位置:首页 > 蛋白库 > BRI1_SOLPE
BRI1_SOLPE
ID   BRI1_SOLPE              Reviewed;        1207 AA.
AC   Q8L899;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Systemin receptor SR160;
DE            EC=2.7.11.1;
DE   AltName: Full=Brassinosteroid LRR receptor kinase;
DE   Flags: Precursor;
OS   Solanum peruvianum (Peruvian tomato) (Lycopersicon peruvianum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4082;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 301-311; 432-440; 548-554
RP   AND 862-874, GLYCOSYLATION, AND SUBSTRATE-BINDING.
RX   PubMed=12060717; DOI=10.1073/pnas.132266499;
RA   Scheer J.M., Ryan C.A. Jr.;
RT   "The systemin receptor SR160 from Lycopersicon peruvianum is a member of
RT   the LRR receptor kinase family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9585-9590(2002).
CC   -!- FUNCTION: Receptor with a serine/threonine-protein kinase activity.
CC       Involved in the perception of systemin, a peptide hormone responsible
CC       for the systemic activation of defense genes in leaves of wounded
CC       plants. May also regulate, in response to brassinosteroid binding, a
CC       signaling cascade involved in plant development (By similarity).
CC       {ECO:0000250}.
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; Single-pass type I membrane
CC       protein.
CC   -!- DOMAIN: A 68 amino acid island between the 20th and the 21th LRR is
CC       essential for the binding of brassinosteroids. {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:12060717}.
CC   -!- MISCELLANEOUS: SR160 is almost identical to BRI1, a brassinosteroid
CC       receptor identified in Lycopersicon esculentum. Competition experiments
CC       indicate that brassinosteroid and systemin are probably perceived by
CC       different regions of the receptor.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY112661; AAM48285.1; -; mRNA.
DR   AlphaFoldDB; Q8L899; -.
DR   SMR; Q8L899; -.
DR   PRIDE; Q8L899; -.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProt.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR045381; BRI1_island_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF20141; Island; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 20.
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; Direct protein sequencing; Glycoprotein;
KW   Kinase; Leucine-rich repeat; Lipid-binding; Membrane; Nucleotide-binding;
KW   Plant defense; Receptor; Repeat; Serine/threonine-protein kinase; Signal;
KW   Steroid-binding; Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..1207
FT                   /note="Systemin receptor SR160"
FT                   /id="PRO_0000024307"
FT   TRANSMEM        803..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          109..131
FT                   /note="LRR 1"
FT   REPEAT          135..157
FT                   /note="LRR 2"
FT   REPEAT          161..181
FT                   /note="LRR 3"
FT   REPEAT          186..207
FT                   /note="LRR 4"
FT   REPEAT          213..234
FT                   /note="LRR 5"
FT   REPEAT          235..257
FT                   /note="LRR 6"
FT   REPEAT          258..280
FT                   /note="LRR 7"
FT   REPEAT          282..304
FT                   /note="LRR 8"
FT   REPEAT          305..325
FT                   /note="LRR 9"
FT   REPEAT          329..350
FT                   /note="LRR 10"
FT   REPEAT          353..375
FT                   /note="LRR 11"
FT   REPEAT          378..401
FT                   /note="LRR 12"
FT   REPEAT          402..423
FT                   /note="LRR 13"
FT   REPEAT          428..450
FT                   /note="LRR 14"
FT   REPEAT          452..474
FT                   /note="LRR 15"
FT   REPEAT          476..499
FT                   /note="LRR 16"
FT   REPEAT          500..523
FT                   /note="LRR 17"
FT   REPEAT          524..547
FT                   /note="LRR 18"
FT   REPEAT          548..570
FT                   /note="LRR 19"
FT   REPEAT          572..594
FT                   /note="LRR 20"
FT   REPEAT          664..686
FT                   /note="LRR 21"
FT   REPEAT          688..711
FT                   /note="LRR 22"
FT   REPEAT          712..735
FT                   /note="LRR 23"
FT   REPEAT          736..758
FT                   /note="LRR 24"
FT   DOMAIN          888..1163
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOTIF           71..78
FT                   /note="Cys pair 1"
FT   MOTIF           771..779
FT                   /note="Cys pair 2"
FT   ACT_SITE        1014
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         894..902
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         916
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        363
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        646
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        662
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        724
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        746
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        767
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1207 AA;  131964 MW;  1422D1DFDA458073 CRC64;
     MKAHKTVFNQ HPLSLNKLFF VLLLIFFLPP ASPAASVNGL YKDSQQLLSF KAALPPTPTL
     LQNWLSSTDP CSFTGVSCKN SRVSSIDLSN TFLSVDFSLV TSYLLPLSNL ESLVLKNANL
     SGSLTSAAKS QCGVTLDSID LAENTISGPI SDISSFGVCS NLKSLNLSKN FLDPPGKEML
     KGATFSLQVL DLSYNNISGF NLFPWVSSMG FVELEFFSIK GNKLAGSIPE LDFKNLSYLD
     LSANNFSTVF PSFKDCSNLQ HLDLSSNKFY GDIGSSLSSC GKLSFLNLTN NQFVGLVPKL
     PSESLQYLYL RGNDFQGVYP NQLADLCKTV VELDLSYNNF SGMVPESLGE CSSLELVDIS
     NNNFSGKLPV DTLLKLSNIK TMVLSFNKFV GGLPDSFSNL PKLETLDMSS NNLTGIIPSG
     ICKDPMNNLK VLYLQNNLFK GPIPDSLSNC SQLVSLDLSF NYLTGSIPSS LGSLSKLKDL
     ILWLNQLSGE IPQELMYLQA LENLILDFND LTGPIPASLS NCTKLNWISL SNNQLSGEIP
     ASLGRLSNLA ILKLGNNSIS GNIPAELGNC QSLIWLDLNT NFLNGSIPPP LFKQSGNIAV
     ALLTGKRYVY IKNDGSKECH GAGNLLEFGG IRQEQLDRIS TRHPCNFTRV YRGITQPTFN
     HNGSMIFLDL SYNKLEGSIP KELGAMYYLS ILNLGHNDLS GMIPQQLGGL KNVAILDLSY
     NRFNGTIPNS LTSLTLLGEI DLSNNNLSGM IPESAPFDTF PDYRFANNSL CGYPLPLPCS
     SGPKSDANQH QKSHRRQASL AGSVAMGLLF SLFCIFGLII VAIETKKRRR KKEAALEAYM
     DGHSHSATAN SAWKFTSARE ALSINLAAFE KPLRKLTFAD LLEATNGFHN DSLVGSGGFG
     DVYKAQLKDG SVVAIKKLIH VSGQGDREFT AEMETIGKIK HRNLVPLLGY CKVGEERLLV
     YEYMKYGSLE DVLHDRKKTG IKLNWPARRK IAIGAARGLA FLHHNCIPHI IHRDMKSSNV
     LLDENLEARV SDFGMARLMS AMDTHLSVST LAGTPGYVPP EYYQSFRCST KGDVYSYGVV
     LLELLTGKQP TDSADFGDNN LVGWVKLHAK GKITDVFDRE LLKEDASIEI ELLQHLKVAC
     ACLDDRHWKR PTMIQVMAMF KEIQAGSGMD STSTIGADDV NFSGVEGGIE MGINGSIKEG
     NELSKHL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024