EXOC4_RAT
ID EXOC4_RAT Reviewed; 975 AA.
AC Q62824;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Exocyst complex component 4;
DE AltName: Full=Exocyst complex component Sec8;
DE Short=rSec8;
GN Name=Exoc4; Synonyms=Sec8, Sec8l1;
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 [MRNA].
RX PubMed=7568183; DOI=10.1073/pnas.92.21.9613;
RA Ting A.E., Hazuka C.D., Hsu S.-C., Kirk M.D., Bean A.J., Scheller R.H.;
RT "rSec6 and rSec8, mammalian homologs of yeast proteins essential for
RT secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9613-9617(1995).
RN [2]
RP INTERACTION WITH SLC6A9.
RX PubMed=16181645; DOI=10.1016/j.neuropharm.2005.07.021;
RA Cubelos B., Gimenez C., Zafra F.;
RT "The glycine transporter GLYT1 interacts with Sec3, a component of the
RT exocyst complex.";
RL Neuropharmacology 49:935-944(2005).
RN [3]
RP INTERACTION WITH MYRIP.
RX PubMed=17827149; DOI=10.1074/jbc.m705167200;
RA Goehring A.S., Pedroja B.S., Hinke S.A., Langeberg L.K., Scott J.D.;
RT "MyRIP anchors protein kinase A to the exocyst complex.";
RL J. Biol. Chem. 282:33155-33167(2007).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=21658605; DOI=10.1016/j.molcel.2011.03.032;
RA Parrini M.C., Sadou-Dubourgnoux A., Aoki K., Kunida K., Biondini M.,
RA Hatzoglou A., Poullet P., Formstecher E., Yeaman C., Matsuda M., Rosse C.,
RA Camonis J.;
RT "SH3BP1, an exocyst-associated RhoGAP, inactivates Rac1 at the front to
RT drive cell motility.";
RL Mol. Cell 42:650-661(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26582389; DOI=10.1091/mbc.e15-02-0061;
RA Seixas C., Choi S.Y., Polgar N., Umberger N.L., East M.P., Zuo X.,
RA Moreiras H., Ghossoub R., Benmerah A., Kahn R.A., Fogelgren B., Caspary T.,
RA Lipschutz J.H., Barral D.C.;
RT "Arl13b and the exocyst interact synergistically in ciliogenesis.";
RL Mol. Biol. Cell 27:308-320(2016).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC {ECO:0000269|PubMed:26582389}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (PubMed:26582389). Interacts with
CC BIRC6/bruce (By similarity). Interacts with MYRIP. Interacts with
CC SH3BP1; required for the localization of both SH3BP1 and the exocyst to
CC the leading edge of migrating cells (By similarity). Interacts with
CC SLC6A9 (PubMed:16181645). {ECO:0000250|UniProtKB:O35382,
CC ECO:0000250|UniProtKB:Q96A65, ECO:0000269|PubMed:16181645,
CC ECO:0000269|PubMed:17827149, ECO:0000269|PubMed:26582389}.
CC -!- INTERACTION:
CC Q62824; F1M7Y5: Prkci; NbExp=2; IntAct=EBI-6959516, EBI-8795211;
CC Q62824; Q8IX03-1: WWC1; Xeno; NbExp=3; IntAct=EBI-6959516, EBI-15812469;
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q96A65}. Cell projection
CC {ECO:0000269|PubMed:21658605}. Note=Colocalizes with CNTRL/centriolin
CC at the midbody ring (By similarity). Localizes at the leading edge of
CC migrating cells (PubMed:21658605). {ECO:0000250|UniProtKB:Q96A65,
CC ECO:0000269|PubMed:21658605}.
CC -!- SIMILARITY: Belongs to the SEC8 family. {ECO:0000305}.
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DR EMBL; U32498; AAC52265.1; -; mRNA.
DR PIR; I59422; I59422.
DR RefSeq; NP_446327.1; NM_053875.1.
DR AlphaFoldDB; Q62824; -.
DR SMR; Q62824; -.
DR BioGRID; 250539; 3.
DR CORUM; Q62824; -.
DR DIP; DIP-40985N; -.
DR IntAct; Q62824; 7.
DR MINT; Q62824; -.
