ID A0A0A7R547_GOSHI Unreviewed; 370 AA.
AC A0A0A7R547;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165};
DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165};
GN Name=MPK18 {ECO:0000313|EMBL:AJA29676.1};
GN Synonyms=LOC107900875 {ECO:0000313|RefSeq:XP_016682111.1,
GN ECO:0000313|RefSeq:XP_016682112.1, ECO:0000313|RefSeq:XP_016682113.1,
GN ECO:0000313|RefSeq:XP_016682114.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|EMBL:AJA29676.1};
RN [1] {ECO:0000313|EMBL:AJA29676.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25492847;
RA Zhang X., Wang L., Xu X., Cai C., Guo W.;
RT "Genome-wide identification of mitogen-activated protein kinase gene family
RT in Gossypium raimondii and the function of their corresponding orthologs in
RT tetraploid cultivated cotton.";
RL BMC Plant Biol. 14:345-345(2014).
RN [2] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [3] {ECO:0000313|RefSeq:XP_016682111.1, ECO:0000313|RefSeq:XP_016682112.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016682111.1,
RC ECO:0000313|RefSeq:XP_016682112.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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=2.7.11.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000494};
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=2.7.11.24; Evidence={ECO:0000256|ARBA:ARBA00000088,
CC ECO:0000256|RuleBase:RU361165};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU361165};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000256|RuleBase:RU361165}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00008832}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. MAP kinase subfamily. {ECO:0000256|RuleBase:RU361165}.
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DR EMBL; KM190120; AJA29676.1; -; mRNA.
DR RefSeq; NP_001313822.1; NM_001326893.1.
DR RefSeq; XP_016682111.1; XM_016826622.1.
DR RefSeq; XP_016682112.1; XM_016826623.1.
DR RefSeq; XP_016682113.1; XM_016826624.1.
DR RefSeq; XP_016682114.1; XM_016826625.1.
DR STRING; 3635.A0A0A7R547; -.
DR PaxDb; 3635-A0A0A7R547; -.
DR GeneID; 107900875; -.
DR KEGG; ghi:107900875; -.
DR OrthoDB; 5474493at2759; -.
DR Proteomes; UP000189702; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07858; STKc_TEY_MAPK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR PANTHER; PTHR24055:SF439; MITOGEN-ACTIVATED PROTEIN KINASE 11-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165};
KW Magnesium {ECO:0000256|RuleBase:RU361165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361165}.
FT DOMAIN 37..323
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 370 AA; 42601 MW; F7B186273F12272A CRC64;
MSMGPGDQSI KGIPTHGGRY VQYNVYGNLF EVPSKYVAPL RPIGRGAYGI VCAAVNSETQ
EEVAIKKIGN AFDNRIDAKR TLREIKLLRH MDHENVVAIK DIIRPPQWEN FNDVYLVYEL
MDTDLHQIIR SNQPLTDDHC RYFLYQILRG LKYVHSANVL HRDLKPSNLF LNANCDLKIG
DFGLARTTSE TDFMTEYVVT RWYRAPELLL NCSEYTAAID IWSVGCILGE IMSRQPLFPG
KDYVHQLRLI TELIGSPDDS SLGFLRSDNA RRYVRQLPQN PRQNFSSRFP NLSPGAIDLL
EKMLIFDPHR RITVDGALCH PYLAPLHDIN EEPVCPRPFS FDFEQPSFTE ENIKELIYRE
SVKFNPDPMY
//
