AFC1_ARATH
ID AFC1_ARATH Reviewed; 467 AA.
AC P51566; Q39184;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine/threonine-protein kinase AFC1;
DE EC=2.7.12.1;
GN Name=AFC1; Synonyms=AME2; OrderedLocusNames=At3g53570; ORFNames=F4P12_270;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7991592; DOI=10.1073/pnas.91.25.12105;
RA Bender J., Fink G.R.;
RT "AFC1, a LAMMER kinase from Arabidopsis thaliana, activates STE12-dependent
RT processes in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12105-12109(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kuromori T., Yamamoto M.;
RT "A.thaliana genes encoding protein kinases of a new family.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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).
CC -!- FUNCTION: Activator of yeast transcription factor, STE12.
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=2.7.12.1;
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=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P51566-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. Lammer subfamily. {ECO:0000305}.
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; U16176; AAA57117.1; -; mRNA.
DR EMBL; D45354; BAA08215.1; -; mRNA.
DR EMBL; AL132966; CAB67664.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79110.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79111.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79112.1; -; Genomic_DNA.
DR PIR; S71169; S71169.
DR RefSeq; NP_001030853.1; NM_001035776.1. [P51566-1]
DR RefSeq; NP_190925.1; NM_115217.3. [P51566-1]
DR RefSeq; NP_850695.2; NM_180364.4. [P51566-1]
DR AlphaFoldDB; P51566; -.
DR SMR; P51566; -.
DR BioGRID; 9842; 1.
DR IntAct; P51566; 1.
DR STRING; 3702.AT3G53570.1; -.
DR PaxDb; P51566; -.
DR PRIDE; P51566; -.
DR ProteomicsDB; 244779; -. [P51566-1]
DR EnsemblPlants; AT3G53570.1; AT3G53570.1; AT3G53570. [P51566-1]
DR EnsemblPlants; AT3G53570.2; AT3G53570.2; AT3G53570. [P51566-1]
DR EnsemblPlants; AT3G53570.4; AT3G53570.4; AT3G53570. [P51566-1]
DR GeneID; 824525; -.
DR Gramene; AT3G53570.1; AT3G53570.1; AT3G53570. [P51566-1]
DR Gramene; AT3G53570.2; AT3G53570.2; AT3G53570. [P51566-1]
DR Gramene; AT3G53570.4; AT3G53570.4; AT3G53570. [P51566-1]
DR KEGG; ath:AT3G53570; -.
DR Araport; AT3G53570; -.
DR TAIR; locus:2084006; AT3G53570.
DR eggNOG; KOG0671; Eukaryota.
DR InParanoid; P51566; -.
DR PhylomeDB; P51566; -.
DR BRENDA; 2.7.12.1; 399.
DR PRO; PR:P51566; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P51566; baseline and differential.
DR Genevisible; P51566; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..467
FT /note="Serine/threonine-protein kinase AFC1"
FT /id="PRO_0000085600"
FT DOMAIN 115..443
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 121..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 117
FT /note="I -> M (in Ref. 1; AAA57117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 54198 MW; A885FD32CE11B181 CRC64;
MQSSVYRDKA SSIAMILETQ RNVEFPHRIV DKRPRKRPRL TWDAAPPLLP PPPPPTVFQP
PLYYGPEFAS GLVPNFVYPN MFYNGLPRQG SPPWRPDDKD GHYVFVVGDT LTPRYQILSK
MGEGTFGQVL ECFDNKNKEV VAIKVIRSIN KYREAAMIEI DVLQRLTRHD VGGSRCVQIR
NWFDYRNHIC IVFEKLGPSL YDFLRKNSYR SFPIDLVREL GRQLLESVAY MHDLRLIHTD
LKPENILLVS SEYIKIPDYK FLSRPTKDGS YFKNLPKSSA IKLIDFGSTT FEHQDHNYIV
STRHYRAPEV ILGVGWNYPC DLWSIGCILV ELCSGEALFQ THENLEHLAM MERVLGPLPP
HMVLRADRRS EKYFRRGAKL DWPEGATSRD SLKAVWKLPR LPNLIMQHVD HSAGDLIDLL
QGLLRYDPTE RFKAREALNH PFFTRSREQS IPPFNPNPHP FLYNQKN
