PAM74_ARATH
ID PAM74_ARATH Reviewed; 884 AA.
AC C0LGW2; F4KJ90; Q9FN96;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase PAM74;
DE EC=2.7.11.1;
DE AltName: Full=Protein PHOTOSYNTHESIS AFFECTED MUTANT 74;
DE Flags: Precursor;
GN Name=PAM74; OrderedLocusNames=At5g59650; ORFNames=MTH12.9;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RA Awan F.S., Schneider A., Leister D., Khan I.A.;
RT "The pam74 mutant is caused by an insertion in a receptor-like kinase
RT gene.";
RL (In) Proceedings of the 18th international conference on Arabidopsis
RL research, abstract#362, Beijing (2007).
RN [5]
RP INTERACTION WITH AMT1-1.
RX PubMed=21423366; DOI=10.3389/fphys.2010.00024;
RA Lalonde S., Sero A., Pratelli R., Pilot G., Chen J., Sardi M.I.,
RA Parsa S.A., Kim D.Y., Acharya B.R., Stein E.V., Hu H.C., Villiers F.,
RA Takeda K., Yang Y., Han Y.S., Schwacke R., Chiang W., Kato N., Loque D.,
RA Assmann S.M., Kwak J.M., Schroeder J.I., Rhee S.Y., Frommer W.B.;
RT "A membrane protein/signaling protein interaction network for Arabidopsis
RT version AMPv2.";
RL Front. Physiol. 1:24-24(2010).
CC -!- FUNCTION: Required for accurate photosynthesis. {ECO:0000269|Ref.4}.
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 -!- SUBUNIT: Binds to the ammonium transporter AMT1-1.
CC {ECO:0000269|PubMed:21423366}.
CC -!- INTERACTION:
CC C0LGW2; C0LGD9: At1g07560; NbExp=2; IntAct=EBI-16888393, EBI-16902423;
CC C0LGW2; A0A178UFM8: AXX17_At5g50380; NbExp=3; IntAct=EBI-16888393, EBI-20653342;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Partially lethal. Survivors turn pale green and
CC show a stunted growth. Affected in photosynthesis; difference in the
CC quantum efficiency of PS11. {ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09503.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB006705; BAB09503.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97216.2; -; Genomic_DNA.
DR EMBL; FJ708806; ACN59397.1; -; mRNA.
DR RefSeq; NP_001318839.1; NM_001345363.1.
DR AlphaFoldDB; C0LGW2; -.
DR SMR; C0LGW2; -.
DR BioGRID; 21330; 240.
DR IntAct; C0LGW2; 235.
DR STRING; 3702.AT5G59650.1; -.
DR PaxDb; C0LGW2; -.
DR EnsemblPlants; AT5G59650.1; AT5G59650.1; AT5G59650.
DR GeneID; 836086; -.
DR Gramene; AT5G59650.1; AT5G59650.1; AT5G59650.
DR KEGG; ath:AT5G59650; -.
DR Araport; AT5G59650; -.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGW2; -.
DR PhylomeDB; C0LGW2; -.
DR PRO; PR:C0LGW2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGW2; baseline and differential.
DR Genevisible; C0LGW2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..884
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase PAM74"
FT /id="PRO_0000387517"
FT TOPO_DOM 24..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 412..433
FT /note="LRR 1"
FT REPEAT 436..457
FT /note="LRR 2"
FT REPEAT 460..480
FT /note="LRR 3"
FT DOMAIN 579..852
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 704
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 585..593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 652
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 739
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 744
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 752
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 884 AA; 98530 MW; 07899C7FD031640D CRC64;
MDSPCWLLLL LLGAFAIIGC VQAQDQQEFI SLDCGLPMTE PSSYTESVTG LRFSSDAEFI
QTGESGKIQA SMENDYLKPY TRLRYFPEER RNCYSLSVDK NRKYLIRARF IYGNYDGRNS
NPIFELHLGP NLWATIDLQK FVNGTMEEIL HTPTSNSLNV CLVKTGTTTP LISALELRPL
GNNSYLTDGS LNLFVRIYLN KTDGFLRYPD DIYDRRWHNY FMVDDWTQIF TTLEVTNDNN
YEPPKKALAA AATPSNASAP LTISWPPDNP GDQYYLYSHF SEIQDLQTND TREFDILWDG
AVVEEGFIPP KLGVTTIHNL SPVTCKGENC IYQLIKTSRS TLPSLLNALE IYTVIQFPRS
ETNENDVVAV KNIEAAYKLS RIRWQGDPCV PQKYAWDGLN CSNNTDVSKP PRVLSLNLSS
SGLTGIIAAA IQNLTHLEKL DLSNNTLTGV VPEFLAQMKS LVIINLSGNN LSGPLPQGLR
REGLELLVQG NPRLCLSGSC TEKNSKKKFP VVIVASVASV AIIVAVLVII FVLSKKKSST
VGALQPPLSM PMVHDNSPEP SIETKKRRFT YSEVIKMTNN FQRVVGEGGF GVVCHGTING
SEQVAVKVLS QSSSQGYKHF KAEVDLLLRV HHTNLVSLVG YCDERDHLAL IYEFLPKGDL
RQHLSGKSGG SFINWGNRLR IALEAALGLE YLHSGCTPPI VHRDIKTTNI LLDEQLKAKL
ADFGLSRSFP IGGETHISTV VAGTPGYLDP EYYQTTRLGE KSDVYSFGIV LLEIITNQPV
IDQSRSKSHI SQWVGFELTR GDITKIMDPN LNGDYESRSV WRVLELAMSC ANPSSVNRPN
MSQVANELKE CLVSENLREN MNMDSQNSLK VSMSFDTELF PRAR
