EXOC7_MOUSE
ID EXOC7_MOUSE Reviewed; 697 AA.
AC O35250; Q8K121;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Exocyst complex component 7;
DE AltName: Full=Exocyst complex component Exo70;
GN Name=Exoc7; Synonyms=Exo70;
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] (ISOFORM 1).
RC TISSUE=Brain;
RA Guo W., Roth D., De Camilli P., Novick P.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Colon;
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 FUNCTION, INTERACTION WITH ARHQ, AND SUBCELLULAR LOCATION.
RX PubMed=12687004; DOI=10.1038/nature01533;
RA Inoue M., Chang L., Hwang J., Chiang S.-H., Saltiel A.R.;
RT "The exocyst complex is required for targeting of Glut4 to the plasma
RT membrane by insulin.";
RL Nature 422:629-633(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, 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. In
CC adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the
CC plasma membrane in response to insulin, perhaps directing the vesicle
CC to the precise site of fusion. It is required for neuron survival and
CC plays an essential role in cortical development (By similarity).
CC {ECO:0000250|UniProtKB:E7FC72, ECO:0000269|PubMed:12687004}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with RAB11FIP3 (By
CC similarity). Interacts with ARHQ in a GTP-dependent manner.
CC {ECO:0000250, ECO:0000269|PubMed:12687004}.
CC -!- INTERACTION:
CC O35250; O35382: Exoc4; NbExp=2; IntAct=EBI-775332, EBI-772648;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12687004}.
CC Cell membrane {ECO:0000269|PubMed:12687004}; Peripheral membrane
CC protein. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9UPT5}.
CC Note=Translocates, as a preformed complex with SEC6 and SEC8, to the
CC plasma membrane in response to insulin through the activation of ARHQ
CC (PubMed:12687004). Colocalizes with CNTRL/centriolin at the midbody
CC ring (By similarity). {ECO:0000250|UniProtKB:Q9UPT5,
CC ECO:0000269|PubMed:12687004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35250-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35250-2; Sequence=VSP_001484, VSP_001485;
CC -!- DOMAIN: The C-terminus is required for translocation to the plasma
CC membrane.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
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DR EMBL; AF014461; AAB69345.1; -; mRNA.
DR EMBL; BC028927; AAH28927.1; -; mRNA.
DR CCDS; CCDS25664.1; -. [O35250-1]
DR CCDS; CCDS48983.1; -. [O35250-2]
DR PIR; T03722; T03722.
DR RefSeq; NP_001156344.1; NM_001162872.1. [O35250-2]
DR RefSeq; NP_058553.2; NM_016857.2. [O35250-1]
DR PDB; 2PFT; X-ray; 2.25 A; A=85-697.
DR PDBsum; 2PFT; -.
DR AlphaFoldDB; O35250; -.
DR SMR; O35250; -.
DR BioGRID; 207307; 3.
DR ComplexPortal; CPX-4982; Exocyst, Exoc6 variant.
DR ComplexPortal; CPX-4983; Exocyst, Exoc6b variant.
DR IntAct; O35250; 8.
DR MINT; O35250; -.
DR STRING; 10090.ENSMUSP00000021147; -.
DR iPTMnet; O35250; -.
DR PhosphoSitePlus; O35250; -.
DR EPD; O35250; -.
DR jPOST; O35250; -.
DR PaxDb; O35250; -.
DR PeptideAtlas; O35250; -.
DR PRIDE; O35250; -.
DR ProteomicsDB; 275703; -. [O35250-1]
DR ProteomicsDB; 275704; -. [O35250-2]
DR Antibodypedia; 19667; 198 antibodies from 33 providers.
DR DNASU; 53413; -.
DR Ensembl; ENSMUST00000021147; ENSMUSP00000021147; ENSMUSG00000020792. [O35250-1]
DR Ensembl; ENSMUST00000106411; ENSMUSP00000102019; ENSMUSG00000020792. [O35250-2]
DR GeneID; 53413; -.
DR KEGG; mmu:53413; -.
DR UCSC; uc007mks.2; mouse. [O35250-1]
DR CTD; 23265; -.
DR MGI; MGI:1859270; Exoc7.
DR VEuPathDB; HostDB:ENSMUSG00000020792; -.
DR eggNOG; KOG2344; Eukaryota.
