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Database: UniProt
Entry: A0A0A2J1C6_PENEN
LinkDB: A0A0A2J1C6_PENEN
Original site: A0A0A2J1C6_PENEN 
ID   A0A0A2J1C6_PENEN        Unreviewed;       348 AA.
AC   A0A0A2J1C6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   02-APR-2025, entry version 39.
DE   SubName: Full=Syntaxin, N-terminal {ECO:0000313|EMBL:KGO55357.1};
GN   ORFNames=PEX2_030610 {ECO:0000313|EMBL:KGO55357.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO55357.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO55357.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO55357.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC       pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO55357.1}.
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DR   EMBL; JQFZ01000195; KGO55357.1; -; Genomic_DNA.
DR   RefSeq; XP_016597508.1; XM_016740336.1.
DR   AlphaFoldDB; A0A0A2J1C6; -.
DR   STRING; 27334.A0A0A2J1C6; -.
DR   GeneID; 27675755; -.
DR   VEuPathDB; FungiDB:PEXP_073310; -.
DR   HOGENOM; CLU_044998_0_1_1; -.
DR   OrthoDB; 421009at2759; -.
DR   PhylomeDB; A0A0A2J1C6; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:TreeGrafter.
DR   GO; GO:0031201; C:SNARE complex; IEA:TreeGrafter.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:TreeGrafter.
DR   GO; GO:0000149; F:SNARE binding; IEA:TreeGrafter.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:TreeGrafter.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:TreeGrafter.
DR   GO; GO:0048278; P:vesicle docking; IEA:TreeGrafter.
DR   GO; GO:0006906; P:vesicle fusion; IEA:TreeGrafter.
DR   CDD; cd15844; SNARE_syntaxin5; 1.
DR   FunFam; 1.20.58.70:FF:000007; ER-golgi SNARE complex subunit; 1.
DR   Gene3D; 1.20.58.70; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR021538; Syntaxin-5_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF3; SYNTAXIN-5; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF11416; Syntaxin-5_N; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        328..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          257..319
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          25..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   348 AA;  38452 MW;  FA54CE6137679A92 CRC64;
     MTGPSIQDRT SEFSAILGHA QKRLGTSKVG SQRQALLTDA QRRQADASPQ GAAQEAKAAR
     SEFARRARDI GRGITGTMAK LQRLAELAKR KTLFDDRPVE ISELTYVIKQ DLAALNQNIA
     SLQALTHAQH PKSTRSKTDQ EGEHNDNVVV MLQGKLADVG ASFKEVLEVR TKNIQASRTR
     TENFVSSVSS KSHSALDAQR SDSPLYNTSG RRTPQPGYQG NSSDLLTLEP SNPSPLGRPS
     FQSDQQLMVM EEGESSNTYV QARGEAIEAI ERTISELGGI FGQLAQMVSE QSEMIQRIDA
     NTEDVVDNVQ GAQRELMKYW TRVSGNRWLI AKMFGILMIF FLLWVLIS
//
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