ID   SEC9_ASHGO              Reviewed;         533 AA.
AC   Q752V4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Protein transport protein SEC9;
GN   Name=SEC9; OrderedLocusNames=AFR469W;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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., Poehlmann 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]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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   -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR   EMBL; AE016819; AAS53840.1; -; Genomic_DNA.
DR   RefSeq; NP_986016.1; NM_212152.1.
DR   AlphaFoldDB; Q752V4; -.
DR   SMR; Q752V4; -.
DR   STRING; 33169.AAS53840; -.
DR   PRIDE; Q752V4; -.
DR   EnsemblFungi; AAS53840; AAS53840; AGOS_AFR469W.
DR   GeneID; 4622293; -.
DR   KEGG; ago:AGOS_AFR469W; -.
DR   eggNOG; KOG3065; Eukaryota.
DR   HOGENOM; CLU_020823_1_0_1; -.
DR   InParanoid; Q752V4; -.
DR   OMA; LDINVHM; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0035493; P:SNARE complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   SMART; SM00397; t_SNARE; 2.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..533
FT                   /note="Protein transport protein SEC9"
FT                   /id="PRO_0000213607"
FT   DOMAIN          318..380
FT                   /note="t-SNARE coiled-coil homology 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          470..532
FT                   /note="t-SNARE coiled-coil homology 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  59285 MW;  955FA94A2C718341 CRC64;
     MGFKKFFGIR PPEEDTPERN RDLLTEEGIA TKNPNSFRKE KFAAYGKFAA ANAQDHVYAP
     AGYEQYARPG AGADKDELES LNRAATDAGD IGNTSRVGQP QQRDPYAVND NYNPYANGTA
     RDPYATAQPY ARQAPVRQAG PRHAAGTPYG SAAVPQGGPG NPYGGSTAGA GTGRNPYQKN
     MNATVYPPAA GKTANPYASM AQDPYGKGEQ RGIAGGPVAM PVPMQPRPQA AAETPRPQAA
     AEKRAPAVDV DDLNAVIEPT NEDDDLNNSI HEGNEGLNGQ GQAPRRGFQT FEELQREQEM
     KQQMEEDEEV DEIKQQIRFT KQSSVASTRN TLKMAQDAEL AGMNSLGMLG HQSEKLNNVE
     RNLNLMKVQN RVAEDKVAEL KRLNRNILAV HVGNPFTSKR KVREAEERIK NQRMQDKMQQ
     EETTTQLMSS TNRIENALND ERHSVRERYQ RDQALERAKK YQFENDEEDD EMEFEIDRNL
     DKIGQVSGRL KKLAIAAGQE IDSQQSRIKR IEEDADDMDI RIHLNTSRLT NIR