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   27-MAR-2024, entry version 167.
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,
RC   Pancreas, 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}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q96A65}.
CC       Note=Colocalizes with CNTRL/centriolin at the midbody ring (By
CC       similarity). Localizes at the leading edge of migrating cells (By
CC       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; 20.
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; 10090-ENSMUSP00000051965; -.
DR   PeptideAtlas; O35382; -.
DR   ProteomicsDB; 267670; -.
DR   Pumba; O35382; -.
DR   Antibodypedia; 18039; 216 antibodies from 28 providers.
DR   DNASU; 20336; -.
DR   Ensembl; ENSMUST00000052266.15; ENSMUSP00000051965.9; ENSMUSG00000029763.18.
DR   GeneID; 20336; -.
DR   KEGG; mmu:20336; -.
DR   UCSC; uc009bgs.1; mouse.
DR   AGR; MGI:1096376; -.
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; HMEVRCR; -.
DR   OrthoDB; 2898137at2759; -.
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; 16 hits in 79 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 262 other cell types or tissues.
DR   ExpressionAtlas; O35382; baseline and differential.
DR   GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043198; C:dendritic shaft; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0032584; C:growth cone membrane; IDA:MGI.
DR   GO; GO:0005902; C:microvillus; IDA: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:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex 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; NAS:ComplexPortal.
DR   GO; GO:0000281; P:mitotic cytokinesis; NAS: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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; NAS:ComplexPortal.
DR   GO; GO:0090522; P:vesicle tethering involved in exocytosis; NAS:ComplexPortal.
DR   InterPro; IPR039682; Sec8/EXOC4.
DR   InterPro; IPR007191; Sec8_exocyst_N.
DR   InterPro; IPR048630; Sec8_M.
DR   PANTHER; PTHR14146; EXOCYST COMPLEX COMPONENT 4; 1.
DR   PANTHER; PTHR14146:SF0; EXOCYST COMPLEX COMPONENT 4; 1.
DR   Pfam; PF20652; Sec8_C; 1.
DR   Pfam; PF04048; Sec8_N; 1.
DR   Genevisible; O35382; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Exocytosis; Phosphoprotein; Protein transport; Reference proteome;
KW   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
//