RIC8A_RAT
ID RIC8A_RAT Reviewed; 529 AA.
AC Q80ZG1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Synembryn-A;
DE AltName: Full=Protein Ric-8A;
GN Name=Ric8a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-529, FUNCTION, AND INTERACTION WITH GNAI1;
RP GNAO1; GNAQ AND GNA13.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12509430; DOI=10.1074/jbc.m211862200;
RA Tall G.G., Krumins A.M., Gilman A.G.;
RT "Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine
RT nucleotide exchange factor.";
RL J. Biol. Chem. 278:8356-8362(2003).
RN [3]
RP FUNCTION.
RX PubMed=16275912; DOI=10.1073/pnas.0508306102;
RA Tall G.G., Gilman A.G.;
RT "Resistance to inhibitors of cholinesterase 8A catalyzes release of
RT Galphai-GTP and nuclear mitotic apparatus protein (NuMA) from
RT NuMA/LGN/Galphai-GDP complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16584-16589(2005).
RN [4]
RP INTERACTION WITH GNAI1 AND RGS14, AND SUBCELLULAR LOCATION.
RX PubMed=21158412; DOI=10.1021/bi101910n;
RA Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.;
RT "Activation of the regulator of G protein signaling 14-Galphai1-GDP
RT signaling complex is regulated by resistance to inhibitors of
RT cholinesterase-8A.";
RL Biochemistry 50:752-762(2011).
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 {ECO:0000269|PubMed:12509430, ECO:0000269|PubMed:16275912}.
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. {ECO:0000269|PubMed:12509430, ECO:0000269|PubMed:21158412}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21158412}. Cell
CC membrane {ECO:0000269|PubMed:21158412}. Note=Colocalizes with RIC8A in
CC CA2 hippocampal neurons (By similarity). Colocalizes with GNAI1 and
CC RGS14 at the plasma membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synembryn family. {ECO:0000305}.
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DR EMBL; AABR03000472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY177754; AAO23336.1; -; mRNA.
DR PDB; 6VU5; EM; 3.50 A; A=1-450.
DR PDBsum; 6VU5; -.
DR AlphaFoldDB; Q80ZG1; -.
DR SMR; Q80ZG1; -.
DR CORUM; Q80ZG1; -.
DR STRING; 10116.ENSRNOP00000018470; -.
DR jPOST; Q80ZG1; -.
DR PaxDb; Q80ZG1; -.
DR PeptideAtlas; Q80ZG1; -.
DR UCSC; RGD:727957; rat.
DR RGD; 727957; Ric8a.
DR eggNOG; KOG4464; Eukaryota.
DR InParanoid; Q80ZG1; -.
DR PRO; PR:Q80ZG1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0071711; P:basement membrane organization; ISO:RGD.
DR GO; GO:0042074; P:cell migration involved in gastrulation; ISO:RGD.
DR GO; GO:0070586; P:cell-cell adhesion involved in gastrulation; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0009416; P:response to light stimulus; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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..529
FT /note="Synembryn-A"
FT /id="PRO_0000235894"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3TIR3"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT MOD_RES 521
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 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPQ8"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 40..56
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 158..173
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 176..186
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 188..199
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:6VU5"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 243..259
FT /evidence="ECO:0007829|PDB:6VU5"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:6VU5"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 307..313
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:6VU5"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 346..350
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:6VU5"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 390..397
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:6VU5"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:6VU5"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:6VU5"
SQ SEQUENCE 529 AA; 59833 MW; 883970DEC25BE7E4 CRC64;
MEPRAVADAL ETGEEDAVTE ALRSFNREHS QSFTFDDAQQ EDRKRLAKLL VSVLEQGLSP
KHRVTWLQTI RILSRDRSCL DSFASRQSLH ALACYADIAI SEEPIPQPPD MDVLLESLKC
LCNLVLSSPT AQMLAAEARL VVRLAERVGL YRKRSYPHEV QFFDLRLLFL LTALRTDVRQ
QLFQELHGVR LLTDALELTL GVAPKENPLV ILPAQETERA MEILKVLFNI TFDSVKREVD
EEDAALYRYL GTLLRHCVMA DRAGDRTEEF HGHTVNLLGN LPLKCLDVLL ALELHEGSLE
FMGVNMDVIN ALLAFLEKRL HQTHRLKECV APVLSVLTEC ARMHRPARKF LKAQVLPPLR
DVRTRPEVGD LLRNKLVRLM THLDTDVKRV AAEFLFVLCS ESVPRFIKYT GYGNAAGLLA
ARGLMAGGRP EGQYSRMRTP TEEYREAKAS INPVTGRVEE KPPNPMEGMT EEQKEHEAMK
LVNMFDKLSR HRLIQPMGMS PRGHLTSLQD AMCETMEGQL SSDPDSDPD
