GenomeNet

Database: UniProt
Entry: O81906
LinkDB: O81906
Original site: O81906 
ID   B120_ARATH              Reviewed;         849 AA.
AC   O81906; Q0WPA4; Q9SVK2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JAN-2019, entry version 148.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase B120;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   Name=B120; OrderedLocusNames=At4g21390; ORFNames=F18E5.10, T6K22.120;
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].
RC   STRAIN=cv. Cvi-0;
RX   PubMed=17656687; DOI=10.1126/science.1143153;
RA   Tang C., Toomajian C., Sherman-Broyles S., Plagnol V., Guo Y.-L.,
RA   Hu T.T., Clark R.M., Nasrallah J.B., Weigel D., Nordborg M.;
RT   "The evolution of selfing in Arabidopsis thaliana.";
RL   Science 317:1070-1072(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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         EC=2.7.11.1;
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         EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
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; EF637083; ABV21215.1; -; Genomic_DNA.
DR   EMBL; AL022603; CAA18703.1; -; Genomic_DNA.
DR   EMBL; AL031187; CAA20204.1; -; Genomic_DNA.
DR   EMBL; AL161555; CAB81246.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84447.1; -; Genomic_DNA.
DR   EMBL; AK229175; BAF01045.1; -; mRNA.
DR   PIR; T05181; T05181.
DR   RefSeq; NP_193870.1; NM_118259.4.
DR   UniGene; At.32633; -.
DR   ProteinModelPortal; O81906; -.
DR   SMR; O81906; -.
DR   BioGrid; 13182; 3.
DR   IntAct; O81906; 3.
DR   STRING; 3702.AT4G21390.1; -.
DR   PaxDb; O81906; -.
DR   PRIDE; O81906; -.
DR   EnsemblPlants; AT4G21390.1; AT4G21390.1; AT4G21390.
DR   GeneID; 827891; -.
DR   Gramene; AT4G21390.1; AT4G21390.1; AT4G21390.
DR   KEGG; ath:AT4G21390; -.
DR   Araport; AT4G21390; -.
DR   TAIR; locus:2141176; AT4G21390.
DR   eggNOG; ENOG410IE3D; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116559; -.
DR   InParanoid; O81906; -.
DR   OMA; IAGYAWR; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; O81906; -.
DR   PRO; PR:O81906; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O81906; baseline and differential.
DR   Genevisible; O81906; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00473; PAN_AP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Kinase; Lectin; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    849       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase B120.
FT                                /FTId=PRO_0000401297.
FT   TOPO_DOM     26    438       Extracellular. {ECO:0000255}.
FT   TRANSMEM    439    459       Helical. {ECO:0000255}.
FT   TOPO_DOM    460    849       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       26    153       Bulb-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      295    332       EGF-like; atypical.
FT   DOMAIN      346    427       PAN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      529    814       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     535    543       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      618    635       CaM-binding. {ECO:0000250}.
FT   ACT_SITE    654    654       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     557    557       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     563    563       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     658    658       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     671    671       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     688    688       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     732    732       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     837    837       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   MOD_RES     844    844       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9LPZ9}.
FT   CARBOHYD    110    110       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    191    191       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    210    210       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    230    230       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    273    273       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    282    282       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    349    349       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    388    388       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    299    311       {ECO:0000250}.
FT   DISULFID    305    320       {ECO:0000250}.
FT   DISULFID    381    402       {ECO:0000250}.
FT   DISULFID    385    391       {ECO:0000250}.
FT   CONFLICT    795    795       V -> A (in Ref. 4; BAF01045).
FT                                {ECO:0000305}.
SQ   SEQUENCE   849 AA;  95168 MW;  03FEB8CF57FD6F67 CRC64;
     MRFFRKTSLY LSLFLYFFLY ESSMAANTIR RGESLRDGIN HKPLVSPQKT FELGFFSPGS
     STHRFLGIWY GNIEDKAVVW VANRATPISD QSGVLMISND GNLVLLDGKN ITVWSSNIES
     STTNNNNRVV SIHDTGNFVL SETDTDRPIW ESFNHPTDTF LPQMRVRVNP QTGDNHAFVS
     WRSETDPSPG NYSLGVDPSG APEIVLWEGN KTRKWRSGQW NSAIFTGIPN MSLLTNYLYG
     FKLSSPPDET GSVYFTYVPS DPSVLLRFKV LYNGTEEELR WNETLKKWTK FQSEPDSECD
     QYNRCGKFGI CDMKGSNGIC SCIHGYEQVS VGNWSRGCRR RTPLKCERNI SVGEDEFLTL
     KSVKLPDFEI PEHNLVDPED CRERCLRNCS CNAYSLVGGI GCMIWNQDLV DLQQFEAGGS
     SLHIRLADSE VGENRKTKIA VIVAVLVGVI LIGIFALLLW RFKRKKDVSG AYCGKNTDTS
     VVVADLTKSK ETTSAFSGSV DIMIEGKAVN TSELPVFSLN AIAIATNDFC KENELGRGGF
     GPVYKGVLED GREIAVKRLS GKSGQGVDEF KNEIILIAKL QHRNLVRLLG CCFEGEEKML
     VYEYMPNKSL DFFLFDETKQ ALIDWKLRFS IIEGIARGLL YLHRDSRLRI IHRDLKVSNV
     LLDAEMNPKI SDFGMARIFG GNQNEANTVR VVGTYGYMSP EYAMEGLFSV KSDVYSFGVL
     LLEIVSGKRN TSLRSSEHGS LIGYAWYLYT HGRSEELVDP KIRVTCSKRE ALRCIHVAML
     CVQDSAAERP NMASVLLMLE SDTATLAAPR QPTFTSTRRN SIDVNFALDS SQQYIVSSNE
     ITSTVVLGR
//
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