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Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM1 (EC 2.7.11.1) (Protein BARELY ANY MERISTEM 1)

 BAME1_ARATH             Reviewed;        1003 AA.
O49545;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
18-JUL-2018, entry version 156.
RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM1;
EC=2.7.11.1;
AltName: Full=Protein BARELY ANY MERISTEM 1;
Flags: Precursor;
Name=BAM1; OrderedLocusNames=At5g65700; ORFNames=F6H11.170, MPA24.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=20064227; DOI=10.1186/1471-2164-11-19;
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
"Genome-wide cloning and sequence analysis of leucine-rich repeat
receptor-like protein kinase genes in Arabidopsis thaliana.";
BMC Genomics 11:19-19(2010).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
SUBCELLULAR LOCATION.
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=16751349; DOI=10.1105/tpc.105.036871;
Hord C.L.H., Chen C., Deyoung B.J., Clark S.E., Ma H.;
"The BAM1/BAM2 receptor-like kinases are important regulators of
Arabidopsis early anther development.";
Plant Cell 18:1667-1680(2006).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=16367950; DOI=10.1111/j.1365-313X.2005.02592.x;
DeYoung B.J., Bickle K.L., Schrage K.J., Muskett P., Patel K.,
Clark S.E.;
"The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-like
proteins are required for meristem function in Arabidopsis.";
Plant J. 45:1-16(2006).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=18780746; DOI=10.1534/genetics.108.091108;
Deyoung B.J., Clark S.E.;
"BAM receptors regulate stem cell specification and organ development
through complex interactions with CLAVATA signaling.";
Genetics 180:895-904(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-996, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[12]
INTERACTION WITH MCLV3; CLE5; CLE11; CLE18; CLE19; CLE22; CLE25;
CLE26; CLE40; CLE41; CLE42; CLV1 AND BAM2, HOMODIMERIZATION, AND
SUBCELLULAR LOCATION.
PubMed=20626648; DOI=10.1111/j.1365-313X.2010.04295.x;
Guo Y., Han L., Hymes M., Denver R., Clark S.E.;
"CLAVATA2 forms a distinct CLE-binding receptor complex regulating
Arabidopsis stem cell specification.";
Plant J. 63:889-900(2010).
-!- FUNCTION: Necessary for male gametophyte development, as well as
ovule specification and function. Involved in cell-cell
communication process required during early anther development,
and regulating cell division and differentiation to organize cell
layers. Required for the development of high-ordered vascular
strands within the leaf and a correlated control of leaf shape,
size and symmetry. May regulate the CLV1-dependent CLV3-mediated
signaling in meristems maintenance. {ECO:0000269|PubMed:16367950,
ECO:0000269|PubMed:16751349, ECO:0000269|PubMed:18780746}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Self-interacts and interacts with BAM2 and CLV1. Binds to
the CLV3, CLE5, CLE11, CLE18, CLE19, CLE22, CLE25, CLE26, CLE40,
CLE41 and CLE42 mature peptides, probably via its extracellular
leucine-rich repeat region. {ECO:0000269|PubMed:20626648}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
ECO:0000269|PubMed:20626648}; Single-pass type I membrane protein
{ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:20626648}.
-!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves,
inflorescences, flowers and siliques.
{ECO:0000269|PubMed:16367950}.
-!- DEVELOPMENTAL STAGE: Expressed in a ring surrounding the center of
meristems extended in the cortex of developing stems and older
pedicels. Present in all developing floral organs, especially in
anthers and gynoecium. Observed in anthers at stage 2 in the
archesporial cells. At stage 3, localized in the primary
sporogenous and primary parietal cells. Subsequently
preferentially expressed in the sporogenous cells at anther stage
4. Later restricted to the tapetum and pollen mother cells (PMCs)
before disappearing progressively. {ECO:0000269|PubMed:16367950,
ECO:0000269|PubMed:16751349}.
-!- DISRUPTION PHENOTYPE: Rescues partially CLV3 disruption. When
associated with BAM2 disruption, abnormal anthers at a very early
stage and later lack of endothecium, middle and tapetum layers.
Loss of stem cells at the shoot and flower meristems.
{ECO:0000269|PubMed:16367950, ECO:0000269|PubMed:16751349,
ECO:0000269|PubMed:18780746}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
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EMBL; AB010075; BAB10677.1; -; Genomic_DNA.
EMBL; AL021684; CAA16688.1; -; Genomic_DNA.
EMBL; CP002688; AED98091.1; -; Genomic_DNA.
EMBL; CP002688; AED98092.1; -; Genomic_DNA.
EMBL; AY099814; AAM20665.1; -; mRNA.
EMBL; BT008810; AAP68249.1; -; mRNA.
EMBL; FJ708816; ACN59407.1; -; mRNA.
