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Y1421_ARATH
ID   Y1421_ARATH             Reviewed;         587 AA.
AC   Q9SH71;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Putative inactive receptor-like protein kinase At1g64210;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g64210; ORFNames=F22C12.3;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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).
CC   -!- INTERACTION:
CC       Q9SH71; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-20651385, EBI-16954682;
CC       Q9SH71; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-20651385, EBI-20651385;
CC       Q9SH71; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-20651385, EBI-20651541;
CC       Q9SH71; C0LGK9: At2g24230; NbExp=2; IntAct=EBI-20651385, EBI-16965118;
CC       Q9SH71; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-20651385, EBI-20654480;
CC       Q9SH71; C0LGT1: At5g10290; NbExp=2; IntAct=EBI-20651385, EBI-16954266;
CC       Q9SH71; Q9LT96: At5g49770; NbExp=2; IntAct=EBI-20651385, EBI-17123993;
CC       Q9SH71; Q9SYQ8: CLV1; NbExp=2; IntAct=EBI-20651385, EBI-1646111;
CC       Q9SH71; Q9LYN8: EMS1; NbExp=2; IntAct=EBI-20651385, EBI-1640748;
CC       Q9SH71; Q9SN97: F18L15.140; NbExp=2; IntAct=EBI-20651385, EBI-20655031;
CC       Q9SH71; Q8GX94: LRR-RLK; NbExp=2; IntAct=EBI-20651385, EBI-16955556;
CC       Q9SH71; Q8GY50: LRR-RLK; NbExp=2; IntAct=EBI-20651385, EBI-20658163;
CC       Q9SH71; Q9M0D8: LRR-RLK; NbExp=2; IntAct=EBI-20651385, EBI-16955231;
CC       Q9SH71; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-20651385, EBI-17121474;
CC       Q9SH71; Q9ZVR7: PSKR1; NbExp=2; IntAct=EBI-20651385, EBI-16172949;
CC       Q9SH71; Q9FN37: PSKR2; NbExp=2; IntAct=EBI-20651385, EBI-16902047;
CC       Q9SH71; Q9FRS6: PXL1; NbExp=2; IntAct=EBI-20651385, EBI-16946268;
CC       Q9SH71; Q9SKB2: SOBIR1; NbExp=2; IntAct=EBI-20651385, EBI-16905883;
CC       Q9SH71; Q9SIT1: TMK3; NbExp=2; IntAct=EBI-20651385, EBI-16896864;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
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DR   EMBL; AC007764; AAF24582.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34210.1; -; Genomic_DNA.
DR   RefSeq; NP_176603.1; NM_105095.2.
DR   AlphaFoldDB; Q9SH71; -.
DR   SMR; Q9SH71; -.
DR   BioGRID; 27947; 62.
DR   IntAct; Q9SH71; 79.
DR   STRING; 3702.AT1G64210.1; -.
DR   PaxDb; Q9SH71; -.
DR   PRIDE; Q9SH71; -.
DR   EnsemblPlants; AT1G64210.1; AT1G64210.1; AT1G64210.
DR   GeneID; 842726; -.
DR   Gramene; AT1G64210.1; AT1G64210.1; AT1G64210.
DR   KEGG; ath:AT1G64210; -.
DR   Araport; AT1G64210; -.
DR   TAIR; locus:2024517; AT1G64210.
DR   eggNOG; ENOG502QTFK; Eukaryota.
DR   HOGENOM; CLU_000288_92_6_1; -.
DR   InParanoid; Q9SH71; -.
DR   OMA; CYGCIGD; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; Q9SH71; -.
DR   PRO; PR:Q9SH71; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SH71; baseline and differential.
DR   Genevisible; Q9SH71; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; -; 1.
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; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..587
FT                   /note="Putative inactive receptor-like protein kinase
FT                   At1g64210"
FT                   /id="PRO_0000401351"
FT   TOPO_DOM        20..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..587
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          89..112
FT                   /note="LRR 1"
FT   REPEAT          113..136
FT                   /note="LRR 2"
FT   REPEAT          137..160
FT                   /note="LRR 3"
FT   REPEAT          161..183
FT                   /note="LRR 4"
FT   REPEAT          184..205
FT                   /note="LRR 5"
FT   DOMAIN          307..581
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         313..321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         462
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         463
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         466
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         477
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   587 AA;  65331 MW;  A220304E519D6F46 CRC64;
     MQIFLFFFSL ILCFVLISSQ TLEDDKKALL HFLSSFNSSR LHWNQSSDVC HSWTGVTCNE
     NGDRIVSVRL PAVGFNGLIP PFTISRLSSL KFLSLRKNHF TGDFPSDFTN LKSLTHLYLQ
     HNHLSGPLLA IFSELKNLKV LDLSNNGFNG SIPTSLSGLT SLQVLNLANN SFSGEIPNLH
     LPKLSQINLS NNKLIGTIPK SLQRFQSSAF SGNNLTERKK QRKTPFGLSQ LAFLLILSAA
     CVLCVSGLSF IMITCFGKTR ISGKLRKRDS SSPPGNWTSR DDNTEEGGKI IFFGGRNHLF
     DLDDLLSSSA EVLGKGAFGT TYKVTMEDMS TVVVKRLKEV VVGRREFEQQ MEIIGMIRHE
     NVAELKAYYY SKDDKLAVYS YYNHGSLFEI LHGNRGRYHR VPLDWDARLR IATGAARGLA
     KIHEGKFIHG NIKSSNIFLD SQCYGCIGDV GLTTIMRSLP QTTCLTSGYH APEITDTRRS
     TQFSDVYSFG VVLLELLTGK SPVSQAELVP TGGENMDLAS WIRSVVAKEW TGEVFDMEIL
     SQSGGFEEEM VEMLQIGLAC VALKQQERPH IAQVLKLIED IRSVDAE
 
 
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