(data stored in SCRATCH zone)

SWISSPROT: Q750U7_ASHGO

ID   Q750U7_ASHGO            Unreviewed;       859 AA.
AC   Q750U7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=Exocyst complex component SEC5 {ECO:0000256|RuleBase:RU365069};
GN   ORFNames=AGOS_AGL158C {ECO:0000313|EMBL:AAS54333.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54333.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54333.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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|RuleBase:RU365069}.
CC   -!- SUBUNIT: Component of the exocyst complex.
CC       {ECO:0000256|RuleBase:RU365069}.
CC   -!- SIMILARITY: Belongs to the SEC5 family.
CC       {ECO:0000256|RuleBase:RU365069}.
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DR   EMBL; AE016820; AAS54333.1; -; Genomic_DNA.
DR   RefSeq; NP_986509.1; NM_211571.1.
DR   STRING; 33169.AAS54333; -.
DR   EnsemblFungi; AAS54333; AAS54333; AGOS_AGL158C.
DR   GeneID; 4622802; -.
DR   KEGG; ago:AGOS_AGL158C; -.
DR   HOGENOM; HOG000065950; -.
DR   InParanoid; Q750U7; -.
DR   KO; K17637; -.
DR   OMA; HDARMEA; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR   GO; GO:0001927; P:exocyst assembly; IEA:EnsemblFungi.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   InterPro; IPR029175; EXOC2/Sec5.
DR   InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR   PANTHER; PTHR13043; PTHR13043; 1.
DR   Pfam; PF15469; Sec5; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750U7.
DR   SWISS-2DPAGE; Q750U7.
KW   Exocytosis {ECO:0000256|RuleBase:RU365069};
KW   Protein transport {ECO:0000256|RuleBase:RU365069};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transport {ECO:0000256|RuleBase:RU365069}.
FT   DOMAIN          123..303
FT                   /note="Sec5"
FT                   /evidence="ECO:0000259|Pfam:PF15469"
FT   REGION          29..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..51
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  99853 MW;  9D8E02A3215CE095 CRC64;
     MVEMLNPFAF DNSKLLEVYQ LKTLNPRSTW EKETTRNDST ENSEASRKQR SLSDIPDPLQ
     PSRSMEGLLE QLNIPPEERH RYYINCNSFN TKLFLRNIHK DDTFKELADA LESLNVSMTE
     EGNDLKNLVQ TNFVRYVRCK SNLDQIYDQF NKRMSGNENF LGIDHLDESV NNMVRGTTMK
     VIPLVDQASK VKHYKSAIRY VQDNKELFDL PKTLIESVNK KDYGTLMSEY KNGCKLYAQT
     KQNHVVTKIW KEVETIIDQY RNHTWEQLLE SVENENQEYF LPLISKLVDL KVEENPVNLW
     MTNRLKRFHT QLRTLSQTMM EKIVNAQHDI LKNNIAENID LTFYLNMETY SEDMKNVASR
     KYNLTDSPIV IEMWLLILKY ITTISDLCTK FVEFWEHVER FMNNSYQTTL LNEKRKENII
     GLGDQTQEEA TMLQLSKTEI AVTREGGQNF VKLLNRALSD LFMSTQQSLG KEQAKVPEGA
     YPSHFGFIPP RCNSLSCLRY LPKIVDPILK FTTELAQLTI TDDCIRILRT LDEMILDRCV
     GAISSTKLRD MSNSHELEDW EVFQVVGDEK YCITQYPEIV LCFNQYSIRT MRDILFSYEK
     LPVLNGISIV SYPSDQLVSV IELQQITSLE SVLESILKNA AKDKDNPRNS HTILTLTNLQ
     HIKAHTFPEI LQYFDEAFES NLNAKKLEIF TLLKKMESSI FGNYLSGLKM TLRDILEEKF
     HDINWATHSS NSFRAGDYII ESLMILVTVH SECFQLGPQL IQRILKESQI FISKYLFEAF
     KPYIGHISSD GLLQITVDLQ FFQRVLRGHL EHETVTILNA CLQSCFQNDI PRMQRCITET
     DPIVTSNLNR TSVQFASFE
//

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