GenomeNet

Database: UniProt
Entry: Q9LMN7
LinkDB: Q9LMN7
Original site: Q9LMN7 
ID   WAK5_ARATH              Reviewed;         733 AA.
AC   Q9LMN7;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   13-FEB-2019, entry version 131.
DE   RecName: Full=Wall-associated receptor kinase 5;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAK5; OrderedLocusNames=At1g21230; ORFNames=F16F4.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=10380805; DOI=10.1023/A:1006197318246;
RA   He Z.-H., Cheeseman I., He D., Kohorn B.D.;
RT   "A cluster of five cell wall-associated receptor kinase genes, Wak1-5,
RT   are expressed in specific organs of Arabidopsis.";
RL   Plant Mol. Biol. 39:1189-1196(1999).
RN   [4]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=12068092; DOI=10.1104/pp.011028;
RA   Verica J.A., He Z.-H.;
RT   "The cell wall-associated kinase (WAK) and WAK-like kinase gene
RT   family.";
RL   Plant Physiol. 129:455-459(2002).
CC   -!- FUNCTION: Serine/threonine-protein kinase that may function as a
CC       signaling receptor of extracellular matrix component. Binding to
CC       pectin may have significance in the control of cell expansion,
CC       morphogenesis and development.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in green tissues such
CC       as stems and leaves. {ECO:0000269|PubMed:10380805}.
CC   -!- INDUCTION: Induced by INA. {ECO:0000269|PubMed:10380805}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; AC036104; AAF81359.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30076.1; -; Genomic_DNA.
DR   PIR; E86345; E86345.
DR   RefSeq; NP_173546.1; NM_101976.2.
DR   ProteinModelPortal; Q9LMN7; -.
DR   SMR; Q9LMN7; -.
DR   BioGrid; 23957; 1.
DR   IntAct; Q9LMN7; 1.
DR   STRING; 3702.AT1G21230.1; -.
DR   PaxDb; Q9LMN7; -.
DR   PRIDE; Q9LMN7; -.
DR   EnsemblPlants; AT1G21230.1; AT1G21230.1; AT1G21230.
DR   GeneID; 838718; -.
DR   Gramene; AT1G21230.1; AT1G21230.1; AT1G21230.
DR   KEGG; ath:AT1G21230; -.
DR   Araport; AT1G21230; -.
DR   TAIR; locus:2014962; AT1G21230.
DR   eggNOG; ENOG410IM0I; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116550; -.
DR   InParanoid; Q9LMN7; -.
DR   OMA; SANICGW; -.
DR   OrthoDB; 496739at2759; -.
DR   PhylomeDB; Q9LMN7; -.
DR   PRO; PR:Q9LMN7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q9LMN7; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR025287; WAK_GUB.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    733       Wall-associated receptor kinase 5.
FT                                /FTId=PRO_0000253304.
FT   TOPO_DOM     24    330       Extracellular. {ECO:0000255}.
FT   TRANSMEM    331    351       Helical. {ECO:0000255}.
FT   TOPO_DOM    352    733       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      231    278       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      279    321       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      408    691       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     414    422       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS    149    152       Poly-Pro.
FT   ACT_SITE    533    533       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     436    436       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     397    397       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     481    481       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     567    567       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     572    572       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     580    580       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   CARBOHYD     57     57       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     77     77       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    110    110       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    137    137       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    184    184       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    206    206       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    218    218       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    232    232       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    247    247       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    289    289       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    314    314       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    235    250       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    244    261       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    263    277       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    283    296       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    290    305       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    307    320       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   733 AA;  82206 MW;  8040BFC89D3D39A7 CRC64;
     MKVHSLFLMA IFFYLAYTQL VKAQPRDDCQ TRCGDVPIDY PFGISTGCYY PGDDSFNITC
     EEDKPNVLSN IEVLNFNHSG QLRGLIPRST VCYDQQTNND FESLWFRLDN LSFSPNNKFT
     LVGCNAWALL STFGIQNYST GCMSLCDTPP PPNSKCNGVG CCRTEVSIPL DSHRIETQPS
     RFENMTSVEH FNPCSYAFFV EDGMFNFSSL EDLKDLRNVT RFPVLLDWSI GNQTCEQVVG
     RNICGGNSTC FDSTRGKGYN CKCLQGFDGN PYLSDGCQDI NECTTRIHNC SDTSTCENTL
     GSFHCQCPSG SDLNTTTMSC IDTPKEEPKY LGWTTVLLGT TIGFLIILLT ISYIQQKMRH
     RKNTELRQQF FEQNGGGMLI QRLSGAGPSN VDVKIFTEEG MKEATDGYNE SRILGQGGQG
     TVYKGILQDN SIVAIKKARL GDRSQVEQFI NEVLVLSQIN HRNVVKLLGC CLETEVPLLV
     YEFISSGTLF DHLHGSMFDS SLTWEHRLRI AIEVAGTLAY LHSYASIPII HRDVKTANIL
     LDENLTAKVA DFGASRLIPM DQEQLTTMVQ GTLGYLDPEY YNTGLLNEKS DVYSFGVVLM
     ELLSGEKALC FERPQSSKHL VSYFVSAMKE NRLHEIIDGQ VMNEYNQREI QESARIAVEC
     TRIMGEERPS MKEVAAELEA LRVKTTKHQW SDQYPKEVEH LLGVQILSTQ GDTSSIGYDS
     IQNVTRLDIE TGR
//
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