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Database: UniProt
Entry: O64778
LinkDB: O64778
Original site: O64778 
ID   Y1142_ARATH             Reviewed;         807 AA.
AC   O64778;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   01-OCT-2014, entry version 108.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g61420;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g61420; ORFNames=T1F9.9;
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;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
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   -!- SIMILARITY: Contains 1 bulb-type lectin domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00038}.
CC   -!- SIMILARITY: Contains 1 EGF-like domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PAN domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00315}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC13899.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
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DR   EMBL; AC004255; AAC13899.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33836.1; -; Genomic_DNA.
DR   RefSeq; NP_176337.1; NM_104823.3.
DR   UniGene; At.36455; -.
DR   UniGene; At.70863; -.
DR   ProteinModelPortal; O64778; -.
DR   SMR; O64778; 89-143, 459-807.
DR   PRIDE; O64778; -.
DR   EnsemblPlants; AT1G61420.1; AT1G61420.1; AT1G61420.
DR   GeneID; 842436; -.
DR   KEGG; ath:AT1G61420; -.
DR   GeneFarm; 55; 3.
DR   TAIR; AT1G61420; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000116559; -.
DR   InParanoid; O64778; -.
DR   OMA; YLHRDSH; -.
DR   PhylomeDB; O64778; -.
DR   BioCyc; ARA:AT1G61420-MONOMER; -.
DR   ArrayExpress; O64778; -.
DR   Genevestigator; O64778; -.
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:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR013227; PAN-2_domain.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR000858; S_locus_glycoprot.
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; PF11883; DUF3403; 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   SUPFAM; SSF51110; SSF51110; 2.
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   3: Inferred from homology;
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     24       {ECO:0000255}.
FT   CHAIN        25    807       G-type lectin S-receptor-like
FT                                serine/threonine-protein kinase
FT                                At1g61420.
FT                                /FTId=PRO_0000401321.
FT   TOPO_DOM     25    426       Extracellular. {ECO:0000255}.
FT   TRANSMEM    427    447       Helical. {ECO:0000255}.
FT   TOPO_DOM    448    807       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       25    144       Bulb-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00038}.
FT   DOMAIN      278    314       EGF-like; atypical.
FT   DOMAIN      333    413       PAN. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00315}.
FT   DOMAIN      494    779       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     500    508       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      583    600       CaM-binding. {ECO:0000250}.
FT   ACT_SITE    619    619       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     522    522       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     623    623       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     636    636       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     653    653       Phosphothreonine. {ECO:0000250}.
FT   CARBOHYD     53     53       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    117    117       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    134    134       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    236    236       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    267    267       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    320    320       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    336    336       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    375    375       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    282    294       {ECO:0000250}.
FT   DISULFID    288    302       {ECO:0000250}.
FT   DISULFID    368    389       {ECO:0000250}.
FT   DISULFID    372    378       {ECO:0000250}.
SQ   SEQUENCE   807 AA;  90406 MW;  6D78921EA0E891FB CRC64;
     MGKKWIVFFA YLLLSSFFIS SSSAGITKES PLPIGQTLSS SNGFYELGFF NFNNSQNQYV
     GIWFKGIIPR VVVWVANREK PVTDSTANLA ISNNGSLLLF NGKHGVAWSS GEALVSNGSR
     AELSDTGNLI VIDNFSGRTL WQSFDHLGDT MLPSSTLKYN LATGEKQVLS SWKSYTDPSV
     GDFVLQITPQ VPTQVLVTKG STPYYRSGPW AKTRFTGIPL MDDTFTGPVS VQQDTNGSGS
     LTYLNRNDRL QRTMLTSKGT QELSWHNGTD WVLNFVAPEH SCDYYGVCGP FGLCVKSVPP
     KCTCFKGFVP KLIEEWKRGN WTGGCVRRTE LYCQGNSTGK YANVFHPVAR IKPPDFYEFA
     SFVNVEECQK SCLHNCSCLA FAYIDGIGCL MWNQDLMDAV QFSEGGELLS IRLARSELGG
     NKRKKAITAS IVSLSLVVII AFVAFCFWRY RVKHNADITT DASQVSWRND LKPQDVPGLD
     FFDMHTIQTA TNNFSISNKL GQGGFGPVYK GKLQDGKEIA VKRLSSSSGQ GKEEFMNEIV
     LISKLQHKNL VRILGCCIEG EEKLLIYEFM LNNSLDTFLF DSRKRLEIDW PKRLDIIQGI
     ARGIHYLHRD SHLKVIHRDL KVSNILLDEK MNPKISDFGL ARMYQGTEYQ DNTRRVVGTL
     GYMAPEYAWT GMFSEKSDIY SFGVLMLEII SGEKISRFSY GKEEKTLIAY AWESWCDTGG
     IDLLDKDVAD SCRPLEVERC VQIGLLCVQH QPADRPNTLE LLSMLTTTSD LPPPEQPTFV
     VHRRDDKSSS EDLITVNEMT KSVILGR
//
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