YKT6A_XENLA
ID YKT6A_XENLA Reviewed; 198 AA.
AC Q6DDU7; O73865;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Synaptobrevin homolog YKT6-A;
DE EC=2.3.1.-;
DE AltName: Full=Xsnare1;
DE Flags: Precursor;
GN Name=ykt6-a;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9675119; DOI=10.1006/bbrc.1998.8957;
RA Park H.-S., Kim M., Shim S., Han J.-K.;
RT "Identification and expression study of a Xenopus homologue of prenylated
RT SNARE gene.";
RL Biochem. Biophys. Res. Commun. 248:235-239(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) 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 -!- DEVELOPMENTAL STAGE: Maternally inherited. Detected in oocytes and
CC eggs. Expression declines during early development and is not detected
CC in neurula, tailbud and tadpole embryos. {ECO:0000269|PubMed:9675119}.
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; AF067648; AAC32182.1; -; mRNA.
DR EMBL; BC077411; AAH77411.1; -; mRNA.
DR PIR; JE0228; JE0228.
DR RefSeq; NP_001081758.1; NM_001088289.1.
DR RefSeq; XP_018109622.1; XM_018254133.1.
DR RefSeq; XP_018109623.1; XM_018254134.1.
DR RefSeq; XP_018109624.1; XM_018254135.1.
DR AlphaFoldDB; Q6DDU7; -.
DR SMR; Q6DDU7; -.
DR DNASU; 398034; -.
DR GeneID; 398034; -.
DR KEGG; xla:398034; -.
DR CTD; 398034; -.
DR Xenbase; XB-GENE-949734; ykt6.S.
DR OMA; MIKASAN; -.
DR OrthoDB; 1362424at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 398034; Expressed in egg cell 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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-A"
FT /id="PRO_0000280713"
FT PROPEP 196..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396665"
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"
FT CONFLICT 27
FT /note="S -> P (in Ref. 1; AAC32182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22611 MW; 062429D29741623F CRC64;
MKLYSLSVLY KGENKVHLLK SAYDVSSFSF FQRSSIQEFM AFTSQLIVER SDKGSRSSVK
EQEYLCHVYV RNDSLAGVVI ADNEYPPRVC FTLLEKVLEE FSTQVDRIDW PSGSPATIQY
NALDSYLSKY QNPRDADPMS KVQAELDETK IILHNTMESL LQRGEKLDDL VSKSEVLGTQ
SKAFYKTARK QNSCCDIM
