Y2027_ARATH
ID Y2027_ARATH Reviewed; 489 AA.
AC Q9SIZ4; Q3EBJ0; Q9XEF4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Inactive receptor-like serine/threonine-protein kinase At2g40270;
DE Flags: Precursor;
GN OrderedLocusNames=At2g40270; ORFNames=T3G21, T7M7.19;
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 [GENOMIC DNA].
RX PubMed=10207155;
RA Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.;
RT "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07.";
RL Genome Res. 9:325-333(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIZ4-2; Sequence=VSP_040372;
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25942.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF085279; AAD25942.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC007020; AAD25662.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09805.1; -; Genomic_DNA.
DR EMBL; AY091778; AAM10326.1; -; mRNA.
DR EMBL; AY149959; AAN31113.1; -; mRNA.
DR EMBL; BX820203; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D84827; D84827.
DR RefSeq; NP_565925.1; NM_129585.5. [Q9SIZ4-1]
DR AlphaFoldDB; Q9SIZ4; -.
DR SMR; Q9SIZ4; -.
DR BioGRID; 3957; 5.
DR IntAct; Q9SIZ4; 5.
DR STRING; 3702.AT2G40270.1; -.
DR iPTMnet; Q9SIZ4; -.
DR PaxDb; Q9SIZ4; -.
DR PRIDE; Q9SIZ4; -.
DR ProteomicsDB; 242596; -. [Q9SIZ4-1]
DR EnsemblPlants; AT2G40270.1; AT2G40270.1; AT2G40270. [Q9SIZ4-1]
DR GeneID; 818619; -.
DR Gramene; AT2G40270.1; AT2G40270.1; AT2G40270. [Q9SIZ4-1]
DR KEGG; ath:AT2G40270; -.
DR Araport; AT2G40270; -.
DR TAIR; locus:2063146; AT2G40270.
DR eggNOG; KOG1187; Eukaryota.
DR InParanoid; Q9SIZ4; -.
DR OrthoDB; 454863at2759; -.
DR PhylomeDB; Q9SIZ4; -.
DR PRO; PR:Q9SIZ4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIZ4; baseline and differential.
DR Genevisible; Q9SIZ4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..489
FT /note="Inactive receptor-like serine/threonine-protein
FT kinase At2g40270"
FT /id="PRO_0000403349"
FT TOPO_DOM 24..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 200..460
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 67..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 52..59
FT /note="KAFGFHRK -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040372"
FT CONFLICT 77
FT /note="N -> S (in Ref. 5; BX820203)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="K -> E (in Ref. 5; BX820203)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="N -> D (in Ref. 5; BX820203)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="T -> A (in Ref. 5; BX820203)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="K -> R (in Ref. 5; BX820203)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="K -> E (in Ref. 5; BX820203)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="F -> L (in Ref. 5; BX820203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 54176 MW; 076C32C95EB9BC6E CRC64;
MLFKMRSFVA FVLLLSWFGS CCSLKDQAVD FLKSEDSLKK DLSSDEDSTY LKAFGFHRKT
LVRNPYKDLP SRKDRKNRVV AATTTPSSSP EPAPKHVSTK ASTVSEPQKR SSTQDVSPSP
SAPLANSPIP RNSHSSVPLV VGCVGGAFFL LLVATGLYFF TSKAGKTVNP WRTGLSGQLQ
KVFVTGIPVL KRSEIEAACE DFSNVIGSCP IGKLFKGTLS SGVEIAVASF ATTTAKDWKD
STEIHFRKKI EMLSKINHKN FANLLGYCEE KEPFTRILIF EYAPNGSLFE HLHYKESEHL
DWGMRLRIAM GLAYCLDHMH QLNPPIAHTN LVSSSLQLTE DYAVKVSDFS FGSSETETNI
NNNTVIDTHI SALNPEDNIY SFGLLLFEMI TGKLIESVNK PDSVDSSLVD FLRGETLAKM
VDPTLESYDA KIENIGEVIK SCLRTDPKER PTMQEVTGWL REITGLSPND ATPKLSPLWW
AELEVLSTA
