EXOC6_MOUSE
ID EXOC6_MOUSE Reviewed; 802 AA.
AC Q8R313;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Exocyst complex component 6;
DE AltName: Full=Exocyst complex component Sec15A;
DE AltName: Full=SEC15-like protein 1;
GN Name=Exoc6; Synonyms=Sec15a, Sec15l1;
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 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 [2]
RP INTERACTION WITH RAB11A.
RX PubMed=15292201; DOI=10.1074/jbc.m402264200;
RA Zhang X.-M., Ellis S., Sriratana A., Mitchell C.A., Rowe T.;
RT "Sec15 is an effector for the Rab11 GTPase in mammalian cells.";
RL J. Biol. Chem. 279:43027-43034(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, 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. Together
CC with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP
CC promotes transcytosis of PODXL to the apical membrane initiation sites
CC (AMIS), apical surface formation and lumenogenesis. {ECO:0000250}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with CNTRL (By
CC similarity). Interacts with RAB11A in a GTP-dependent manner.
CC {ECO:0000250, ECO:0000250|UniProtKB:O54923,
CC ECO:0000269|PubMed:15292201}.
CC -!- INTERACTION:
CC Q8R313; Q62739: Rab3ip; Xeno; NbExp=2; IntAct=EBI-9202179, EBI-2028671;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54923}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Cell
CC projection, growth cone {ECO:0000250|UniProtKB:O54923}. Midbody,
CC Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. Note=Perinuclear in
CC undifferentiated cells. Redistributes to growing neurites and growth
CC cones during neuronal differentiation (By similarity). Colocalizes with
CC CNTRL/centriolin at the midbody ring (By similarity).
CC {ECO:0000250|UniProtKB:O54923, ECO:0000250|UniProtKB:Q8TAG9}.
CC -!- SIMILARITY: Belongs to the SEC15 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC026859; AAH26859.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8R313; -.
DR SMR; Q8R313; -.
DR ComplexPortal; CPX-4982; Exocyst, Exoc6 variant.
DR IntAct; Q8R313; 1.
DR MINT; Q8R313; -.
DR STRING; 10090.ENSMUSP00000064332; -.
DR iPTMnet; Q8R313; -.
DR PhosphoSitePlus; Q8R313; -.
DR EPD; Q8R313; -.
DR jPOST; Q8R313; -.
DR MaxQB; Q8R313; -.
DR PaxDb; Q8R313; -.
DR PeptideAtlas; Q8R313; -.
DR PRIDE; Q8R313; -.
DR ProteomicsDB; 275488; -.
DR MGI; MGI:1351611; Exoc6.
DR eggNOG; KOG2176; Eukaryota.
DR InParanoid; Q8R313; -.
DR Reactome; R-MMU-264876; Insulin processing.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR ChiTaRS; Exoc6; mouse.
DR PRO; PR:Q8R313; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R313; protein.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030218; P:erythrocyte differentiation; 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:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
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 Gene3D; 1.10.357.30; -; 1.
DR Gene3D; 1.20.58.670; -; 1.
DR InterPro; IPR007225; EXOC6/Sec15.
DR InterPro; IPR042045; EXOC6/Sec15_C_dom1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR046361; Sec15_C.
DR PANTHER; PTHR12702; PTHR12702; 1.
DR Pfam; PF04091; Sec15; 1.
DR PIRSF; PIRSF025007; Sec15; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Exocytosis; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..802
FT /note="Exocyst complex component 6"
FT /id="PRO_0000118952"
SQ SEQUENCE 802 AA; 93077 MW; 7AA82DCADBCD8E8B CRC64;
MAESCEALGT VPEHERILQE IESTDTACVG PTLRSVYDDQ PNAHKKFMEK LDACIRNHDK
EIEKMCNFHH QGFVDAITEL LKVRADAEKL KVTDTNRRFQ DAGKEVIIQT EDIIRCRIQQ
RNITTVVEKL QLCLPVLEMY SKLKEQMSMK RYYSALKTME QLENVYFPRV SQYRFCQLMM
ETLPKLREDM MNYCMSDLTY GLESIRKHSD KIGEAAMKQA QQQKSFSVAL QKQNNMRFGK
NMHVNNDRIL EEKSDVIPKH ALEEEAENDE EVLTVQDLVD FSPVYRCLHI YSALGDEETF
ENYYRKQRKK QARLVLQPQS SVHETVDGYR RYFTQIVGFF VVEDHILHVT QGLVTRVYTE
ELWNMALSKI IAVLRAHSSY CTDPDLVLEL KNLIVIFADT LQGYGFPVNR LFDLLFEIRD
QYNETLLKKW AGIFRDIFEE DNYSPIPIGS EEEYKVVISR FPFQDPDLEK QSFPKKFPMS
QSVPLIYIQV KEFIYASLKF SESLHRSSTE IDDMLRKSTN LLLTRILSSC LLNLIRKPHI
GLTELVQIII NTTHLEQACK YLEDFITNIT NISQETVHTT RLYGLSTFKD ARHAAEGEIY
TKLNQKIDEF VQLADYDWTM AESDGRASGY LMDLINFLRS IFQVFTHLPG KVAQTACMSA
CQHLSTSLMQ MLLDSELKQI SMGAVQQFNL DVIQCELFAS SEPVPGFQGD TLQLAFIDLR
QLLDLFMVWD WSTYLADYGQ PASKYLRVNP HAALTLLEKM KDTSKKNNIF AQFRKNDRDR
QKLIETVVRQ LRGLVTGMSQ HT
