ID E2ATZ0_CAMFO Unreviewed; 200 AA.
AC E2ATZ0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Synaptobrevin-like protein YKT6 {ECO:0000313|EMBL:EFN63121.1};
GN ORFNames=EAG_07799 {ECO:0000313|EMBL:EFN63121.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN63121.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- FUNCTION: Vesicular soluble NSF attachment protein receptor (v-SNARE)
CC mediating vesicle docking and fusion to a specific acceptor cellular
CC compartment. Functions in endoplasmic reticulum to Golgi transport; as
CC part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in
CC early/recycling endosome to TGN transport; as part of a SNARE complex
CC composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase
CC activity. {ECO:0000256|ARBA:ARBA00025256}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00025701}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00025701}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00025701}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004444}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004444}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004444}. 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}.
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DR EMBL; GL442747; EFN63121.1; -; Genomic_DNA.
DR RefSeq; XP_011263900.1; XM_011265598.2.
DR AlphaFoldDB; E2ATZ0; -.
DR STRING; 104421.E2ATZ0; -.
DR EnsemblMetazoa; XM_011265598.3; XP_011263900.1; LOC105255996.
DR GeneID; 105255996; -.
DR KEGG; cfo:105255996; -.
DR InParanoid; E2ATZ0; -.
DR OMA; HYIGIIR; -.
DR OrthoDB; 24529at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; 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 SMART; SM01270; Longin; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT DOMAIN 9..128
FT /note="Longin"
FT /evidence="ECO:0000259|PROSITE:PS50859"
FT DOMAIN 139..199
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
SQ SEQUENCE 200 AA; 22698 MW; E9D99D8AB6094E15 CRC64;
MVKLYALTVL YKSPTSATTL KAAYDVESFS FFQRNSIKEF MCFVSKTIVE RTQTCARQSV
KEGEYMCHVY VRADNLAAVL ISDHEYPRRV AHTLITKIMD EFEVKNLSST WPALKEATTD
FPQINTYLAK YQNPVEADAL TKMQNDLDET KIILHNTLEA VLQRGEKLDD LVSKSEGLSI
QSKAFYKTAR KTNSCCSLAP
//
