ID   YKT6B_XENLA             Reviewed;         198 AA.
AC   Q32N70;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Synaptobrevin homolog YKT6-B;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=ykt6-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2005) 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:0000250|UniProtKB:O15498}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic
CC       vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-
CC       anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Probably
CC       cycles through vesicles between Golgi and endosomes. {ECO:0000250}.
CC   -!- DOMAIN: The longin domain regulates palmitoylation and membrane
CC       targeting. {ECO:0000250}.
CC   -!- PTM: Palmitoylated; catalyzes its own palmitoylation. Palmitoylation is
CC       required for Golgi targeting. {ECO:0000250|UniProtKB:O15498}.
CC   -!- PTM: Farnesylation is required for Golgi targeting.
CC       {ECO:0000250|UniProtKB:O15498}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; BC108800; AAI08801.1; -; mRNA.
DR   RefSeq; NP_001090150.1; NM_001096681.1.
DR   RefSeq; XP_018106774.1; XM_018251285.1.
DR   AlphaFoldDB; Q32N70; -.
DR   SMR; Q32N70; -.
DR   BioGRID; 593010; 1.
DR   DNASU; 735229; -.
DR   GeneID; 735229; -.
DR   KEGG; xla:735229; -.
DR   CTD; 735229; -.
DR   Xenbase; XB-GENE-6254082; ykt6.L.
DR   OMA; ITDHEYP; -.
DR   OrthoDB; 1362424at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 735229; Expressed in blastula and 19 other tissues.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:HGNC-UCL.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:HGNC-UCL.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:HGNC-UCL.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:HGNC-UCL.
DR   GO; GO:0006903; P:vesicle targeting; ISS:HGNC-UCL.
DR   CDD; cd14824; Longin; 1.
DR   CDD; cd15867; R-SNARE_YKT6; 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   Pfam; PF13774; Longin; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   SMART; SM01270; Longin; 1.
DR   SUPFAM; SSF64356; SSF64356; 1.
DR   PROSITE; PS50859; LONGIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW   Golgi apparatus; Lipoprotein; Membrane; Methylation; Palmitate;
KW   Prenylation; Protein transport; Reference proteome; Transferase; Transport.
FT   CHAIN           1..195
FT                   /note="Synaptobrevin homolog YKT6-B"
FT                   /id="PRO_0000280714"
FT   PROPEP          196..198
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396666"
FT   DOMAIN          8..127
FT                   /note="Longin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT   DOMAIN          138..198
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   MOD_RES         195
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           194
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           195
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  22613 MW;  C57621CCAB28D70D CRC64;
     MKLYSLSVLY KGENKVHLLK SAYDVSSFSF FQRSSVQEFM TFTSQLIVER SDKGSRSSVK
     EQEYLCHVYV RNDSLAGVVI ADNEYPPRVC FTLLEKVLEE FSTQVDRIDW PSGSPATIQY
     NALDSYLSKY QNPRDADPMS KVQAELDETK IVLHNTMESL LQRGEKLDDL VSKSEVLGTQ
     SKAFYKTARK QNSCCDIM