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YKT61_ARATH
ID   YKT61_ARATH             Reviewed;         199 AA.
AC   Q9ZRD6;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=VAMP-like protein YKT61 {ECO:0000303|PubMed:15919093};
DE            Short=AtYKT61 {ECO:0000303|PubMed:15919093};
DE   AltName: Full=Geranylgeranylated protein 1 {ECO:0000303|Ref.1};
DE            Short=AtGP1 {ECO:0000303|Ref.1};
DE   Flags: Precursor;
GN   Name=YKT61 {ECO:0000303|PubMed:15919093};
GN   OrderedLocusNames=At5g58060 {ECO:0000312|Araport:AT5G58060};
GN   ORFNames=K21L19.5 {ECO:0000312|EMBL:BAB10997.1},
GN   K21L19_40 {ECO:0000312|EMBL:BAB10997.1};
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.
RA   Biermann B.J., Price J.R., Crowell D.N., Randall S.K.;
RT   "A collection of cDNAs encoding isoprenylated plant proteins.";
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15342965; DOI=10.1247/csf.29.49;
RA   Uemura T., Ueda T., Ohniwa R.L., Nakano A., Takeyasu K., Sato M.H.;
RT   "Systematic analysis of SNARE molecules in Arabidopsis: dissection of the
RT   post-Golgi network in plant cells.";
RL   Cell Struct. Funct. 29:49-65(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH SYP41, SUBUNIT, AND TISSUE SPECIFICITY.
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).
CC   -!- FUNCTION: May be involved in the secretory pathway (By similarity).
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). {ECO:0000250|UniProtKB:O15498,
CC       ECO:0000269|PubMed:15919093}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9ZRD6-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in roots, stems, flowers and
CC       leaves. {ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:15919093}.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR   EMBL; U64918; AAD00112.1; -; mRNA.
DR   EMBL; AB024029; BAB10997.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96992.1; -; Genomic_DNA.
DR   EMBL; AF325040; AAG40392.1; -; mRNA.
DR   EMBL; AF385703; AAK60295.1; -; mRNA.
DR   EMBL; AY133669; AAM91499.1; -; mRNA.
DR   RefSeq; NP_200614.1; NM_125191.4. [Q9ZRD6-1]
DR   AlphaFoldDB; Q9ZRD6; -.
DR   SMR; Q9ZRD6; -.
DR   BioGRID; 21162; 9.
DR   IntAct; Q9ZRD6; 6.
DR   iPTMnet; Q9ZRD6; -.
DR   PRIDE; Q9ZRD6; -.
DR   ProteomicsDB; 242336; -. [Q9ZRD6-1]
DR   EnsemblPlants; AT5G58060.1; AT5G58060.1; AT5G58060. [Q9ZRD6-1]
DR   GeneID; 835918; -.
DR   Gramene; AT5G58060.1; AT5G58060.1; AT5G58060. [Q9ZRD6-1]
DR   KEGG; ath:AT5G58060; -.
DR   Araport; AT5G58060; -.
DR   HOGENOM; CLU_074848_2_0_1; -.
DR   InParanoid; Q9ZRD6; -.
DR   OMA; ITDHEYP; -.
DR   PhylomeDB; Q9ZRD6; -.
DR   PRO; PR:Q9ZRD6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9ZRD6; baseline and differential.
DR   Genevisible; Q9ZRD6; 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   Alternative splicing; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Palmitate; Prenylation; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..196
FT                   /note="VAMP-like protein YKT61"
FT                   /id="PRO_0000206748"
FT   PROPEP          197..199
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:O15498"
FT                   /id="PRO_0000370846"
FT   DOMAIN          7..133
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;  22544 MW;  19642F929F3F2CCB CRC64;
     MKITALLVLK CAPEASDPVI LSNASDVSHF GYFQRSSVKE FVVFVGRTVA SRTPPSQRQS
     VQHEEYKVHA YNRNGLCAVG FMDDHYPVRS AFSLLNQVLD EYQKSFGESW RSAKEDSNQP
     WPYLTEALNK FQDPAEADKL LKIQRELDET KIILHKTIDS VLARGEKLDS LVEKSSDLSM
     ASQMFYKQAK KTNSCCTIL
 
 
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