ID M3WK78_FELCA Unreviewed; 311 AA. AC M3WK78; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 3. DT 14-DEC-2022, entry version 62. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165}; GN Name=MAPK3 {ECO:0000313|Ensembl:ENSFCAP00000013148.4, GN ECO:0000313|VGNC:VGNC:68168}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000013148.4, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000013148.4, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013148.4, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A., RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A., RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G., RA Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000013148.4, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013148.4, RC ECO:0000313|Proteomes:UP000011712}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000013148.4} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013148.4}; RG Ensembl; RL Submitted (AUG-2022) 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|ARBA:ARBA00001946, CC ECO:0000256|RuleBase:RU361165}; CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine CC phosphorylation. {ECO:0000256|RuleBase:RU361165}. CC -!- SUBCELLULAR LOCATION: Membrane, caveola CC {ECO:0000256|ARBA:ARBA00004345}. 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}. 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; AANG04004202; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; M3WK78; -. DR Ensembl; ENSFCAT00000014177.5; ENSFCAP00000013148.4; ENSFCAG00000014173.5. DR VGNC; VGNC:68168; MAPK3. DR eggNOG; KOG0660; Eukaryota. DR GeneTree; ENSGT00940000160691; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; M3WK78; -. DR Proteomes; UP000011712; Chromosome E3. DR Bgee; ENSFCAG00000014173; Expressed in testis and 10 other tissues. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProt. DR GO; GO:0005829; C:cytosol; IEA:UniProt. DR GO; GO:0005769; C:early endosome; IEA:UniProt. DR GO; GO:0005925; C:focal adhesion; IEA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt. DR GO; GO:0005770; C:late endosome; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0072584; P:caveolin-mediated endocytosis; IEA:UniProt. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:UniProt. DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IEA:UniProt. DR GO; GO:0090170; P:regulation of Golgi inheritance; IEA:UniProt. DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IEA:UniProt. DR GO; GO:0042221; P:response to chemical; IEA:UniProt. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008349; MAPK_ERK1/2. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01770; ERK1ERK2MAPK. 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 3: Inferred from homology; 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:UP000011712}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361165}. FT DOMAIN 13..262 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 311 AA; 35947 MW; 824CF53706E5B7F2 CRC64; VVKGQPFDVG PRYTQLQYIG EGAYGMVSSA YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN VIGIRDILRA PTLEAMRDVY IVQDLMETDL YKLLKSQQLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLINTTCD LKGYTKSIDI WSVGCILAEM LSNRPIFPGK HYLDQLNHIL GILGSPSQED LNCIINMKAR NYLQSLPSKT KVAWAKLFPK SDAKALDLLD RMLTFNPNKR ITVEEALAHP YLEQYYDPTD EPVAEEPFTF DMELDDLPKE RLKELIFQET ARFQPGALEA P //