EXOC4_MOUSE
ID EXOC4_MOUSE Reviewed; 975 AA.
AC O35382;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Exocyst complex component 4;
DE AltName: Full=Exocyst complex component Sec8;
GN Name=Exoc4; Synonyms=Sec8, Sec8l1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RX PubMed=9441674; DOI=10.1006/dbio.1997.8727;
RA Friedrich G.A., Hildebrand J.D., Soriano P.;
RT "The secretory protein Sec8 is required for paraxial mesoderm formation in
RT the mouse.";
RL Dev. Biol. 192:364-374(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 TISSUE SPECIFICITY.
RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019;
RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R.,
RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T.,
RA Kinoshita M.;
RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required
RT for the suppression of alpha-synuclein neurotoxicity.";
RL Neuron 53:519-533(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC {ECO:0000250|UniProtKB:Q62824}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q62824,
CC ECO:0000250|UniProtKB:Q96A65, ECO:0000269|PubMed:17827149}.
CC -!- INTERACTION:
CC O35382; O35250: Exoc7; NbExp=2; IntAct=EBI-772648, EBI-775332;
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q96A65}. Cell projection
CC {ECO:0000250|UniProtKB:Q62824}. Note=Colocalizes with CNTRL/centriolin
CC at the midbody ring (By similarity). Localizes at the leading edge of
CC migrating cells (By similarity). {ECO:0000250|UniProtKB:Q62824,
CC ECO:0000250|UniProtKB:Q96A65}.
CC -!- TISSUE SPECIFICITY: Expressed in the striatum (at protein level).
CC {ECO:0000269|PubMed:17296554}.
CC -!- SIMILARITY: Belongs to the SEC8 family. {ECO:0000305}.
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DR EMBL; AF022962; AAB86537.1; -; mRNA.
DR EMBL; BC034644; AAH34644.1; -; mRNA.
DR CCDS; CCDS19987.1; -.
DR RefSeq; NP_033174.2; NM_009148.3.
DR AlphaFoldDB; O35382; -.
DR SMR; O35382; -.
DR BioGRID; 203152; 17.
DR ComplexPortal; CPX-4982; Exocyst, Exoc6 variant.
DR ComplexPortal; CPX-4983; Exocyst, Exoc6b variant.
DR DIP; DIP-32368N; -.
DR IntAct; O35382; 9.
DR MINT; O35382; -.
DR STRING; 10090.ENSMUSP00000051965; -.
DR iPTMnet; O35382; -.
DR PhosphoSitePlus; O35382; -.
DR EPD; O35382; -.
DR MaxQB; O35382; -.
DR PaxDb; O35382; -.
DR PeptideAtlas; O35382; -.
DR PRIDE; O35382; -.
DR ProteomicsDB; 267670; -.
DR Antibodypedia; 18039; 184 antibodies from 28 providers.
DR DNASU; 20336; -.
DR Ensembl; ENSMUST00000052266; ENSMUSP00000051965; ENSMUSG00000029763.
DR GeneID; 20336; -.
DR KEGG; mmu:20336; -.
DR UCSC; uc009bgs.1; mouse.
DR CTD; 60412; -.
DR MGI; MGI:1096376; Exoc4.
DR VEuPathDB; HostDB:ENSMUSG00000029763; -.
DR eggNOG; KOG3691; Eukaryota.
DR GeneTree; ENSGT00390000001439; -.
DR HOGENOM; CLU_012416_0_0_1; -.
DR InParanoid; O35382; -.
DR OMA; SLPNWTD; -.
DR OrthoDB; 96167at2759; -.
DR PhylomeDB; O35382; -.
DR TreeFam; TF313954; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 20336; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Exoc4; mouse.
DR PRO; PR:O35382; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O35382; protein.
DR Bgee; ENSMUSG00000029763; Expressed in rostral migratory stream and 259 other tissues.
DR ExpressionAtlas; O35382; baseline and differential.
DR Genevisible; O35382; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0032584; C:growth cone membrane; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IDA:BHF-UCL.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0044091; P:membrane biogenesis; ISO:MGI.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISO:MGI.
DR GO; GO:0048341; P:paraxial mesoderm formation; IMP:MGI.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; ISO:MGI.
DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
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_0000118935"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:Q96A65"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96A65"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96A65"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 692
FT /note="G -> A (in Ref. 1; AAB86537)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="S -> R (in Ref. 1; AAB86537)"
FT /evidence="ECO:0000305"
FT CONFLICT 832
FT /note="S -> T (in Ref. 1; AAB86537)"
FT /evidence="ECO:0000305"
FT CONFLICT 949..975
FT /note="RLQRLKEIICEQAAIKQATKDKKITTV -> SCRDSRRSSVSRLPSSKPPRT
FT RK (in Ref. 1; AAB86537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 975 AA; 110545 MW; 8DB5E154FA44E52A CRC64;
MAAEAAGGKY RSTVSKSKDP SGLLISVIRT LSTSDDVEDR ENEKGRLEEA YEKCDRDLDE
LIVQHYTELT TAIRTYQSIT ERITNSRNKI KQVKENLLSC KMLLHCKRDE LRKLWIEGIE
HKHVLNLLDE IENIKQVPQK LEQCMASKHY LSATDMLVSA VESLEGPLLQ VEGLSDLRLE
LHSKKMNLHL VLIEELHRHL YIKSTSRVVQ RNKEKGKMSS HGKDPSPGPL IDVSNIPTPR
KFLDASQYSA AGGSSVREMN LQDVKEDLEC DPEENSTLFM GILIQGLARL KKIPETVKAI
KERLEQELKQ IVKRSTTQVA DSAYQRGESL TVDNQPRLLL ELLELLFDKF NAVATAHSVV
LGYLQDSVGT QLTQQEEIKL YDMADVWVKI QDVLQMLLTE YLDMKNTRTA SEPSAQLSYA
STGREFAAFF AKKKPQRPKN SLFKFESSSH AISMSAYLRE QRRELYSRSG ELQGGPDDNL
IEGGGTKFVC KPGARNITVI FHPLLRFIQE IEHALGLGPA KQCPLREFLT VYIKSIFLNQ
VLAEINKEIE GVTKTSDPLK ILANADTMKV LGVQRPLLQS TIIVEKTVQD LMNLMHDLSA
YSDQFLNMVC VKLQEYKDTC STAYRGIVQS EEKLVISASW AKDDDISRLL KSLPNWTNMA
QPKQLRPKRE EEEDFIRAAF GKESEVLIGN LGDKLIPPQD ILRDVSDLKA LANMHESLEW
LAGRTKSAFS NLSTSQMLSP AQESHVNMDL PPVSEQIMQT LSELAKTFQD MADRCLLVLH
LEVRVHCFHY LIPLAKEGNY AIVANVESMD YDPLVVKLNK DISAMEEAMS ASLQQHKFQY
IFEGLGHLIS CILINGAQYF RRISESGIKK MCRNIFVLQQ NLTNITMSRE ADLDFARQYY
EMLYNTADEL LNLVVDQGVK YTELEYIHAL TLLHRSQTGV GDQTTQNTRL QRLKEIICEQ
AAIKQATKDK KITTV