EXOC1_MOUSE
ID EXOC1_MOUSE Reviewed; 894 AA.
AC Q8R3S6; E9QQ24;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Exocyst complex component 1;
DE AltName: Full=Exocyst complex component Sec3;
GN Name=Exoc1; Synonyms=Sec3, Sec3l1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND SER-473, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with EEF1A1. Interacts with
CC SLC6A9; interaction increases the transporter capacity of SLC6A9
CC probably by promoting its insertion into the cell membrane.
CC {ECO:0000250|UniProtKB:Q9NV70}.
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q9NV70}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NV70}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9NV70}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9NV70}. Note=Colocalizes with CNTRL/centriolin
CC at the midbody ring. Localizes in cell membrane in the presence of
CC SLC6A9. {ECO:0000250|UniProtKB:Q9NV70}.
CC -!- SIMILARITY: Belongs to the SEC3 family. {ECO:0000305}.
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DR EMBL; AC127332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024678; AAH24678.1; -; mRNA.
DR CCDS; CCDS71607.1; -.
DR RefSeq; NP_001276699.1; NM_001289770.1.
DR AlphaFoldDB; Q8R3S6; -.
DR SMR; Q8R3S6; -.
DR BioGRID; 213768; 6.
DR ComplexPortal; CPX-4982; Exocyst, Exoc6 variant.
DR ComplexPortal; CPX-4983; Exocyst, Exoc6b variant.
DR CORUM; Q8R3S6; -.
DR STRING; 10090.ENSMUSP00000109121; -.
DR iPTMnet; Q8R3S6; -.
DR PhosphoSitePlus; Q8R3S6; -.
DR EPD; Q8R3S6; -.
DR jPOST; Q8R3S6; -.
DR MaxQB; Q8R3S6; -.
DR PaxDb; Q8R3S6; -.
DR PeptideAtlas; Q8R3S6; -.
DR PRIDE; Q8R3S6; -.
DR ProteomicsDB; 275556; -.
DR Antibodypedia; 23967; 102 antibodies from 23 providers.
DR Ensembl; ENSMUST00000087133; ENSMUSP00000084373; ENSMUSG00000036435.
DR GeneID; 69940; -.
DR KEGG; mmu:69940; -.
DR UCSC; uc008xva.2; mouse.
DR CTD; 55763; -.
DR MGI; MGI:2445020; Exoc1.
DR VEuPathDB; HostDB:ENSMUSG00000036435; -.
DR eggNOG; KOG2148; Eukaryota.
DR GeneTree; ENSGT00940000158640; -.
DR HOGENOM; CLU_015381_1_0_1; -.
DR InParanoid; Q8R3S6; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 69940; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Exoc1; mouse.
DR PRO; PR:Q8R3S6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R3S6; protein.
DR Bgee; ENSMUSG00000036435; Expressed in retinal neural layer and 250 other tissues.
DR ExpressionAtlas; Q8R3S6; baseline and differential.
DR Genevisible; Q8R3S6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; ISO:MGI.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0007566; P:embryo implantation; IMP: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:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR028258; Sec3-PIP2_bind.
DR InterPro; IPR019160; Sec3_C.
DR Pfam; PF15277; Sec3-PIP2_bind; 1.
DR Pfam; PF09763; Sec3_C; 1.
DR SMART; SM01313; Sec3-PIP2_bind; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Exocytosis; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..894
FT /note="Exocyst complex component 1"
FT /id="PRO_0000118914"
FT REGION 437..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..199
FT /evidence="ECO:0000255"
FT COILED 205..259
FT /evidence="ECO:0000255"
FT COMPBIAS 437..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NV70"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NV70"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 329
FT /note="V -> I (in Ref. 2; AAH24678)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="L -> S (in Ref. 2; AAH24678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 101889 MW; 50CA79A8F56091E7 CRC64;
MTAIKHALQR DIFTPNDERL LSIVNVCKAG KKKKNCFLCA TVTTERPVQV KVVKVKKSDK
GDFYKRQIAW ALRDLAVVDA KDAIKENPEF DLHFEKVYKW VASSTAEKNA FISCIWKLNQ
RYLRKKIDFV NVSSQLLEES VPSGENQSVA GGDEEAVDEY QELNAREEQD IEIMMEGCEC
AISNAEAFAE KLSRELQVLD GANIQSIMAS EKQVNTLMQL LDEALTEVDQ IELKLSSYEE
MLQSVKEQMD QISESNHLIH LSNTNNVKLL SEIEFLVNHM DLAKGHIKAL QEGDLVSSRG
IEACTNAADA LLQCMNVALR PGHDMLLAVK QQQQRFSDLR EHFARRLASH LNNVFVQQGH
DQSSTLAQHS VELTLPNHHP FHRDLLRYAK LMEWLKSTDY GKYEGLTKNY MDYLSRLYER
EIKDFFEVAK MKMTGTSKES KKFATLPRKE SAVKQETESL HGSSGKLTGS TSSLNKLSVQ
SSGSRRSQSS SLLDMGNMSA SDLDVADRTK FDKIFEQVLS ELEPLCLAEQ DFISKFFKLQ
QHQNMSASMT EAEDLDGGSL LRQHSSGTLL PVSSEKDMIR QMMIKIFRCI EPELNNLIAL
GDKVDSFNSL YMLVKMSHHV WTAQNVDPAS FLSTTLGNVL VTVKRNFDKC ISNQIRQMEE
VKISKKSKVG ILPFVAEFEE FAGLAESIFK NAERRGDLDK AYTKLIRGVF INVEKVANES
QKTPRDVVMM ENFHHIFATL SRLKISCLEA EKKEAKQKYT DHLQSYVIYS LGQPLEKLNH
FFEGVEARVA QGIREEEVSY QLAFNKQELR KVIKEYPGKE VKKGLDNLYK KVDKHLCEEE
NLLQVVWHSM QDEFIRQYKH FEGLIARCYP GSGVTMEFTI QDILDYCSSI AQSH
