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Y5815_ARATH
ID   Y5815_ARATH             Reviewed;         785 AA.
AC   Q9LVN2;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Probably inactive leucine-rich repeat receptor-like protein kinase At5g58150;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g58150; ORFNames=MCK7.2;
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   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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA   Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT   "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT   like protein kinase genes in Arabidopsis thaliana.";
RL   BMC Genomics 11:19-19(2010).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. La-0;
RX   PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT   immobilized metal ion affinity chromatography and mass spectrometry.";
RL   Mol. Cell. Proteomics 2:1234-1243(2003).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:14506206}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. Lacks the conserved Asp active site at position 645, which is
CC       replaced by a Glu residue.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AB019228; BAA96906.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97005.1; -; Genomic_DNA.
DR   EMBL; AY091097; AAM14048.1; -; mRNA.
DR   EMBL; AY123035; AAM67568.1; -; mRNA.
DR   EMBL; FJ708804; ACN59395.1; -; mRNA.
DR   RefSeq; NP_200623.1; NM_125200.2.
DR   AlphaFoldDB; Q9LVN2; -.
DR   SMR; Q9LVN2; -.
DR   BioGRID; 21171; 17.
DR   IntAct; Q9LVN2; 17.
DR   STRING; 3702.AT5G58150.1; -.
DR   iPTMnet; Q9LVN2; -.
DR   PaxDb; Q9LVN2; -.
DR   PRIDE; Q9LVN2; -.
DR   ProteomicsDB; 242935; -.
DR   EnsemblPlants; AT5G58150.1; AT5G58150.1; AT5G58150.
DR   GeneID; 835927; -.
DR   Gramene; AT5G58150.1; AT5G58150.1; AT5G58150.
DR   KEGG; ath:AT5G58150; -.
DR   Araport; AT5G58150; -.
DR   TAIR; locus:2161303; AT5G58150.
DR   eggNOG; ENOG502QTEF; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; Q9LVN2; -.
DR   OMA; SAHKLGH; -.
DR   OrthoDB; 136642at2759; -.
DR   PhylomeDB; Q9LVN2; -.
DR   PRO; PR:Q9LVN2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LVN2; differential.
DR   Genevisible; Q9LVN2; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 4.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 11.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..785
FT                   /note="Probably inactive leucine-rich repeat receptor-like
FT                   protein kinase At5g58150"
FT                   /id="PRO_0000389467"
FT   TOPO_DOM        22..436
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        437..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        458..785
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          64..88
FT                   /note="LRR 1"
FT   REPEAT          89..112
FT                   /note="LRR 2"
FT   REPEAT          114..136
FT                   /note="LRR 3"
FT   REPEAT          138..160
FT                   /note="LRR 4"
FT   REPEAT          161..184
FT                   /note="LRR 5"
FT   REPEAT          186..208
FT                   /note="LRR 6"
FT   REPEAT          210..232
FT                   /note="LRR 7"
FT   REPEAT          236..258
FT                   /note="LRR 8"
FT   REPEAT          259..283
FT                   /note="LRR 9"
FT   REPEAT          284..306
FT                   /note="LRR 10"
FT   REPEAT          307..330
FT                   /note="LRR 11"
FT   REPEAT          331..355
FT                   /note="LRR 12"
FT   REPEAT          357..377
FT                   /note="LRR 13"
FT   REPEAT          379..405
FT                   /note="LRR 14"
FT   DOMAIN          521..785
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         527..535
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         510
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         518
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         594
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O22476"
FT   MOD_RES         683
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   785 AA;  86611 MW;  3328A3586E0E3E5E CRC64;
     MRLSLWGSLL FFSFFVKHLT SLDPNTDAYH LSSFFSAMRL PNSPQAHTFS SLCSWPGVVV
     CDSSENVLHI SASGLDLSGS IPDNTIGKMS KLQTLDLSGN KITSLPSDLW SLSLLESLNL
     SSNRISEPLP SNIGNFMSLH TLDLSFNSIS GKIPAAISNL VNLTTLKLHN NDFQFGVPPE
     LVHCRSLLSI DLSSNRLNES LPVGFGSAFP LLKSLNLSRN LFQGSLIGVL HENVETVDLS
     ENRFDGHILQ LIPGHKHNWS SLIHLDLSDN SFVGHIFNGL SSAHKLGHLN LACNRFRAQE
     FPEIGKLSAL HYLNLSRTNL TNIIPREISR LSHLKVLDLS SNNLTGHVPM LSVKNIEVLD
     LSLNKLDGDI PRPLLEKLAM MQRFNFSFNN LTFCNPNFSQ ETIQRSFINI RNNCPFAAKP
     IITKGKKVNK KNTGLKIGLG LAISMAFLLI GLLLILVALR VRRKSRTWAT KLAINNTEPN
     SPDQHDSTTD IKQATQIPVV MIDKPLMKMT LADLKAATFN FDRGTMLWEG KSGPTYGAVL
     PGGFRAALKV IPSGTTLTDT EVSIAFERLA RINHPNLFPL CGYCIATEQR IAIYEDLDMV
     NLQSLLHNNG DDSAPWRLRH KIALGTARAL AFLHHGCIPP MVHGEVKAAT ILLDSSQEPR
     LADFGLVKLL DEQFPGSESL DGYTPPEQER NASPTLESDV YSFGVVLLEL VSGKKPEGDL
     VNWVRGLVRQ GQGLRAIDPT MQETVPEDEI AEAVKIGYLC TADLPWKRPT MQQVVGLLKD
     ISPNY
 
 
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