DR STRING; 10116.ENSRNOP00000064888; -.
DR iPTMnet; Q62824; -.
DR PhosphoSitePlus; Q62824; -.
DR jPOST; Q62824; -.
DR PRIDE; Q62824; -.
DR GeneID; 116654; -.
DR KEGG; rno:116654; -.
DR UCSC; RGD:621791; rat.
DR CTD; 60412; -.
DR RGD; 621791; Exoc4.
DR eggNOG; KOG3691; Eukaryota.
DR InParanoid; Q62824; -.
DR OrthoDB; 96167at2759; -.
DR PhylomeDB; Q62824; -.
DR Reactome; R-RNO-264876; Insulin processing.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:Q62824; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0032584; C:growth cone membrane; ISO:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR GO; GO:0035748; C:myelin sheath abaxonal region; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:RGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0055108; P:Golgi to transport vesicle transport; IDA:RGD.
DR GO; GO:0044091; P:membrane biogenesis; IMP:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:RGD.
DR GO; GO:0048341; P:paraxial mesoderm formation; ISO:RGD.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0051223; P:regulation of protein transport; IMP:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR GO; GO:0006903; P:vesicle targeting; TAS:UniProtKB.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IEA:InterPro.
DR InterPro; IPR039682; Sec8/EXOC4.
DR InterPro; IPR007191; Sec8_exocyst_N.
DR PANTHER; PTHR14146; PTHR14146; 1.
DR Pfam; PF04048; Sec8_exocyst; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Exocytosis; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96A65"
FT CHAIN 2..975
FT /note="Exocyst complex component 4"
FT /id="PRO_0000118936"
FT COILED 32..114
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96A65"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96A65"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96A65"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96A65"
SQ SEQUENCE 975 AA; 110553 MW; C52FD3553BE75858 CRC64;
MAAEAAGGKY RSTVSKSKDP SGLLISVIRT LSTSDDVEDR ENEKGRLEEA YEKCDRDLDE
LIVQHYTELT TAIRTYQSIT ERITNSRNKI KQVKENLLSC KMLLHCKRDE LRKLWIEGIE
HKHVLNLLDE IENIKQVPQK LEQCMASKHY LSATDMLVSA VESLEGPLLQ VEGLSDLRLE
LHSKKMNLHL VLIEELHRHL YIKSTSRVVQ RNKEKGKMSS HGKDASPGPL IDVSNISTPR
KFLDATQYSA AGSSSVREMN LQDIKEDLDC DPEENSTLFM GILIQGLARL KKIPETVKAI
KERLEQELKQ IVKRSTTQVA DSAYQRGESL TVDNQPRLLL ELLELLFDKF NAVASAHSIV
LGYLQDSVGT QPTQQEEIKL YDMADVWVKI QDVLQMLLTE YLDMKNTRTA SEPSAQLSYA
STGREFAAFF AKKKPQRPKN SLFKFESSSH AISMSAYLRE QRRELYSRSG ELQGGPDDNL
IEGGGTKFVC KPGARNITVI FHPLLRFIQE IEHALGLGPA KQCLLREFLT IYIKNIFLNQ
VLTEINKEIE GVTKTSDPLK ILANADTMKV LGVQRPLLQS TIIVEKTVQD LMNLMHDLSA
YSDQFLNMVC VKLQEYKDTC STAYRGIVQS EEKLVISASW AKDDDISRLL KSLPNWTNMA
QPKQLRPKRE EEEDFIRAAF GKESEVLIGN LGDKLIPPQD ILRDVSDLKA LANMHESLEW
LAGRTKSAFS SLSASQMLSP AQESHVNMDL PPVSEQIMQT LSELAKSFQD MADRCLLVLH
LEVRVHCFHY LIPLAKEGNY AIVANVESMD YDPLVVKLNK DISAMEEAMS ASLQQHKFQY
IFEGLGHLIS CILINGAQYF RRISESGIKK MCRNIFVLQQ NLTNITMSRE ADLDFARQYY
EMLYNTADEL LNLVVDQGVK YTELEYIHAL TLLHRSQTGV GDQTTQNTRL QRLKEIICEQ
AAIKQATKDK KITTV
