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 24-JAN-2024, entry version 168. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SwissPalm; O35250; -. DR EPD; O35250; -. DR jPOST; O35250; -. DR PaxDb; 10090-ENSMUSP00000021147; -. DR PeptideAtlas; O35250; -. DR ProteomicsDB; 275703; -. [O35250-1] DR ProteomicsDB; 275704; -. [O35250-2] DR Pumba; O35250; -. DR Antibodypedia; 19667; 220 antibodies from 33 providers. DR DNASU; 53413; -. DR Ensembl; ENSMUST00000021147.14; ENSMUSP00000021147.8; ENSMUSG00000020792.16. [O35250-1] DR Ensembl; ENSMUST00000106411.10; ENSMUSP00000102019.4; ENSMUSG00000020792.16. [O35250-2] DR GeneID; 53413; -. DR KEGG; mmu:53413; -. DR UCSC; uc007mks.2; mouse. [O35250-1] DR AGR; MGI:1859270; -. 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; GIIRAGP; -. DR OrthoDB; 903986at2759; -. 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 81 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 273 other cell types or tissues. DR ExpressionAtlas; O35250; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0000281; P:mitotic cytokinesis; NAS: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; NAS:ComplexPortal. DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; NAS:ComplexPortal. DR Gene3D; 1.20.1280.170; Exocyst complex component Exo70; 2. DR InterPro; IPR016159; Cullin_repeat-like_dom_sf. DR InterPro; IPR004140; Exo70. DR InterPro; IPR046364; Exo70_C. DR PANTHER; PTHR12542:SF41; EXOCYST COMPLEX COMPONENT 7; 1. DR PANTHER; PTHR12542; EXOCYST COMPLEX PROTEIN EXO70; 1. DR Pfam; PF03081; Exo70_C; 1. DR Pfam; PF20669; Exo70_N; 1. DR SUPFAM; SSF74788; Cullin repeat-like; 1. DR Genevisible; O35250; MM. 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 //