Koelle M.R., Garcia-Marcos M.;
RT "Evolutionary conservation of a GPCR-independent mechanism of trimeric G
RT protein activation.";
RL Mol. Biol. Evol. 33:820-837(2016).
CC -!- FUNCTION: Acts as a non-receptor guanine nucleotide exchange factor
CC which binds to and activates G-protein alpha subunit goa-1.
CC {ECO:0000269|PubMed:26659249}.
CC -!- SUBUNIT: Interacts (via GBA motif) with guanine nucleotide-binding
CC protein G(o) subunit alpha goa-1 (in GDP-bound form); the interaction
CC leads to activation of goa-1. {ECO:0000269|PubMed:18629017,
CC ECO:0000269|PubMed:26659249}.
CC -!- INTERACTION:
CC Q9TZI4; P51875: goa-1; NbExp=3; IntAct=EBI-6094450, EBI-316062;
CC -!- TISSUE SPECIFICITY: Expressed in some neurons including the head and
CC tail neurons, HSN and VC, in a subset of glial cells, in the distal
CC tips cells and in the intestine. {ECO:0000269|PubMed:26659249}.
CC -!- DOMAIN: The GBA (G-alpha binding and activating) motif mediates binding
CC to the alpha subunits of guanine nucleotide-binding proteins (G
CC proteins). {ECO:0000269|PubMed:26659249}.
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DR EMBL; BX284602; CCD70880.1; -; Genomic_DNA.
DR EMBL; AF408762; AAO27841.1; -; mRNA.
DR PIR; T33514; T33514.
DR RefSeq; NP_494285.2; NM_061884.5.
DR AlphaFoldDB; Q9TZI4; -.
DR IntAct; Q9TZI4; 1.
DR STRING; 6239.F59H5.1; -.
DR EPD; Q9TZI4; -.
DR PaxDb; Q9TZI4; -.
DR PeptideAtlas; Q9TZI4; -.
DR EnsemblMetazoa; F59H5.1.1; F59H5.1.1; WBGene00019130.
DR GeneID; 173603; -.
DR KEGG; cel:CELE_F59H5.1; -.
DR UCSC; F59H5.1; c. elegans.
DR CTD; 173603; -.
DR WormBase; F59H5.1; CE31963; WBGene00019130; gbas-1.
DR eggNOG; ENOG502T72K; Eukaryota.
DR GeneTree; ENSGT00970000196179; -.
DR HOGENOM; CLU_367708_0_0_1; -.
DR InParanoid; Q9TZI4; -.
DR OMA; DRRIAWI; -.
DR PhylomeDB; Q9TZI4; -.
DR PRO; PR:Q9TZI4; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00019130; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
DR InterPro; IPR006570; SPK_dom.
DR SMART; SM00583; SPK; 1.
PE 1: Evidence at protein level;
KW Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..758
FT /note="G-protein alpha subunit activating protein gbas-1"
FT /id="PRO_0000448585"
FT REGION 30..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 653..666
FT /note="GBA"
FT /evidence="ECO:0000269|PubMed:26659249"
FT COMPBIAS 30..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 337..758
FT /note="Missing: In gk136226; no major changes in egg-laying
FT behavior with mutants shutting off egg laying during
FT starvation and resuming egg laying when re-fed as in wild-
FT type animals. Mutants show a decrease in the number of laid
FT eggs under fed and re-fed conditions."
FT /evidence="ECO:0000269|PubMed:26659249"
FT MUTAGEN 575..758
FT /note="Missing: In gk578844; no major changes in egg-laying
FT behavior with mutants shutting off egg laying during
FT starvation and resuming egg laying when re-fed as in wild-
FT type animals. Mutants show a decrease in the number of laid
FT eggs under fed and re-fed conditions."
FT /evidence="ECO:0000269|PubMed:26659249"
FT MUTAGEN 657
FT /note="V->A: Impairs binding to goa-1."
FT /evidence="ECO:0000269|PubMed:26659249"
FT MUTAGEN 660
FT /note="F->A: Abolishes binding to goa-1 and ability of
FT gbas-1 to activate goa-1."
FT /evidence="ECO:0000269|PubMed:26659249"
FT MUTAGEN 661
FT /note="L->A: Abolishes binding to goa-1."
FT /evidence="ECO:0000269|PubMed:26659249"
SQ SEQUENCE 758 AA; 88387 MW; 7A09454A270DD59F CRC64;
MRSVRSSSRT PKPVKRFVFD EDEDLEEIDL DEVDNADFER EDDEEEVLSE PSESPYTSTP
KSSKRVNKTR GTKDFFKKDE SLQLFRFVLN ECRSQKPGRV GRVAKKRVGV NSMKYWERYK
REIQGYRLPK QYRYHYSFYS KCFYKVLGLT PEEKVDLYYA CEMPVVTDAE KQWLVEQFHV
EFDEFGVIIG SDVCTHWDEE HSDSEDDSGK KEEKAREVSR YTEYHDDMMW KFIVDKISEG
AQPIIDKHPI WDEFVKLNEE NDVISKKSGR NHYDRFRRIL VPNLHFMPYD DFTKAVLYER
LEYPIPEEYR KILFTTTGAD INESGFIEYL PPSTIHQISP IVPIPCHKSN PKFSQLKEPK
DLILWSERKK FTPREDSQIW EFVRRKCVDS AGIFVKNDVL RGRGTLFFKD FRNTERKYES
ITQRFVVLRK LIMDTDYSLK QKLEIYYAIS QPVDEDALDA FKSIACLVLN PDGTIRFAIS
KSFLIGRISD EPAKLEAENY SYVYDLFIFN ETFGTAENPE PLCSVSQNRA EKFMLVSQLV
FRFISRFEAL EDRRIAWITP NAQVAPKEPV PAPSKKKSAF EAYQSSPQTF DTIQRFSTKR
PFFCGDNFQI PPKKPFLAEE DVKLEPMEYE NSEQIVENAE IKLEPAEELL DAETVTVEEF
LMNSYSTAAP STSTAPAPPK APVTAPPAPQ KSAQLLGKID FAIGKMRENF DRFLQFAQQN
SADLTVVQRY RYDAQMQQMT EKFTKDVSKV LSGDSIKR
