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Y2393_ARATH
ID   Y2393_ARATH             Reviewed;         815 AA.
AC   O80623;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Probable receptor-like protein kinase At2g39360;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g39360; ORFNames=F12L6.2;
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=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   [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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA   Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA   Barbier-Brygoo H., Ephritikhine G.;
RT   "A high content in lipid-modified peripheral proteins and integral receptor
RT   kinases features in the arabidopsis plasma membrane proteome.";
RL   Mol. Cell. Proteomics 6:1980-1996(2007).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=19529822; DOI=10.1093/mp/ssn083;
RA   Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT   "Diverse transcriptional programs associated with environmental stress and
RT   hormones in the Arabidopsis receptor-like kinase gene family.";
RL   Mol. Plant 2:84-107(2009).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812};
CC       Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}.
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; AC004218; AAC27827.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09665.1; -; Genomic_DNA.
DR   EMBL; AF325084; AAK17152.1; -; mRNA.
DR   PIR; T00546; T00546.
DR   RefSeq; NP_181468.1; NM_129493.3.
DR   AlphaFoldDB; O80623; -.
DR   SMR; O80623; -.
DR   BioGRID; 3859; 15.
DR   IntAct; O80623; 15.
DR   STRING; 3702.AT2G39360.1; -.
DR   iPTMnet; O80623; -.
DR   PaxDb; O80623; -.
DR   PRIDE; O80623; -.
DR   ProteomicsDB; 243146; -.
DR   EnsemblPlants; AT2G39360.1; AT2G39360.1; AT2G39360.
DR   GeneID; 818521; -.
DR   Gramene; AT2G39360.1; AT2G39360.1; AT2G39360.
DR   KEGG; ath:AT2G39360; -.
DR   Araport; AT2G39360; -.
DR   TAIR; locus:2039717; AT2G39360.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_000288_42_2_1; -.
DR   InParanoid; O80623; -.
DR   OMA; LVEWAMK; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; O80623; -.
DR   PRO; PR:O80623; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80623; baseline and differential.
DR   Genevisible; O80623; AT.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR   InterPro; IPR045272; ANXUR1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR27003; PTHR27003; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Signal; Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..815
FT                   /note="Probable receptor-like protein kinase At2g39360"
FT                   /id="PRO_0000386554"
FT   TOPO_DOM        27..407
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..815
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          487..761
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        612
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         493..501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        355
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   815 AA;  91321 MW;  D3F4E07B73D8342D CRC64;
     MINLKLFLEL KLCFLITLLC SSHISSVSDT FFINCGSPTN VTVNNRTFVS DNNLVQGFSV
     GTTDSNSGDE STLFQTARVF SDESSSTYRF PIEEHGWFLI RIYFLPLVSA SQDLTTARFS
     VSAQNFTLIR EYKPSTTSVV REYILNVTTD SLLLQFLPRT GSVSFINALE VLRLPETLIP
     EDAKLIGTQK DLKLSSHAME TVSRVNMGNL SVSRDQDKLW RQWDSDSAYK AHFGTPVMNL
     KAVNFSAGGI TDDIAPVYVY GTATRLNSDL DPNTNANLTW TFKVEPGFDY FVRFHFCNII
     VDPFGFERQI RFDIFVNSEK VRTIDMTEVL NGTFGAPFFV DAVMRKAKSR EGFLNLSIGL
     VMDVSSYPVS FINGFEISKL SNDKRSLDAF DAILPDGSSS NKSSNTSVGL IAGLSAALCV
     ALVFGVVVSW WCIRKRRRRN RQMQTVHSRG DDHQIKKNET GESLIFSSSK IGYRYPLALI
     KEATDDFDES LVIGVGGFGK VYKGVLRDKT EVAVKRGAPQ SRQGLAEFKT EVEMLTQFRH
     RHLVSLIGYC DENSEMIIVY EYMEKGTLKD HLYDLDDKPR LSWRQRLEIC VGAARGLHYL
     HTGSTRAIIH RDVKSANILL DDNFMAKVAD FGLSKTGPDL DQTHVSTAVK GSFGYLDPEY
     LTRQQLTEKS DVYSFGVVML EVVCGRPVID PSLPREKVNL IEWAMKLVKK GKLEDIIDPF
     LVGKVKLEEV KKYCEVTEKC LSQNGIERPA MGDLLWNLEF MLQVQAKDEK AAMVDDKPEA
     SVVGSTMQFS VNGVGDIAGV SMSKVFAQMV REETR
 
 
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