ID A0A0A2IGU4_PENEN Unreviewed; 200 AA.
AC A0A0A2IGU4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 03-MAY-2023, entry version 44.
DE RecName: Full=Synaptobrevin homolog YKT6 {ECO:0000256|ARBA:ARBA00026133};
GN ORFNames=PEX2_079860 {ECO:0000313|EMBL:KGO56379.1};
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:KGO56379.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO56379.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO56379.1,
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: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004342}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC {ECO:0000256|ARBA:ARBA00008025}.
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:KGO56379.1}.
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DR EMBL; JQFZ01000170; KGO56379.1; -; Genomic_DNA.
DR RefSeq; XP_016598174.1; XM_016745256.1.
DR AlphaFoldDB; A0A0A2IGU4; -.
DR STRING; 27334.A0A0A2IGU4; -.
DR GeneID; 27680676; -.
DR HOGENOM; CLU_074848_0_1_1; -.
DR OrthoDB; 24529at2759; -.
DR PhylomeDB; A0A0A2IGU4; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd14824; Longin; 1.
DR CDD; cd15867; R-SNARE_YKT6; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 3.30.450.50; Longin domain; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR045848; R-SNARE_YKT6.
DR InterPro; IPR001388; Synaptobrevin-like.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45806; SYNAPTOBREVIN HOMOLOG YKT6; 1.
DR PANTHER; PTHR45806:SF1; SYNAPTOBREVIN HOMOLOG YKT6; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 7..107
FT /note="Longin"
FT /evidence="ECO:0000259|PROSITE:PS50859"
FT DOMAIN 140..200
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
SQ SEQUENCE 200 AA; 22851 MW; 12252D4480D5F365 CRC64;
MKILYMGVFR NDTRPALQLC GEKDLSSFSR FTRQNYDEFL MLFTRTVAER TKPGQRQDIE
EKAYTFHAYG RTEGVSGVIM TDGDYPALVA HQLLGKIVDE FLAKYPRTAF SDPSLRENAC
PLPQLKEYIV KYQDPGQADS IMKIQQELDE TKIVLHKTIE SVLERGEKID SLVQKSDGLS
AQSKMFYTQA KKQNSCCVLM
//
