GenomeNet

Database: UniProt
Entry: A0A2U9BU59_SCOMX
LinkDB: A0A2U9BU59_SCOMX
Original site: A0A2U9BU59_SCOMX 
ID   A0A2U9BU59_SCOMX        Unreviewed;       356 AA.
AC   A0A2U9BU59;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative synaptobrevin-like YKT6 {ECO:0000313|EMBL:AWP07433.1};
GN   ORFNames=SMAX5B_010458 {ECO:0000313|EMBL:AWP07433.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP07433.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP07433.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP026251; AWP07433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9BU59; -.
DR   Proteomes; UP000246464; Chromosome 9.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022892}.
FT   TRANSMEM        309..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..126
FT                   /note="Longin"
FT                   /evidence="ECO:0000259|PROSITE:PS50859"
FT   DOMAIN          138..195
FT                   /note="V-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50892"
FT   REGION          237..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  38953 MW;  85BA89317DCD8D42 CRC64;
     MKLYSLSILY KGATKSNLLK AATDLSSFSF FQRSSIQEFM TFTSALIVER TSQGSRASVK
     EQEYLCHVYV RNDSLGAVVI ADTEYPQRVA FTLLDKVLDE FSRQVDSIDW PSGNPETINY
     KTLDIHLSKY QNPREADAMT KVQAELDETK IILHNTMESL LERGEKLDDL VAKSEHLGNQ
     SKAFYKTDES EEGWKVVAGV KCDLSGLVTD GGAEGVMGSA VKCEFPTEAP ERIARSASGA
     GAQLSGGERK TSREPMSGSG RTTTPTAWTE MVDPDLAGQL SHAVRQRNGS TAAVTHPSCT
     EGSFTRSSGI IPGAIAATVF IAFLLALYAV LWKCMVSPPQ RKHSKVRVRV HQRSSV
//
DBGET integrated database retrieval system