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Y1343_ARATH
ID   Y1343_ARATH             Reviewed;         829 AA.
AC   Q9XID3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=G-type lectin S-receptor-like serine/threonine-protein kinase At1g34300;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g34300; ORFNames=F23M19.5;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., 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., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 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).
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, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; 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: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; AC007454; AAD39605.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31694.1; -; Genomic_DNA.
DR   EMBL; AY090246; AAL90909.1; -; mRNA.
DR   EMBL; BT001084; AAN46865.1; -; mRNA.
DR   PIR; B86467; B86467.
DR   RefSeq; NP_174690.1; NM_103152.4.
DR   AlphaFoldDB; Q9XID3; -.
DR   SMR; Q9XID3; -.
DR   IntAct; Q9XID3; 2.
DR   STRING; 3702.AT1G34300.1; -.
DR   iPTMnet; Q9XID3; -.
DR   PaxDb; Q9XID3; -.
DR   PRIDE; Q9XID3; -.
DR   ProteomicsDB; 242417; -.
DR   EnsemblPlants; AT1G34300.1; AT1G34300.1; AT1G34300.
DR   GeneID; 840330; -.
DR   Gramene; AT1G34300.1; AT1G34300.1; AT1G34300.
DR   KEGG; ath:AT1G34300; -.
DR   Araport; AT1G34300; -.
DR   TAIR; locus:2026155; AT1G34300.
DR   eggNOG; ENOG502QRWA; Eukaryota.
DR   HOGENOM; CLU_000288_116_2_1; -.
DR   InParanoid; Q9XID3; -.
DR   OMA; PWPTRFA; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q9XID3; -.
DR   PRO; PR:Q9XID3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XID3; baseline and differential.
DR   Genevisible; Q9XID3; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; HDA: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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:UniProt.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   Gene3D; 2.90.10.10; -; 2.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR045874; LRK10-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR27009; PTHR27009; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PIRSF; PIRSF000641; SRK; 1.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51110; SSF51110; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 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; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Kinase; Lectin; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..829
FT                   /note="G-type lectin S-receptor-like serine/threonine-
FT                   protein kinase At1g34300"
FT                   /id="PRO_0000401314"
FT   TOPO_DOM        26..421
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        443..829
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..140
FT                   /note="Bulb-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          143..260
FT                   /note="Bulb-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DOMAIN          264..301
FT                   /note="EGF-like"
FT   DOMAIN          317..399
FT                   /note="Apple"
FT   DOMAIN          484..759
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          572..589
FT                   /note="CaM-binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        608
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         490..498
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         512
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         532
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   MOD_RES         799
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPZ9"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        268..280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        274..289
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        317..399
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        350..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        354..360
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
SQ   SEQUENCE   829 AA;  91293 MW;  908A5438F177D197 CRC64;
     MAVKTPFLKL LPLLLLLLHF PFSFSTIPLG SVIYASGSNQ NWPSPNSTFS VSFVPSPSPN
     SFLAAVSFAG SVPIWSAGTV DSRGSLRLHT SGSLRLTNGS GTTVWDSKTD RLGVTSGSIE
     DTGEFILLNN RSVPVWSSFD NPTDTIVQSQ NFTAGKILRS GLYSFQLERS GNLTLRWNTS
     AIYWNHGLNS SFSSNLSSPR LSLQTNGVVS IFESNLLGGA EIVYSGDYGD SNTFRFLKLD
     DDGNLRIYSS ASRNSGPVNA HWSAVDQCLV YGYCGNFGIC SYNDTNPICS CPSRNFDFVD
     VNDRRKGCKR KVELSDCSGN TTMLDLVHTR LFTYEDDPNS ESFFAGSSPC RANCLSSVLC
     LASVSMSDGS GNCWQKHPGS FFTGYQWPSV PSTSYVKVCG PVVANTLERA TKGDDNNSKV
     HLWIVAVAVI AGLLGLVAVE IGLWWCCCRK NPRFGTLSSH YTLLEYASGA PVQFTYKELQ
     RCTKSFKEKL GAGGFGTVYR GVLTNRTVVA VKQLEGIEQG EKQFRMEVAT ISSTHHLNLV
     RLIGFCSQGR HRLLVYEFMR NGSLDNFLFT TDSAKFLTWE YRFNIALGTA KGITYLHEEC
     RDCIVHCDIK PENILVDDNF AAKVSDFGLA KLLNPKDNRY NMSSVRGTRG YLAPEWLANL
     PITSKSDVYS YGMVLLELVS GKRNFDVSEK TNHKKFSIWA YEEFEKGNTK AILDTRLSED
     QTVDMEQVMR MVKTSFWCIQ EQPLQRPTMG KVVQMLEGIT EIKNPLCPKT ISEVSFSGNS
     MSTSHASMFV ASGPTRSSSF SATRSFQTMG ITSSGPASTR ISEGSMLGS
 
 
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