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Database: UniProt
Entry: B4INK3_DROSE
LinkDB: B4INK3_DROSE
Original site: B4INK3_DROSE 
ID   B4INK3_DROSE            Unreviewed;       894 AA.
AC   B4INK3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Exocyst complex component 2 {ECO:0000256|ARBA:ARBA00017526, ECO:0000256|RuleBase:RU365069};
GN   Name=Dsec\GM11139 {ECO:0000313|EMBL:EDW44612.1};
GN   ORFNames=Dsec_GM11139 {ECO:0000313|EMBL:EDW44612.1};
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN   [1] {ECO:0000313|EMBL:EDW44612.1, ECO:0000313|Proteomes:UP000001292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25
RC   {ECO:0000313|Proteomes:UP000001292};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC       {ECO:0000256|ARBA:ARBA00002660, ECO:0000256|RuleBase:RU365069}.
CC   -!- SUBUNIT: Component of the exocyst complex.
CC       {ECO:0000256|RuleBase:RU365069}.
CC   -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000256|ARBA:ARBA00010578,
CC       ECO:0000256|RuleBase:RU365069}.
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DR   EMBL; CH676463; EDW44612.1; -; Genomic_DNA.
DR   RefSeq; XP_002045313.1; XM_002045277.1.
DR   AlphaFoldDB; B4INK3; -.
DR   SMR; B4INK3; -.
DR   STRING; 7238.B4INK3; -.
DR   EnsemblMetazoa; FBtr0194124; FBpp0192616; FBgn0166084.
DR   GeneID; 6621133; -.
DR   KEGG; dse:6621133; -.
DR   HOGENOM; CLU_005811_1_0_1; -.
DR   OMA; RMWMDVD; -.
DR   OrthoDB; 2901642at2759; -.
DR   PhylomeDB; B4INK3; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0000145; C:exocyst; IEA:UniProtKB-UniRule.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00603; IPT_PCSR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR029175; EXOC2/Sec5.
DR   InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_dom.
DR   PANTHER; PTHR13043:SF1; EXOCYST COMPLEX COMPONENT 2; 1.
DR   PANTHER; PTHR13043; EXOCYST COMPLEX COMPONENT SEC5; 1.
DR   Pfam; PF15469; Sec5; 1.
DR   Pfam; PF01833; TIG; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483, ECO:0000256|RuleBase:RU365069};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU365069};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365069}.
FT   DOMAIN          5..86
FT                   /note="IPT/TIG"
FT                   /evidence="ECO:0000259|Pfam:PF01833"
FT   DOMAIN          126..889
FT                   /note="Exocyst complex component EXOC2/Sec5 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15469"
FT   REGION          398..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  100754 MW;  9447C55E6403D3FA CRC64;
     MAPQPVVTGL SPKEGPPGTR VIIRGEFLGT RVHDLIGLKI CGSDCLLSAE WKSPNKIIAR
     TGPAKGKGDI IVTTLSGGVG TSTVQFRAYH ETIGPLKESA VWIEESPSQN FAWGRRTLAQ
     SGLTQEDPLG LSIEGNEQKI PEDLRDLFPE ACGDLSQEHF SPAWFLLENH LATSFEDLKA
     GLSYLKRKVE SQKEGQLSFL KSNAGSVIDQ LDTLMNIRDK LQEDVKLHGN ETLNILETSI
     ENSISESQKI FTDVLVRKEK ADSTRSVLFA LSRHKFLFCL PNSVDRRAKA GEYDIVVNDY
     SRAKNLFGKT EIPIFRKVLE EVDHRILSVR KQLHEKVVKM PQSVEQQKKL IKALISLELQ
     QSGTPIGDKL RNIDPAWDAI EARAKYLEWT FRQTFDQHTS KDSSAQEKAK NRDSSQAPNR
     VNFCEELCDI AASQLPDLWR LGQLYFTGEL RGPHDPKPGD FKRMVLNAIE KFCVYLRLAI
     LIATDQRALR QSSGLAWPIG SASATHQFLP WIPQCLRFTR IAYATLISLD LPSEALDIIQ
     KLIDEVRLFC FSIIFKRATD RCKKLGSQET WELGVEEYPG ATLLPAALEA LLIETLDEVQ
     SVCMQRETRE GNLLEPQSDG QREVTQRLQE FLSAFSAVIE ELAFHSHDEE TPTHNVSQLL
     GFPNAQQPDS VAGSSGAAAV TWEQRMLCCL ANYAYCNKIF FPRLGDIFVR YGYPLPTLAI
     ETARYTVNQL FTNLLEEYVE HKGDPLVGTI EPSMYLGRFQ WDHEMEIGQL RPYAHECCDN
     LVGVYSEIYS ISPALLRPIL ESIVQTISEE LARLMSCVQR FSFTGAIQAH VDIRLLRDSL
     EGYVNETAKN YFMEALEAIN PPLSGEQKRK ADEILERVKR NMRLQLLCFS VKDP
//
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