GenomeNet

Database: UniProt
Entry: Q9LMN6
LinkDB: Q9LMN6
Original site: Q9LMN6 
ID   WAK4_ARATH              Reviewed;         738 AA.
AC   Q9LMN6; O81819;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   13-FEB-2019, entry version 132.
DE   RecName: Full=Wall-associated receptor kinase 4;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAK4; OrderedLocusNames=At1g21210; ORFNames=F16F4.10;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
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   [2]
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   [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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION.
RX   PubMed=11402163; DOI=10.1105/tpc.13.6.1317;
RA   Lally D., Ingmire P., Tong H.-Y., He Z.-H.;
RT   "Antisense expression of a cell wall-associated protein kinase, WAK4,
RT   inhibits cell elongation and alters morphology.";
RL   Plant Cell 13:1317-1331(2001).
RN   [5]
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. {ECO:0000269|PubMed:11402163}.
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: Strictly expressed in siliques.
CC       {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; AJ009695; CAA08793.1; -; Genomic_DNA.
DR   EMBL; AC036104; AAF81361.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30075.1; -; Genomic_DNA.
DR   PIR; D86345; D86345.
DR   RefSeq; NP_173544.1; NM_101974.3.
DR   ProteinModelPortal; Q9LMN6; -.
DR   SMR; Q9LMN6; -.
DR   BioGrid; 23955; 8.
DR   IntAct; Q9LMN6; 8.
DR   STRING; 3702.AT1G21210.1; -.
DR   PaxDb; Q9LMN6; -.
DR   PRIDE; Q9LMN6; -.
DR   EnsemblPlants; AT1G21210.1; AT1G21210.1; AT1G21210.
DR   GeneID; 838716; -.
DR   Gramene; AT1G21210.1; AT1G21210.1; AT1G21210.
DR   KEGG; ath:AT1G21210; -.
DR   Araport; AT1G21210; -.
DR   TAIR; locus:2014952; AT1G21210.
DR   eggNOG; ENOG410IM0I; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116550; -.
DR   InParanoid; Q9LMN6; -.
DR   OMA; PWANGHE; -.
DR   OrthoDB; 496739at2759; -.
DR   PhylomeDB; Q9LMN6; -.
DR   PRO; PR:Q9LMN6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q9LMN6; 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   GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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     22       {ECO:0000255}.
FT   CHAIN        23    738       Wall-associated receptor kinase 4.
FT                                /FTId=PRO_0000253303.
FT   TOPO_DOM     23    335       Extracellular. {ECO:0000255}.
FT   TRANSMEM    336    356       Helical. {ECO:0000255}.
FT   TOPO_DOM    357    738       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      232    278       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      279    325       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      410    693       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     416    424       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    535    535       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     438    438       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     399    399       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     483    483       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     569    569       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     574    574       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     582    582       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   CARBOHYD     34     34       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     56     56       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    109    109       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    115    115       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    132    132       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    182    182       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    208    208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    293    293       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    318    318       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    236    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    300       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    294    309       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    311    324       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   738 AA;  81704 MW;  3927EBC7C7F57267 CRC64;
     MKVQRLFLVA IFCLSYMQLV KGQTLPRCPE KCGNVTLEYP FGFSPGCWRA EDPSFNLSCV
     NENLFYKGLE VVEISHSSQL RVLYPASYIC YNSKGKFAKG TYYWSNLGNL TLSGNNTITA
     LGCNSYAFVS SNGTRRNSVG CISACDALSH EANGECNGEG CCQNPVPAGN NWLIVRSYRF
     DNDTSVQPIS EGQCIYAFLV ENGKFKYNAS DKYSYLQNRN VGFPVVLDWS IRGETCGQVG
     EKKCGVNGIC SNSASGIGYT CKCKGGFQGN PYLQNGCQDI NECTTANPIH KHNCSGDSTC
     ENKLGHFRCN CRSRYELNTT TNTCKPKGNP EYVEWTTIVL GTTIGFLVIL LAISCIEHKM
     KNTKDTELRQ QFFEQNGGGM LMQRLSGAGP SNVDVKIFTE EGMKEATDGY DENRILGQGG
     QGTVYKGILP DNSIVAIKKA RLGDNSQVEQ FINEVLVLSQ INHRNVVKLL GCCLETEVPL
     LVYEFISSGT LFDHLHGSMF DSSLTWEHRL RMAVEIAGTL AYLHSSASIP IIHRDIKTAN
     ILLDENLTAK VADFGASRLI PMDKEDLATM VQGTLGYLDP EYYNTGLLNE KSDVYSFGVV
     LMELLSGQKA LCFERPQTSK HIVSYFASAT KENRLHEIID GQVMNENNQR EIQKAARIAV
     ECTRLTGEER PGMKEVAAEL EALRVTKTKH KWSDEYPEQE DTEHLVGVQK LSAQGETSSS
     IGYDSIRNVA ILDIEAGR
//
DBGET integrated database retrieval system