YKT6_RAT
ID YKT6_RAT Reviewed; 198 AA.
AC Q5EGY4; O35487;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Synaptobrevin homolog YKT6;
DE EC=2.3.1.-;
DE Flags: Precursor;
GN Name=Ykt6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=10073573; DOI=10.1089/104454999315529;
RA Catchpoole D.R., Wanjin H.;
RT "Characterization of the sequence and expression of a Ykt6 prenylated SNARE
RT from rat.";
RL DNA Cell Biol. 18:141-145(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RA Lippert U., Ferrari D.M., Jahn R.;
RT "Expression of rat Ykt6 in rat basophil (RBL) cells.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GOSR1; GOSR2 AND STX5.
RX PubMed=11323436; DOI=10.1074/jbc.m102786200;
RA Zhang T., Hong W.;
RT "Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and
RT participates in a late stage in endoplasmic reticulum-Golgi transport.";
RL J. Biol. Chem. 276:27480-27487(2001).
RN [4]
RP INTERACTION WITH BET1L; GOSR1 AND STX5.
RX PubMed=11927603; DOI=10.1083/jcb.200112127;
RA Shorter J., Beard M.B., Seemann J., Dirac-Svejstrup A.B., Warren G.;
RT "Sequential tethering of Golgins and catalysis of SNAREpin assembly by the
RT vesicle-tethering protein p115.";
RL J. Cell Biol. 157:45-62(2002).
RN [5]
RP INTERACTION WITH BET1L; GOSR1 AND STX5.
RX PubMed=12388752; DOI=10.1091/mbc.e02-01-0004;
RA Xu Y., Martin S., James D.E., Hong W.;
RT "GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is
RT implicated in traffic in the early cisternae of the Golgi apparatus.";
RL Mol. Biol. Cell 13:3493-3507(2002).
RN [6]
RP TISSUE SPECIFICITY, ISOPRENYLATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF CYS-194 AND CYS-195.
RX PubMed=12589064; DOI=10.1091/mbc.e02-09-0556;
RA Hasegawa H., Zinsser S., Rhee Y., Vik-Mo E.O., Davanger S., Hay J.C.;
RT "Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment
RT by its profilin-like amino terminal domain.";
RL Mol. Biol. Cell 14:698-720(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-8; PHE-39; PHE-42; ARG-50;
RP ARG-56 AND VAL-59.
RX PubMed=15331663; DOI=10.1242/jcs.01314;
RA Hasegawa H., Yang Z., Oltedal L., Davanger S., Hay J.C.;
RT "Intramolecular protein-protein and protein-lipid interactions control the
RT conformation and subcellular targeting of neuronal Ykt6.";
RL J. Cell Sci. 117:4495-4508(2004).
RN [8]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP X.
RX PubMed=28770820; DOI=10.1038/ncomms14130;
RA Zhang S., Masuyer G., Zhang J., Shen Y., Lundin D., Henriksson L.,
RA Miyashita S.I., Martinez-Carranza M., Dong M., Stenmark P.;
RT "Identification and characterization of a novel botulinum neurotoxin.";
RL Nat. Commun. 8:14130-14130(2017).
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:0000269|PubMed:11323436}.
CC -!- SUBUNIT: Identified in 2 different SNARE complexes; the first one
CC composed of GOSR1, GOSR2 and STX5 and the second one composed of BET1L,
CC GOSR1 and STX5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasmic vesicle membrane;
CC Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor;
CC Cytoplasmic side. Note=Probably cycles through vesicles between Golgi
CC and endosomes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed by neurons in brain and faintly
CC detected in spleen, lung and kidney (at protein level). Ubiquitously
CC expressed. {ECO:0000269|PubMed:12589064}.
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 -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type X (BoNT/X) which hydrolyzes the 173-Lys-|-Ser-174 bond
CC and probably inhibits neurotransmitter release (PubMed:28770820). It
CC remains unknown whether BoNT/X is ever produced, or what organisms it
CC targets. {ECO:0000269|PubMed:28770820}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF033027; AAD09152.1; -; mRNA.
DR EMBL; AY881621; AAW81771.1; -; mRNA.
DR RefSeq; NP_113880.2; NM_031692.2.
DR PDB; 3KYQ; X-ray; 2.44 A; A=1-198.
DR PDBsum; 3KYQ; -.
DR AlphaFoldDB; Q5EGY4; -.
DR SMR; Q5EGY4; -.
DR CORUM; Q5EGY4; -.
DR IntAct; Q5EGY4; 6.
DR STRING; 10116.ENSRNOP00000020693; -.
DR jPOST; Q5EGY4; -.
DR PaxDb; Q5EGY4; -.
DR PRIDE; Q5EGY4; -.
DR Ensembl; ENSRNOT00000020693; ENSRNOP00000020693; ENSRNOG00000014785.
