SKM1_ARATH
ID SKM1_ARATH Reviewed; 960 AA.
AC O82318; Q42355;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase SKM1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein STERILITY-REGULATING KINASE MEMBER 1 {ECO:0000303|PubMed:23910659};
DE Flags: Precursor;
GN Name=SKM1 {ECO:0000303|PubMed:23910659};
GN OrderedLocusNames=At2g25790 {ECO:0000312|Araport:AT2G25790};
GN ORFNames=F17H15.18 {ECO:0000312|EMBL:AAC42251.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126.
RC STRAIN=cv. Columbia; TISSUE=Protoplast;
RA Cooke R., Laudie M., Raynal M., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-717, DISRUPTION PHENOTYPE, INTERACTION WITH
RP CLE45, AND TISSUE SPECIFICITY.
RX PubMed=23910659; DOI=10.1016/j.cub.2013.06.060;
RA Endo S., Shinohara H., Matsubayashi Y., Fukuda H.;
RT "A novel pollen-pistil interaction conferring high-temperature tolerance
RT during reproduction via CLE45 signaling.";
RL Curr. Biol. 23:1670-1676(2013).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27354416; DOI=10.15252/embr.201642450;
RA Kang Y.H., Hardtke C.S.;
RT "Arabidopsis MAKR5 is a positive effector of BAM3-dependent CLE45
RT signaling.";
RL EMBO Rep. 17:1145-1154(2016).
CC -!- FUNCTION: Receptor with a serine/threonine-protein kinase activity (By
CC similarity). Together with SKM2, LRR-rich receptor-like kinase (LRR-
CC RLK) required for male fertility by the perception of CLE43 and CLE45
CC peptides and the transduction of their promoting action in pollen
CC tubes, especially under relatively high temperature (at 30 degrees
CC Celsius), thus conferring tolerance against high temperature probably
CC through the maintenance of mitochondrial activity (PubMed:23910659).
CC Seems to not be involved in the perception of CLE45 peptide in roots
CC (PubMed:27354416). {ECO:0000250|UniProtKB:Q9ZWC8,
CC ECO:0000269|PubMed:23910659, ECO:0000269|PubMed:27354416}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Self-interacts (By similarity). Binds to CLE45 present in the
CC pistil, particularly under relatively high temperature (at 30 degrees
CC Celsius) (PubMed:23910659). {ECO:0000250|UniProtKB:Q9SYQ8,
CC ECO:0000269|PubMed:23910659}.
CC -!- INTERACTION:
CC O82318; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-20661246, EBI-20651541;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9SYQ8};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen grains and roots vascular
CC tissues (PubMed:23910659). Present in roots (PubMed:27354416).
CC {ECO:0000269|PubMed:23910659, ECO:0000269|PubMed:27354416}.
CC -!- DEVELOPMENTAL STAGE: In roots, restricted to the mature vasculature but
CC absent from the meristem. {ECO:0000269|PubMed:27354416}.
CC -!- DISRUPTION PHENOTYPE: Insensitivity of pollen tubes to CLE43 and,
CC partially, to CLE45 peptides-mediated growth stimulation
CC (PubMed:23910659). Pollen tubes of plants missing both SKM1 and SKM2
CC are fully insensitive to CLE45 peptides (PubMed:23910659). Reduced seed
CC production at 30 degrees Celsius, but not at 22 degrees Celsius
CC (PubMed:23910659). {ECO:0000269|PubMed:23910659}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23395.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC005395; AAC42251.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07753.1; -; Genomic_DNA.
DR EMBL; FJ708700; ACN59295.1; -; mRNA.
DR EMBL; F20108; CAA23395.1; ALT_FRAME; mRNA.
DR PIR; G84652; G84652.
DR RefSeq; NP_180150.1; NM_128139.3.
DR AlphaFoldDB; O82318; -.
DR SMR; O82318; -.
DR BioGRID; 2473; 29.
DR IntAct; O82318; 29.
DR STRING; 3702.AT2G25790.1; -.
DR PaxDb; O82318; -.
DR PRIDE; O82318; -.
DR ProteomicsDB; 243149; -.
