ERECT_ARATH » LRR receptor-like serine/threonine-protein kinase ERECTA

ERECT_ARATH » LRR receptor-like serine/threonine-protein kinase ERECTA
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
ERECT_ARATH » LRR receptor-like serine/threonine-protein kinase ERECTA » Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1;Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1;Protein TRANSPIRATION EFFICIENCY 1;
Hydrophobic Thickness 29.6 ± 1.8 Å
Tilt Angle 3 ± 2°
ΔGtransfer -39.3 kcal/mol
ΔGfold -20.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology Out
TM Segments 574-602 (568-603)
Pathways none
PDB none
OPM none
Complexes none
Interactions

BET12, Complex: ERECT:BET12

C98A3, Complex: ERECT:C98A3

ERL1, Complex: ERECT:ERL1

MSBP1, Complex: ERECT:MSBP1

TCMO, Complex: ERECT:TCMO

TMM, Complex: ERECT:TMM

UBC34, Complex: ERECT:UBC34

Domains

AA: 23-64, PDBID: 4J0M, Subunit B, Seq Identity:44%, Leucine rich repeat N-terminal domain

AA: 116-176, PDBID: 4M7E, Subunit C, Seq Identity:43%, Leucine rich repeat

AA: 379-439, PDBID: 4M7E, Subunit C, Seq Identity:40%, Leucine rich repeat

AA: 427-487, PDBID: 3RGX, Subunit A, Seq Identity:39%, Leucine rich repeat

AA: 648-913, PDBID: 3TL8, Subunit A, Seq Identity:40%, Protein kinase domain

UniProt annotation for ERECT_ARATH » LRR receptor-like serine/threonine-protein kinase ERECTA
FUNCTION: Receptor kinase that, together with ERL1 and ERL2, regulates aerial architecture, including inflorescence (e.g. shoot apical meristem-originating organ shape, elongation of the internode and pedicels, and adaxial-abaxial polarity), and stomatal patterning (e.g. density and clustering), probably by tuning cell division and expansion. Redundantly involved with ERL1 in procambial development regulation. Forms a functional ligand- receptor pair with EPF2 (AC Q8LC53) (PubMed). Modulates plant transpiration efficiency by controlling stomatal density, leaf photosynthetic capacity, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. A phloem-specific expression of ER is sufficient for proper inflorescence architecture (PubMed). Probable major trait regulating canalization (maintenance of phenotype despite varying environment) in many aspect of the plant physiology (e.g. plant morphology, light-dependent leaves number, branch number, flowering time, phytate and mineral concentrations) by transducing microenvironmental variation into phenotypic differentiation (ecological amplifier). May maintain development integrity in heat stress conditions. Regulates cell wall composition and structure. Confers resistance to the pathogenic bacteria Ralstonia solanacearum and to the necrotrophic fungi Plectosphaerella cucumerina and Pythium irregulare, and required for callose deposition upon infection. Resistance to P.cucumerina seems cell wall-mediated.

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.

SUBUNIT: Homodimer and heterodimer with ERL1. Interacts with EPF1, EPF2, EPFL4, EPFL5 and EPFL6.

TISSUE SPECIFICITY: Mostly expressed in shoot apical meristems (SAM), organ primordia, flowers, siliques and young rosette leaves, and, to a lower extent, in stems and cauline leaves. Expressed in growing inflorescence stems and pedicels. Detected in epidermis, phloem and xylem.

DEVELOPMENTAL STAGE: Strongly expressed in organ primordia and immature organs but weakly in mature organs. Observed in SAM at low levels during the vegetative growth with an increase at the transition to the reproductive growth phase. At the reproductive stage, localized in the young developing flowers. Expressed in inflorescence meristem and is up-regulated during flower initiation and formation of flower organs. Also found in cells that differentiate into pedicels.

DOMAIN: The kinase domain is not required for ligand binding.

UniProt features for ERECT_ARATH » LRR receptor-like serine/threonine-protein kinase ERECTA
SIGNAL 1 24 Potential.
CHAIN 25 976 LRR receptor-like serine/threonine- protein kinase ERECTA.
REPEAT 69 92 LRR 1.
REPEAT 93 115 LRR 2.
REPEAT 117 140 LRR 3.
REPEAT 141 163 LRR 4.
REPEAT 165 187 LRR 5.
REPEAT 189 212 LRR 6.
REPEAT 213 235 LRR 7.
REPEAT 237 259 LRR 8.
REPEAT 260 282 LRR 9.
REPEAT 284 306 LRR 10.
REPEAT 308 330 LRR 11.
REPEAT 332 355 LRR 12.
REPEAT 356 379 LRR 13.
REPEAT 380 401 LRR 14.
REPEAT 404 425 LRR 15.
REPEAT 428 449 LRR 16.
REPEAT 452 473 LRR 17.
REPEAT 476 498 LRR 18.
REPEAT 500 522 LRR 19.
REPEAT 523 545 LRR 20.
DOMAIN 648 918 Protein kinase.
ACT_SITE 773 773 Proton acceptor (By similarity).
Amino Acid Sequence for ERECT_ARATH » LRR receptor-like serine/threonine-protein kinase ERECTA
MALFRDIVLL GFLFCLSLVA TVTSEEGATL LEIKKSFKDV NNVLYDWTTS PSSDYCVWRG VSCENVTFNV VALNLSDLNL DGEISPAIGD LKSLLSIDLR GNRLSGQIPD EIGDCSSLQN LDLSFNELSG DIPFSISKLK QLEQLILKNN QLIGPIPSTL SQIPNLKILD LAQNKLSGEI PRLIYWNEVL QYLGLRGNNL VGNISPDLCQ LTGLWYFDVR NNSLTGSIPE TIGNCTAFQV LDLSYNQLTG EIPFDIGFLQ VATLSLQGNQ LSGKIPSVIG LMQALAVLDL SGNLLSGSIP PILGNLTFTE KLYLHSNKLT GSIPPELGNM SKLHYLELND NHLTGHIPPE LGKLTDLFDL NVANNDLEGP IPDHLSSCTN LNSLNVHGNK FSGTIPRAFQ KLESMTYLNL SSNNIKGPIP VELSRIGNLD TLDLSNNKIN GIIPSSLGDL EHLLKMNLSR NHITGVVPGD FGNLRSIMEI DLSNNDISGP IPEELNQLQN IILLRLENNN LTGNVGSLAN CLSLTVLNVS HNNLVGDIPK NNNFSRFSPD SFIGNPGLCG SWLNSPCHDS RRTVRVSISR AAILGIAIGG LVILLMVLIA ACRPHNPPPF LDGSLDKPVT YSTPKLVILH MNMALHVYED IMRMTENLSE KYIIGHGASS TVYKCVLKNC KPVAIKRLYS HNPQSMKQFE TELEMLSSIK HRNLVSLQAY SLSHLGSLLF YDYLENGSLW DLLHGPTKKK TLDWDTRLKI AYGAAQGLAY LHHDCSPRII HRDVKSSNIL LDKDLEARLT DFGIAKSLCV SKSHTSTYVM GTIGYIDPEY ARTSRLTEKS DVYSYGIVLL ELLTRRKAVD DESNLHHLIM SKTGNNEVME MADPDITSTC KDLGVVKKVF QLALLCTKRQ PNDRPTMHQV TRVLGSFMLS EQPPAATDTS ATLAGSCYVD EYANLKTPHS VNCSSMSASD AQLFLRFGQV ISQNSE