ID   RIC8A_PONAB             Reviewed;         530 AA.
AC   Q5R8F5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Synembryn-A;
DE   AltName: Full=Protein Ric-8A;
GN   Name=RIC8A;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate
CC       some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and
CC       GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in
CC       regulation of microtubule pulling forces during mitotic movement of
CC       chromosomes by stimulating G(i)-alpha protein, possibly leading to
CC       release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-
CC       alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ)
CC       protein by enhancing the G(q)-coupled receptor-mediated ERK activation
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAO1 and
CC       GNAQ, and with GNA13 with lower affinity. Does not interact with G-
CC       alpha proteins when they are in complex with subunits beta and gamma.
CC       Interacts (via C-terminus) with RGS14; the interaction stimulates the
CC       dissociation of the complex between RGS14 and the active GTP-bound form
CC       of GNAI1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}. Note=Colocalizes with RIC8A in CA2 hippocampal neurons.
CC       Colocalizes with GNAI1 and RGS14 at the plasma membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synembryn family. {ECO:0000305}.
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DR   EMBL; CR859797; CAH91955.1; -; mRNA.
DR   RefSeq; NP_001126134.1; NM_001132662.1.
DR   AlphaFoldDB; Q5R8F5; -.
DR   SMR; Q5R8F5; -.
DR   STRING; 9601.ENSPPYP00000022354; -.
DR   GeneID; 100173091; -.
DR   KEGG; pon:100173091; -.
DR   CTD; 60626; -.
DR   eggNOG; KOG4464; Eukaryota.
DR   HOGENOM; CLU_018602_1_0_1; -.
DR   InParanoid; Q5R8F5; -.
DR   OMA; NADPIFT; -.
DR   OrthoDB; 1110075at2759; -.
DR   TreeFam; TF314907; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IEA:Ensembl.
DR   GO; GO:0070586; P:cell-cell adhesion involved in gastrulation; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0001944; P:vasculature development; IEA:Ensembl.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR019318; Gua_nucleotide_exch_fac_Ric8.
DR   InterPro; IPR008376; Synembryn.
DR   PANTHER; PTHR12425; PTHR12425; 1.
DR   Pfam; PF10165; Ric8; 1.
DR   PRINTS; PR01802; SYNEMBRYN.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..530
FT                   /note="Synembryn-A"
FT                   /id="PRO_0000235893"
FT   MOD_RES         435
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT   MOD_RES         440
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT   MOD_RES         442
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TIR3"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT   MOD_RES         523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
SQ   SEQUENCE   530 AA;  59695 MW;  A0E099956BF0B76B CRC64;
     MEPRTVAEAV ETGKEDVIME ALRSYNQEHS QSFTFDDAQQ EDRKRLAELL VSVLEQGLPP
     SHRVTWLQSV RILSRDHNCL DPFTSRQSLQ ALACYADISV SEGSVPESPD MDVVLESLKC
     LCNLVLSSPV AQMLAAEARL VVKLTERVGL YRERSFPHDV QFFDLRLLFL LTALRTDVRQ
     QLFQELKGVR LLTDTLELTL GVTPEGNPPK LLPSQETERA MEILKVLFNI TLDSIKGEVD
     EEDAALYRHL GTLLRHCVMI ATAGDRTEEF HGHAVNLLGN LPLKCLDVLF TLEPHGDSVE
     FMGVNMDVIR ALLIFLEKRL HQTHRLKESV APVLSVLTEC ARMHRPARKF LKAQVLPPLR
     DVRTRPEVGE MLRNKLVRLM THLDTDVKRV AAEFLFVLCS ESVPRFIKYT GYGNAAGLLA
     ARGLMAGGRP EGQYSEDEDT DTDEYKEAKA SINPVTGRVE EKPPNPMEGM TEEQKEHEAM
     KLVTMFDKLS RNRVIQPMGM SPRGHLTSLQ DAMCETMEQQ LSSDPDSDPD