EXOC7_RAT
ID EXOC7_RAT Reviewed; 653 AA.
AC O54922;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Exocyst complex component 7;
DE AltName: Full=Exocyst complex component Exo70;
DE Short=rExo70;
GN Name=Exoc7; Synonyms=Exo70;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9405631; DOI=10.1073/pnas.94.26.14438;
RA Kee Y., Yoo J.-S., Hazuka C.D., Peterson K.E., Hsu S.-C., Scheller R.H.;
RT "Subunit structure of the mammalian exocyst complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14438-14443(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). It is required for
CC neuron survival and plays an essential role in cortical development (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:E7FC72}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with ARHQ in a GTP-dependent
CC manner. Interacts with RAB11FIP3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O35250}. Cell membrane
CC {ECO:0000250|UniProtKB:O35250}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O35250}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q9UPT5}. Note=Translocates, as a preformed
CC complex with SEC6 and SEC8, to the plasma membrane in response to
CC insulin through the activation of ARHQ (By similarity). Colocalizes
CC with CNTRL/centriolin at the midbody ring (By similarity).
CC {ECO:0000250|UniProtKB:O35250, ECO:0000250|UniProtKB:Q9UPT5}.
CC -!- DOMAIN: The C-terminus is required for translocation to the plasma
CC membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
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DR EMBL; AF032667; AAC01579.1; -; mRNA.
DR RefSeq; NP_073182.1; NM_022691.1.
DR RefSeq; XP_008766651.1; XM_008768429.2.
DR AlphaFoldDB; O54922; -.
DR SMR; O54922; -.
DR BioGRID; 249170; 2.
DR CORUM; O54922; -.
DR IntAct; O54922; 1.
DR STRING; 10116.ENSRNOP00000013281; -.
DR iPTMnet; O54922; -.
DR PhosphoSitePlus; O54922; -.
DR jPOST; O54922; -.
DR PaxDb; O54922; -.
DR PRIDE; O54922; -.
DR GeneID; 64632; -.
DR KEGG; rno:64632; -.
DR CTD; 23265; -.
DR RGD; 620236; Exoc7.
DR VEuPathDB; HostDB:ENSRNOG00000070201; -.
DR eggNOG; KOG2344; Eukaryota.
DR HOGENOM; CLU_010236_4_0_1; -.
DR InParanoid; O54922; -.
DR OMA; GPIYGNT; -.
DR OrthoDB; 410847at2759; -.
DR PhylomeDB; O54922; -.
DR Reactome; R-RNO-264876; Insulin processing.
DR Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR PRO; PR:O54922; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000009617; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; O54922; RN.
DR GO; GO:0034451; C:centriolar satellite; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:RGD.
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 Cell membrane; Coiled coil; Cytoplasm; Exocytosis; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..653
FT /note="Exocyst complex component 7"
FT /id="PRO_0000118962"
FT REGION 1..384
FT /note="SEC8 and ARHQ binding"
FT /evidence="ECO:0000250"
FT REGION 238..272
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 COMPBIAS 257..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 653 AA; 75046 MW; DA206444F767E794 CRC64;
MIPPQEASAR RREIEDKLKQ EEETLSFIRD SLEKSDQLTK NMVSILSSFE SRLMKLENSI
IPVHKQTENL QRLQENVEKT LSCLDHVISY YHVASDTEKI IREGPTGRLE EYLGSMAKIQ
KAVEYFQDNS PDSPELNKVK LLFERGKESL ESEFRSLMTR HSKVISPVLV LDLISADDEL
EVQEDVVLEH LPESVLQDVI RISRWLVEYG RNQDFMNVYY QIRSSQLDRS IKGLKEHFRK
SSSSSGVPYS PAIPNKRKDT PTKKPIKRPG RDDMLDVETD AYIHCVSAFV RLAQSEYQLL
MGIIPEHHQK KTFDSLIQDA LDGLMLEGEN IVSAARKAII RHDFSTVLTV FPILRHLKQT
KPEFDQVLQG TAASTKNKLP GLITSMETIG AKALEDFADN IKNDPDKEYN MPKDGTVHEL
TSNAILFLQQ LLDFQETAGA MLASQETSSS ATSYNSEFSK RLLSTYICKV LGNLQLNLLS
KSKVYEDPAL SAIFLHNNYN YILKSLEKSE LIQLVAVTQK TAERSYREHI EQQIQTYQRS
WLKVTDYIAE KNLPVFQPGV KLRDKERQMI KERFKGFNDG LEELCKIQKA WAIPDTEQRD
KIRQAQKSIV KETYGAFLHR YSSVPFTKNP EKYIKYRVEQ VGDMIDRLFD TSA
