ID M3WK78_FELCA Unreviewed; 311 AA. AC M3WK78; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 3. DT 10-FEB-2021, entry version 55. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165}; DE EC=2.7.11.24 {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165}; GN Name=MAPK3 {ECO:0000313|Ensembl:ENSFCAP00000013148, 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, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000013148, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013148, 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, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013148, 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} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013148}; RG Ensembl; RL Submitted (MAR-2013) 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. 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 STRING; 9685.ENSFCAP00000013148; -. DR Ensembl; ENSFCAT00000014177; ENSFCAP00000013148; ENSFCAG00000014173. 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 embryo and 11 other tissues. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. 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; SSF56112; 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|RuleBase:RU000304}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000304}; KW 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" 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 //