EMBL; AK226485; BAE98627.1; -; mRNA.
PIR; T05898; T05898.
RefSeq; NP_001190624.1; NM_001203695.1.
RefSeq; NP_201371.1; NM_125967.5.
UniGene; At.1921; -.
ProteinModelPortal; O49545; -.
SMR; O49545; -.
BioGrid; 21941; 6.
IntAct; O49545; 2.
STRING; 3702.AT5G65700.1; -.
iPTMnet; O49545; -.
PaxDb; O49545; -.
PRIDE; O49545; -.
EnsemblPlants; AT5G65700.1; AT5G65700.1; AT5G65700.
EnsemblPlants; AT5G65700.2; AT5G65700.2; AT5G65700.
GeneID; 836699; -.
Gramene; AT5G65700.1; AT5G65700.1; AT5G65700.
Gramene; AT5G65700.2; AT5G65700.2; AT5G65700.
KEGG; ath:AT5G65700; -.
Araport; AT5G65700; -.
TAIR; locus:2169965; AT5G65700.
eggNOG; ENOG410IERA; Eukaryota.
eggNOG; COG0515; LUCA.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000116551; -.
InParanoid; O49545; -.
OMA; WPVIEYL; -.
OrthoDB; EOG093601AP; -.
PhylomeDB; O49545; -.
PRO; PR:O49545; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; O49545; baseline and differential.
Genevisible; O49545; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0048437; P:floral organ development; IGI:TAIR.
GO; GO:0048229; P:gametophyte development; IGI:TAIR.
GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
Gene3D; 3.80.10.10; -; 4.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR025875; Leu-rich_rpt_4.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR013210; LRR_N_plant-typ.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00560; LRR_1; 1.
Pfam; PF12799; LRR_4; 1.
Pfam; PF08263; LRRNT_2; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Developmental protein;
Differentiation; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Serine/threonine-protein kinase; Signal; Transferase;
Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1003 Leucine-rich repeat receptor-like
serine/threonine-protein kinase BAM1.
/FTId=PRO_0000403352.
TOPO_DOM 20 640 Extracellular. {ECO:0000255}.
TRANSMEM 641 661 Helical. {ECO:0000255}.
TOPO_DOM 662 1003 Cytoplasmic. {ECO:0000255}.
REPEAT 68 92 LRR 1.
REPEAT 93 116 LRR 2.
REPEAT 117 140 LRR 3.
REPEAT 142 165 LRR 4.
REPEAT 166 191 LRR 5.
REPEAT 193 213 LRR 6.
REPEAT 215 238 LRR 7.
REPEAT 239 262 LRR 8.
REPEAT 263 285 LRR 9.
REPEAT 286 310 LRR 10.
REPEAT 312 334 LRR 11.
REPEAT 335 358 LRR 12.
REPEAT 359 382 LRR 13.
REPEAT 385 406 LRR 14.
REPEAT 407 430 LRR 15.
REPEAT 432 454 LRR 16.
REPEAT 455 480 LRR 17.
REPEAT 482 502 LRR 18.
REPEAT 503 526 LRR 19.
REPEAT 527 550 LRR 20.
REPEAT 551 574 LRR 21.
REPEAT 575 598 LRR 22.
DOMAIN 694 971 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 700 708 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 820 820 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 722 722 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 686 686 Phosphothreonine.
{ECO:0000250|UniProtKB:O22476}.
MOD_RES 769 769 Phosphotyrosine.
{ECO:0000250|UniProtKB:O22476}.
MOD_RES 807 807 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 855 855 Phosphoserine.
{ECO:0000250|UniProtKB:Q9M0G7}.
MOD_RES 863 863 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 870 870 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9M0G7}.
MOD_RES 871 871 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9M0G7}.
MOD_RES 996 996 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 586 586 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 601 601 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1003 AA; 109203 MW; E7577BC093F76228 CRC64;
MKLFLLLLFL LHISHTFTAS RPISEFRALL SLKTSLTGAG DDKNSPLSSW KVSTSFCTWI
GVTCDVSRRH VTSLDLSGLN LSGTLSPDVS HLRLLQNLSL AENLISGPIP PEISSLSGLR
HLNLSNNVFN GSFPDEISSG LVNLRVLDVY NNNLTGDLPV SVTNLTQLRH LHLGGNYFAG
KIPPSYGSWP VIEYLAVSGN ELVGKIPPEI GNLTTLRELY IGYYNAFEDG LPPEIGNLSE
LVRFDGANCG LTGEIPPEIG KLQKLDTLFL QVNVFSGPLT WELGTLSSLK SMDLSNNMFT
GEIPASFAEL KNLTLLNLFR NKLHGEIPEF IGDLPELEVL QLWENNFTGS IPQKLGENGK
LNLVDLSSNK LTGTLPPNMC SGNKLETLIT LGNFLFGSIP DSLGKCESLT RIRMGENFLN
GSIPKGLFGL PKLTQVELQD NYLSGELPVA GGVSVNLGQI SLSNNQLSGP LPPAIGNFTG
VQKLLLDGNK FQGPIPSEVG KLQQLSKIDF SHNLFSGRIA PEISRCKLLT FVDLSRNELS
GEIPNEITAM KILNYLNLSR NHLVGSIPGS ISSMQSLTSL DFSYNNLSGL VPGTGQFSYF
NYTSFLGNPD LCGPYLGPCK DGVAKGGHQS HSKGPLSASM KLLLVLGLLV CSIAFAVVAI
IKARSLKKAS ESRAWRLTAF QRLDFTCDDV LDSLKEDNII GKGGAGIVYK GVMPNGDLVA
VKRLAAMSRG SSHDHGFNAE IQTLGRIRHR HIVRLLGFCS NHETNLLVYE YMPNGSLGEV
LHGKKGGHLH WDTRYKIALE AAKGLCYLHH DCSPLIVHRD VKSNNILLDS NFEAHVADFG
LAKFLQDSGT SECMSAIAGS YGYIAPEYAY TLKVDEKSDV YSFGVVLLEL VTGRKPVGEF
GDGVDIVQWV RKMTDSNKDS VLKVLDPRLS SIPIHEVTHV FYVAMLCVEE QAVERPTMRE
VVQILTEIPK LPPSKDQPMT ESAPESELSP KSGVQSPPDL LNL


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CSB-EL013180MO Mouse Leucine-rich repeat serine_threonine-protein kinase 1(LRRK1) ELISA kit 96T
DB136_HUMAN Mouse ELISA Kit FOR Leucine-rich repeat and guanylate kinase domain-containing protein 96T


 

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