ID   EXOC6_CANLF             Reviewed;         803 AA.
AC   E2R766;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
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, SEC15L, SEC15L1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=20890297; DOI=10.1038/ncb2106;
RA   Bryant D.M., Datta A., Rodriguez-Fraticelli A.E., Peraenen J.,
RA   Martin-Belmonte F., Mostov K.E.;
RT   "A molecular network for de novo generation of the apical surface and
RT   lumen.";
RL   Nat. Cell Biol. 12:1035-1045(2010).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane (By
CC       similarity). Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2,
CC       CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane
CC       initiation sites (AMIS), apical surface formation and lumenogenesis.
CC       {ECO:0000250, ECO:0000269|PubMed:20890297}.
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC       EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with CNTRL.
CC       Interacts with RAB11A in a GTP-dependent manner (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:O54923}.
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}.
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DR   RefSeq; NP_001300715.1; NM_001313786.1.
DR   AlphaFoldDB; E2R766; -.
DR   SMR; E2R766; -.
DR   STRING; 9615.ENSCAFP00000011202; -.
DR   PaxDb; E2R766; -.
DR   GeneID; 477771; -.
DR   KEGG; cfa:477771; -.
DR   CTD; 54536; -.
DR   eggNOG; KOG2176; Eukaryota.
DR   InParanoid; E2R766; -.
DR   OrthoDB; 185623at2759; -.
DR   Proteomes; UP000002254; Chromosome 28.
DR   Bgee; ENSCAFG00000007534; Expressed in granulocyte and 48 other tissues.
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: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:0090522; P:vesicle tethering involved in exocytosis; IEA:InterPro.
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   3: Inferred from homology;
KW   Cell projection; Cytoplasm; Exocytosis; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..803
FT                   /note="Exocyst complex component 6"
FT                   /id="PRO_0000409022"
SQ   SEQUENCE   803 AA;  93532 MW;  FD950699C1E6C753 CRC64;
     MAENSEGLGT VPEHERILQE IESTDTACVG PTLRSVYDDQ PNAHKKFMEK LDACIRNHDK
     EIEKMCNFHH QGFVDAITEL LKVRTDAEKL KVQVTDTNRR FQDAGKEVII QTEDIIRCRI
     QQRNITTVVE NLQYAFPVLE MYSKLKEQMT AKRYYSALKT MEQLENVYFP RVSQYRFCQL
     MIENLPKLRE DIKEISMSDL KDFLESIRKH SDKIGETAMK QAQQQKTFSV ALQKQNNVKF
     GKNMYINDRI PEERKENELK QGFEEEDENE EEILTVQDLV DFSPVYRCLH IYSVLGDEET
     FENYYRKQRK KQARLVLQPQ SNMHETVDGY RRYFTQIVGF FVVEDHILHV TQGLVTRAYT
     DELWNMALSK IIAVLRAHSS YCTDPDLVLE LKNLIVIFAD TLQGYGFPVN RLFDLLFEIR
     DQYNETLLKK WAGVFRDIFE EDNYSPIPIV NEEEYKAVIS KFPFQDPDFE KQSFPKKFPM
     SQSVPHIYIQ VKEFIYASLK FSESLHRSST EIDDMLRKST NLLLTRTLSS CLLNLIRKPH
     IGLTELVQII INTTHLEQAC KYLEDFITNI TNISQETVHT TRLYGLSTFK DARHAAEGEI
     YTKLNQKIDE FVQLADYDWT MSEPDGRASG YLMDLINFLR SIFQVFTHLP GKVAQTACMS
     ACQHLSTSLM QMLLDSELKQ ISMGAVQQFN LDVIQCELFA SSEPVPGFQG DTLQLAFIDL
     RQLLDLFMVW DWSTYLADYG QPASKYLRVN PNTALTLLEK MKDTSKKNNI FAQFRKNDRD
     KQKLIETVVK QLRSLVNGMS QHT