DR EnsemblPlants; AT2G25790.1; AT2G25790.1; AT2G25790.
DR GeneID; 817121; -.
DR Gramene; AT2G25790.1; AT2G25790.1; AT2G25790.
DR KEGG; ath:AT2G25790; -.
DR Araport; AT2G25790; -.
DR TAIR; locus:2043540; AT2G25790.
DR eggNOG; ENOG502QRRF; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; O82318; -.
DR OMA; WIDSSID; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O82318; -.
DR PRO; PR:O82318; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82318; baseline and differential.
DR Genevisible; O82318; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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:0042277; F:peptide binding; IPI:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IMP:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
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 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; 9.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..960
FT /note="Leucine-rich repeat receptor-like serine/threonine-
FT protein kinase SKM1"
FT /id="PRO_0000389454"
FT TOPO_DOM 30..634
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 71..96
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 97..120
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 122..146
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 149..168
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 169..194
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 196..216
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 217..240
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 241..264
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 265..288
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 290..312
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 313..336
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 338..360
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 361..384
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 386..408
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 409..432
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 434..454
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 455..477
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 478..501
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 503..525
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 526..549
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 550..573
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 575..598
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT DOMAIN 691..953
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 221..226
FT /note="CLE45 peptide binding"
FT /evidence="ECO:0000250|UniProtKB:O65440"
FT BINDING 697..705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 717
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 834
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 61..68
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MUTAGEN 717
FT /note="K->E: In KDSKM1; lost kinase activity (kinase-dead).
FT High-temperature exposure (HTE) mediated reduction in seeds
FT number."
FT /evidence="ECO:0000269|PubMed:23910659"
SQ SEQUENCE 960 AA; 106448 MW; 865D523C610DD838 CRC64;
MSTSHHHHHP PYLITTLFFL FLNFSCLHAN ELELLLSFKS SIQDPLKHLS SWSYSSTNDV
CLWSGVVCNN ISRVVSLDLS GKNMSGQILT AATFRLPFLQ TINLSNNNLS GPIPHDIFTT
SSPSLRYLNL SNNNFSGSIP RGFLPNLYTL DLSNNMFTGE IYNDIGVFSN LRVLDLGGNV
LTGHVPGYLG NLSRLEFLTL ASNQLTGGVP VELGKMKNLK WIYLGYNNLS GEIPYQIGGL
SSLNHLDLVY NNLSGPIPPS LGDLKKLEYM FLYQNKLSGQ IPPSIFSLQN LISLDFSDNS
LSGEIPELVA QMQSLEILHL FSNNLTGKIP EGVTSLPRLK VLQLWSNRFS GGIPANLGKH
NNLTVLDLST NNLTGKLPDT LCDSGHLTKL ILFSNSLDSQ IPPSLGMCQS LERVRLQNNG
FSGKLPRGFT KLQLVNFLDL SNNNLQGNIN TWDMPQLEML DLSVNKFFGE LPDFSRSKRL
KKLDLSRNKI SGVVPQGLMT FPEIMDLDLS ENEITGVIPR ELSSCKNLVN LDLSHNNFTG
EIPSSFAEFQ VLSDLDLSCN QLSGEIPKNL GNIESLVQVN ISHNLLHGSL PFTGAFLAIN
ATAVEGNIDL CSENSASGLR PCKVVRKRST KSWWLIITST FAAFLAVLVS GFFIVLVFQR
THNVLEVKKV EQEDGTKWET QFFDSKFMKS FTVNTILSSL KDQNVLVDKN GVHFVVKEVK
KYDSLPEMIS DMRKLSDHKN ILKIVATCRS ETVAYLIHED VEGKRLSQVL SGLSWERRRK
IMKGIVEALR FLHCRCSPAV VAGNLSPENI VIDVTDEPRL CLGLPGLLCM DAAYMAPETR
EHKEMTSKSD IYGFGILLLH LLTGKCSSSN EDIESGVNGS LVKWARYSYS NCHIDTWIDS
SIDTSVHQRE IVHVMNLALK CTAIDPQERP CTNNVLQALE STSSSSSSCT TYLSKILSLA
