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YKT62_ARATH
ID   YKT62_ARATH             Reviewed;         199 AA.
AC   Q9LVM9;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=VAMP-like protein YKT62 {ECO:0000303|PubMed:15919093};
DE            Short=AtYKT62 {ECO:0000303|PubMed:15919093};
DE   AltName: Full=ATGP1-like protein;
DE   Flags: Precursor;
GN   Name=YKT62 {ECO:0000303|PubMed:15919093};
GN   OrderedLocusNames=At5g58180 {ECO:0000312|Araport:AT5G58180};
GN   ORFNames=MCK7.5 {ECO:0000312|EMBL:BAA96909.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   FUNCTION, INTERACTION WITH SYP41, AND SUBUNIT.
RX   PubMed=15919093; DOI=10.1016/j.jmb.2005.04.061;
RA   Chen Y., Shin Y.-K., Bassham D.C.;
RT   "YKT6 is a core constituent of membrane fusion machineries at the
RT   Arabidopsis trans-Golgi network.";
RL   J. Mol. Biol. 350:92-101(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=24021022; DOI=10.1186/1471-2091-14-22;
RA   Kim S.-J., Bassham D.C.;
RT   "Functional redundancy between trans-Golgi network SNARE family members in
RT   Arabidopsis thaliana.";
RL   BMC Biochem. 14:22-22(2013).
CC   -!- FUNCTION: Involved in the secretory pathway (PubMed:15919093).
CC       Essential for membrane fusion mediated by either SYP41 or SYP61;
CC       triggers the fusion of phospholipid vesicles containing SYP41 or SYP61
CC       and VTI12 (PubMed:15919093, PubMed:24021022).
CC       {ECO:0000269|PubMed:15919093, ECO:0000269|PubMed:24021022}.
CC   -!- SUBUNIT: Interacts with SYP41 (PubMed:15919093). Core constituent of
CC       the SNARE complex required for membrane fusion at the trans-Golgi
CC       network (PubMed:15919093). {ECO:0000269|PubMed:15919093}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; AB019228; BAA96909.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97008.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97009.1; -; Genomic_DNA.
DR   RefSeq; NP_001318826.1; NM_001345292.1.
DR   RefSeq; NP_200626.1; NM_125203.2.
DR   AlphaFoldDB; Q9LVM9; -.
DR   SMR; Q9LVM9; -.
DR   BioGRID; 21174; 1.
DR   STRING; 3702.AT5G58180.1; -.
DR   PaxDb; Q9LVM9; -.
DR   PRIDE; Q9LVM9; -.
DR   ProteomicsDB; 242939; -.
DR   EnsemblPlants; AT5G58180.1; AT5G58180.1; AT5G58180.
DR   EnsemblPlants; AT5G58180.2; AT5G58180.2; AT5G58180.
DR   GeneID; 835930; -.
DR   Gramene; AT5G58180.1; AT5G58180.1; AT5G58180.
DR   Gramene; AT5G58180.2; AT5G58180.2; AT5G58180.
DR   KEGG; ath:AT5G58180; -.
DR   Araport; AT5G58180; -.
DR   TAIR; locus:2161288; AT5G58180.
DR   eggNOG; KOG0861; Eukaryota.
DR   HOGENOM; CLU_074848_2_0_1; -.
DR   InParanoid; Q9LVM9; -.
DR   OMA; PWPYLKE; -.
DR   OrthoDB; 1362424at2759; -.
DR   PhylomeDB; Q9LVM9; -.
DR   PRO; PR:Q9LVM9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LVM9; baseline and differential.
DR   Genevisible; Q9LVM9; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
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; IPR001388; Synaptobrevin.
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; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Methylation; Palmitate; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..196
FT                   /note="VAMP-like protein YKT62"
FT                   /id="PRO_0000206749"
FT   PROPEP          197..199
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:O15498"
FT                   /id="PRO_0000370847"
FT   DOMAIN          7..131
FT                   /note="Longin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT   DOMAIN          139..199
FT                   /note="v-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT   MOD_RES         196
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:O15498"
FT   LIPID           195
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O15498"
FT   LIPID           196
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:O15498"
SQ   SEQUENCE   199 AA;  22909 MW;  3A031F8088FA5582 CRC64;
     MKITALLVLK CDPETREPVI LANVSDLSQF GKFSFYRSNF EEFIVFIART VARRTPPGQR
     QSVKHEEYKV HAYNINGLCA VGFMDDHYPV RSAFSLLNQV LDVYQKDYGD TWRFENSSQP
     WPYLKEASDK FRDPAEADKL LKIQRELDET KIILHKTIDG VLARGEKLDS LVEKSSELSL
     ASKMFYKQAK KTNSCCTLL
 
 
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