ID   AFC3_ARATH              Reviewed;         400 AA.
AC   P51568; Q39185;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   02-SEP-2026, entry version 167.
DE   RecName: Full=Serine/threonine-protein kinase AFC3;
DE            EC=2.7.12.1;
GN   Name=AFC3; Synonyms=AME3; OrderedLocusNames=At4g32660;
GN   ORFNames=F4D11.140;
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].
RA   Kuromori T., Yamamoto M.;
RT   "A.thaliana genes encoding protein kinases of a new family.";
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-400.
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC   -!- INTERACTION:
CC       P51568; P92964: RS31; NbExp=3; IntAct=EBI-25519318, EBI-927132;
CC       P51568; O81127: RSZ21; NbExp=3; IntAct=EBI-25519318, EBI-927172;
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=P51568-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. Lammer subfamily. {ECO:0000305}.
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DR   EMBL; D45355; BAA08216.1; -; mRNA.
DR   EMBL; AL022537; CAA18595.1; -; Genomic_DNA.
DR   EMBL; AL161581; CAB79983.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86100.1; -; Genomic_DNA.
DR   EMBL; OZ408686; CAO7049652.1; -; Genomic_DNA.
DR   EMBL; U16178; AAA57119.1; -; mRNA.
DR   PIR; T04460; T04460.
DR   RefSeq; NP_194992.1; NM_119418.3. [P51568-1]
DR   AlphaFoldDB; P51568; -.
DR   SMR; P51568; -.
DR   BioGRID; 14687; 8.
DR   FunCoup; P51568; 3429.
DR   IntAct; P51568; 2.
DR   STRING; 3702.P51568; -.
DR   iPTMnet; P51568; -.
DR   PaxDb; 3702-P51568; -.
DR   GeneID; 829401; -.
DR   KEGG; ath:AT4G32660; -.
DR   Araport; AT4G32660; -.
DR   TAIR; AT4G32660; AME3.
DR   eggNOG; KOG0671; Eukaryota.
DR   InParanoid; P51568; -.
DR   PhylomeDB; P51568; -.
DR   BRENDA; 2.7.12.1; 399.
DR   PRO; PR:P51568; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P51568; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISM:TAIR.
DR   GO; GO:0005886; C:plasma membrane; ISM:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
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:0046777; P:protein autophosphorylation; HDA:TAIR.
DR   GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR   CDD; cd14134; PKc_CLK; 1.
DR   FunFam; 1.10.510.10:FF:000612; Serine/threonine-protein kinase AFC2; 1.
DR   FunFam; 3.30.200.20:FF:000463; Serine/threonine-protein kinase AFC2; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR051175; CLK_kinases.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45646; SERINE/THREONINE-PROTEIN KINASE DOA-RELATED; 1.
DR   PANTHER; PTHR45646:SF11; SERINE_THREONINE-PROTEIN KINASE DOA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..400
FT                   /note="Serine/threonine-protein kinase AFC3"
FT                   /id="PRO_0000085602"
FT   DOMAIN          71..396
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         77..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        8
FT                   /note="S -> N (in Ref. 5; AAA57119)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  46224 MW;  8F707ABDCF9B1352 CRC64;
     MIANGFESMD KERVRKRPRM TWDEAPAEPE AKRAVIKGHG SDGRILSPPL RDDDRDGHYV
     FSLRDNLTPR YKILSKMGEG TFGRVLECWD RDTKEYVAIK IIRSIKKYRD AAMIEIDVLQ
     KLVKSDKGRT RCVQMKNWFD YRNHICIVFE KLGPSLFDFL KRNKYSAFPL ALVRDFGCQL
     LESVAYMHEL QLVHTDLKPE NILLVSSENV KLPDNKRSAA NETHFRCLPK SSAIKLIDFG
     STVCDNRIHH SIVQTRHYRS PEVILGLGWS YQCDLWSIGC ILFELCTGEA LFQTHDNLEH
     LAMMERALGP LPEHMTRKAS RGAEKYFRRG CRLNWPEGAN SRESIRAVKR LDRLKDMVSK
     HVDNTRSRFA DLLYGLLAYD PSERLTANEA LDHPFFKSSS
//