DR GeneTree; ENSGT00390000003595; -.
DR HOGENOM; CLU_010236_4_0_1; -.
DR InParanoid; O35250; -.
DR OMA; GPIYGNT; -.
DR OrthoDB; 410847at2759; -.
DR PhylomeDB; O35250; -.
DR TreeFam; TF324243; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 53413; 14 hits in 76 CRISPR screens.
DR ChiTaRS; Exoc7; mouse.
DR EvolutionaryTrace; O35250; -.
DR PRO; PR:O35250; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35250; protein.
DR Bgee; ENSMUSG00000020792; Expressed in embryonic brain and 269 other tissues.
DR ExpressionAtlas; O35250; baseline and differential.
DR Genevisible; O35250; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0032584; C:growth cone membrane; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; 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; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR004140; Exo70.
DR InterPro; IPR046364; Exo70_C.
DR PANTHER; PTHR12542; PTHR12542; 1.
DR Pfam; PF03081; Exo70; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Exocytosis; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..697
FT /note="Exocyst complex component 7"
FT /id="PRO_0000118961"
FT REGION 1..384
FT /note="SEC8 and ARHQ binding"
FT REGION 238..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..42
FT /evidence="ECO:0000255"
FT COILED 63..85
FT /evidence="ECO:0000255"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54922"
FT VAR_SEQ 270..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001484"
FT VAR_SEQ 477..489
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001485"
FT CONFLICT 40
FT /note="R -> K (in Ref. 1; AAB69345)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="V -> I (in Ref. 1; AAB69345)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="K -> E (in Ref. 1; AAB69345)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="Y -> F (in Ref. 1; AAB69345)"
FT /evidence="ECO:0000305"
FT CONFLICT 610..611
FT /note="ER -> DP (in Ref. 1; AAB69345)"
FT /evidence="ECO:0000305"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 109..129
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 134..161
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 193..209
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 214..240
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 307..334
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 340..371
FT /evidence="ECO:0007829|PDB:2PFT"
FT TURN 377..380
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 381..398
FT /evidence="ECO:0007829|PDB:2PFT"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 409..434
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 450..464
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 466..474
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 500..526
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 532..547
FT /evidence="ECO:0007829|PDB:2PFT"
FT TURN 548..552
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 555..560
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 566..582
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:2PFT"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 608..632
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 640..666
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 674..677
FT /evidence="ECO:0007829|PDB:2PFT"
FT HELIX 682..690
FT /evidence="ECO:0007829|PDB:2PFT"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:2PFT"
SQ SEQUENCE 697 AA; 79960 MW; 0A78F00E1D5D575A CRC64;
MIPPQEASAR RREIEDKLKQ EEETLSFIRD SLEKSDQLTR NMVSILSSFE SRLMKLENSI
IPVHKQTENL QRLQENVEKT LSCLDHVISY YHVASDTEKI IREGPTGRLE EYLGSMAKIQ
KAVEYFQDNS PDSPELNKVK LLFERGKESL ESEFRSLMTR HSKVVSPVLL LDLISADDEL
EVQEDVVLEH LPESVLRDVV RISRWLVEYG RNQDFMNVYY QIRSSQLDRS IKGLKEHFRK
SSSSSGVPYS PAIPNKRKDT PTKKPIKRPG TIRKAQNLLK QYSQHGLDGK KGGSNLIPLE
GRDDMLDVET DAYIHCVSAF VKLAQSEYRL LMEIIPEHHQ KKTFDSLIQD ALDGLMLEGE
NIVSAARKAI IRHDFSTVLT VFPILRHLKQ TKPEFDQVLQ GTAASTKNKL PGLITSMETI
GAKALEDFAD NIKNDPDKEY NMPKDGTVHE LTSNAILFLQ QLLDFQETAG AMLASQVLGD
TYNIPLDPRE TSSSATSYSS EFSKRLLSTY ICKVLGNLQL NLLSKSKVYE DPALSAIFLH
NNYNYILKSL EKSELIQLVA VTQKTAERSY REHIEQQIQT YQRSWLKVTD YIAEKNLPVF
QPGVKLRDKE RQMIKERFKG FNDGLEELCK IQKVWAIPDT EQRDKIRQAQ KDIVKETYGA
FLHRYGSVPF TKNPEKYIKY RVEQVGDMID RLFDTSA
