RIC8A_BOVIN
ID RIC8A_BOVIN Reviewed; 530 AA.
AC Q5E9J8; Q17QK2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Synembryn-A;
DE AltName: Full=Protein Ric-8A;
GN Name=RIC8A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BT020922; AAX08939.1; -; mRNA.
DR EMBL; BC118313; AAI18314.1; -; mRNA.
DR RefSeq; NP_001015627.1; NM_001015627.2.
DR PDB; 6N85; X-ray; 2.50 A; B=1-492.
DR PDB; 6N86; X-ray; 3.90 A; B=1-492.
DR PDBsum; 6N85; -.
DR PDBsum; 6N86; -.
DR AlphaFoldDB; Q5E9J8; -.
DR SASBDB; Q5E9J8; -.
DR SMR; Q5E9J8; -.
DR STRING; 9913.ENSBTAP00000002646; -.
DR PaxDb; Q5E9J8; -.
DR PRIDE; Q5E9J8; -.
DR Ensembl; ENSBTAT00000002646; ENSBTAP00000002646; ENSBTAG00000002042.
DR GeneID; 521037; -.
DR KEGG; bta:521037; -.
DR CTD; 60626; -.
DR VEuPathDB; HostDB:ENSBTAG00000002042; -.
DR VGNC; VGNC:33961; RIC8A.
DR eggNOG; KOG4464; Eukaryota.
DR GeneTree; ENSGT00390000014700; -.
DR HOGENOM; CLU_018602_1_0_1; -.
DR InParanoid; Q5E9J8; -.
DR OMA; NADPIFT; -.
DR OrthoDB; 1110075at2759; -.
DR TreeFam; TF314907; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000002042; Expressed in myometrium and 107 other tissues.
DR ExpressionAtlas; Q5E9J8; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
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:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..530
FT /note="Synembryn-A"
FT /id="PRO_0000235889"
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"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:6N85"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 40..56
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 158..174
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:6N85"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:6N85"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:6N85"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 241..259
FT /evidence="ECO:0007829|PDB:6N85"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 326..343
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:6N85"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:6N85"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:6N85"
FT HELIX 412..421
FT /evidence="ECO:0007829|PDB:6N85"
SQ SEQUENCE 530 AA; 59499 MW; F663746DB9F588EB CRC64;
MEPRAVADAL ETGEEDVVME ALRAYNRENS QSFTFDDAQQ EDRKRLAKLL VSVLEQGLPP
SRRVIWLQSI RILSRDRSCL DSFTSRRSLQ ALACYAGISA SQGSVPEPLN MDVVLESLKC
LCNLVLSSPV AQALAAEAGL VVRLAERVGL CRQSSFPHDV QFFDLRLLFL LTALRTDVRQ
QLFQELQGVR LLTRALELTL GMTEGERHPE LLPPQETERA MEILKVLFNI TFDSIKREVD
EEDAALYRHL GTLLRHCVML AAAGDRTEEL HGHAVNLLGN LPVKCLDVLL TLEPHEGSLE
FLGVNMDVIR VLLSFMEKRL HQTHRLKESV APVLSVLTEC ARMHRPARKF LKAQVLPPLR
DVRTRPEVGE LLRNKLVRLM THLDTDVKRV AAEFLFVLCS ESVPRFIKYT GYGNAAGLLA
ARGLMAGGRP EGQYSEDEDT DTDEYKEAKA SINPVTGRVE EKPPNPMEGM TEEQKEHEAM
KLVNMFDKLS RHRVIQPMGM SPRGQLTSLQ DAMCETMEGQ LSSDPDSDPD