DR GeneID; 64351; -.
DR KEGG; rno:64351; -.
DR UCSC; RGD:70897; rat.
DR CTD; 10652; -.
DR RGD; 70897; Ykt6.
DR eggNOG; KOG0861; Eukaryota.
DR GeneTree; ENSGT00390000015164; -.
DR HOGENOM; CLU_074848_3_0_1; -.
DR InParanoid; Q5EGY4; -.
DR OMA; ITDHEYP; -.
DR OrthoDB; 1362424at2759; -.
DR PhylomeDB; Q5EGY4; -.
DR TreeFam; TF105606; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR EvolutionaryTrace; Q5EGY4; -.
DR PRO; PR:Q5EGY4; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000014785; Expressed in stomach and 20 other tissues.
DR Genevisible; Q5EGY4; RN.
DR GO; GO:0097440; C:apical dendrite; IDA:RGD.
DR GO; GO:0097441; C:basal dendrite; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
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:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:HGNC-UCL.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:RGD.
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:0042147; P:retrograde transport, endosome to Golgi; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW ER-Golgi transport; Golgi apparatus; Lipoprotein; Membrane; Methylation;
KW Palmitate; Phosphoprotein; Prenylation; Protein transport;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..195
FT /note="Synaptobrevin homolog YKT6"
FT /id="PRO_0000280711"
FT PROPEP 196..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396663"
FT DOMAIN 8..131
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 SITE 173..174
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type X (BoNT/X)"
FT /evidence="ECO:0000269|PubMed:28770820"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15498"
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 MUTAGEN 8
FT /note="V->D: Mistargeted to Golgi and plasma membrane.
FT Normally targeted to vesicular structures; when associated
FT with A-194 or A-195."
FT /evidence="ECO:0000269|PubMed:15331663"
FT MUTAGEN 39
FT /note="F->E: Mistargeted to Golgi and plasma membrane; when
FT associated with E-42. Normally targeted to vesicular
FT structures; when associated with E-42 and A-195."
FT /evidence="ECO:0000269|PubMed:15331663"
FT MUTAGEN 42
FT /note="F->E: Mistargeted to Golgi and plasma membrane; when
FT associated with E-39. Normally targeted to vesicular
FT structures; when associated with E-39 and A-195."
FT /evidence="ECO:0000269|PubMed:15331663"
FT MUTAGEN 50
FT /note="R->E: Mistargeted to Golgi and plasma membrane; when
FT associated with E-56. Normally targeted to vesicular
FT structures; when associated with E-56 and A-195."
FT /evidence="ECO:0000269|PubMed:15331663"
FT MUTAGEN 56
FT /note="R->E: Mistargeted to Golgi and plasma membrane; when
FT associated with E-50. Normally targeted to vesicular
FT structures; when associated with E-50 and A-195."
FT /evidence="ECO:0000269|PubMed:15331663"
FT MUTAGEN 59
FT /note="V->E: Mistargeted to Golgi and plasma membrane."
FT /evidence="ECO:0000269|PubMed:15331663"
FT MUTAGEN 194
FT /note="C->A: Loss of prenylation and normally targeted to
FT vesicular structures; when associated with A-195. Normally
FT targeted to vesicular structures; when associated with D-
FT 8."
FT /evidence="ECO:0000269|PubMed:12589064"
FT MUTAGEN 195
FT /note="C->A: Loss of prenylation and normally targeted to
FT vesicular structures; when associated with A-194. Normally
FT targeted to vesicular structures; when associated with D-8.
FT Normally targeted to vesicular structures; when associated
FT with E-39 and E-42. Normally targeted to vesicular
FT structures; when associated with E-50 and E-56."
FT /evidence="ECO:0000269|PubMed:12589064"
FT CONFLICT 9
FT /note="F -> L (in Ref. 1; AAD09152)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="P -> K (in Ref. 1; AAD09152)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="E -> Q (in Ref. 1; AAD09152)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="R -> T (in Ref. 1; AAD09152)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:3KYQ"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:3KYQ"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:3KYQ"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3KYQ"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:3KYQ"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3KYQ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:3KYQ"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:3KYQ"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3KYQ"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:3KYQ"
SQ SEQUENCE 198 AA; 22369 MW; 384F4EDBC8295407 CRC64;
MKLYSLSVFY KGEPKAVLLK AAYDVSSFSF FQRSSVQEFM TFTSQLIVER SAKGSRASVK
EQEYLCHVYV RSDSLAGVVI ADSEYPSRVA FTLLEKVLDE FSKQVDRIDW PVGSPATIHY
TALDGHLSRY QNPREADPMS KVQAELDETK IILHNTMESL LERGEKLDDL VSKSEVLGTQ
SKAFYKTARK QNSCCAIM
