YKT6_MOUSE
ID YKT6_MOUSE Reviewed; 198 AA.
AC Q9CQW1; O88595;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Synaptobrevin homolog YKT6;
DE EC=2.3.1.-;
DE Flags: Precursor;
GN Name=Ykt6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Kidney, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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:0000250|UniProtKB:O15498}.
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. {ECO:0000250}.
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; AF076956; AAC26834.1; -; mRNA.
DR EMBL; AK002916; BAB22455.1; -; mRNA.
DR EMBL; AK007486; BAB25062.1; -; mRNA.
DR EMBL; AK147098; BAE27674.1; -; mRNA.
DR EMBL; AK150472; BAE29589.1; -; mRNA.
DR EMBL; AK159253; BAE34934.1; -; mRNA.
DR EMBL; AL645469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006760; AAH06760.1; -; mRNA.
DR CCDS; CCDS24410.1; -.
DR RefSeq; NP_062635.2; NM_019661.4.
DR AlphaFoldDB; Q9CQW1; -.
DR SMR; Q9CQW1; -.
DR BioGRID; 207964; 7.
DR IntAct; Q9CQW1; 1.
DR MINT; Q9CQW1; -.
DR STRING; 10090.ENSMUSP00000002818; -.
DR iPTMnet; Q9CQW1; -.
DR PhosphoSitePlus; Q9CQW1; -.
DR SwissPalm; Q9CQW1; -.
DR EPD; Q9CQW1; -.
DR MaxQB; Q9CQW1; -.
DR PaxDb; Q9CQW1; -.
DR PeptideAtlas; Q9CQW1; -.
DR PRIDE; Q9CQW1; -.
DR ProteomicsDB; 299616; -.
DR Antibodypedia; 27085; 73 antibodies from 17 providers.
DR DNASU; 56418; -.
DR Ensembl; ENSMUST00000002818; ENSMUSP00000002818; ENSMUSG00000002741.
DR GeneID; 56418; -.
DR KEGG; mmu:56418; -.
DR UCSC; uc007hxp.3; mouse.
DR CTD; 10652; -.
DR MGI; MGI:1927550; Ykt6.
DR VEuPathDB; HostDB:ENSMUSG00000002741; -.
DR eggNOG; KOG0861; Eukaryota.
DR GeneTree; ENSGT00390000015164; -.
DR HOGENOM; CLU_074848_3_0_1; -.
DR InParanoid; Q9CQW1; -.
DR OMA; ITDHEYP; -.
DR OrthoDB; 1362424at2759; -.
DR PhylomeDB; Q9CQW1; -.
DR TreeFam; TF105606; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 56418; 25 hits in 71 CRISPR screens.
DR ChiTaRS; Ykt6; mouse.
DR PRO; PR:Q9CQW1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQW1; protein.
DR Bgee; ENSMUSG00000002741; Expressed in cortical plate and 254 other tissues.
DR Genevisible; Q9CQW1; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0097441; C:basal dendrite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:HGNC-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
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:MGI.
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 Coiled coil; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transferase; Transport.
FT CHAIN 1..195
FT /note="Synaptobrevin homolog YKT6"
FT /id="PRO_0000280710"
FT PROPEP 196..198
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396662"
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 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 CONFLICT 95
FT /note="E -> D (in Ref. 1; AAC26834)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="E -> V (in Ref. 1; AAC26834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22314 MW; 50A6E4EA7614592B CRC64;
MKLYSLSVLY KGDPKAVLLK AAYDVSSFSF FQRSSVQEFM TFTSQLIVER SGKGSRASVK
EQEYLCHVYV RSDSLAGVVI ADSEYPSRVA FTLLEKVLDE FSKQVDRIDW PVGSPATIQY
TGLDDHLSKY QNPREADPMS KVQAELDETK IILHNTMESL LERGEKLDDL VSKSEVLGTQ
SKAFYKTARK QNSCCAIM
