MK07_BOVIN
ID MK07_BOVIN Reviewed; 781 AA.
AC A5PKJ4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Mitogen-activated protein kinase 7;
DE Short=MAP kinase 7;
DE Short=MAPK 7;
DE EC=2.7.11.24;
GN Name=MAPK7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in various cellular processes such as
CC proliferation, differentiation and cell survival. The upstream
CC activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it
CC translocates to the nucleus and phosphorylates various downstream
CC targets including MEF2C. EGF activates MAPK7 through a Ras-independent
CC and MAP2K5-dependent pathway. May have a role in muscle cell
CC differentiation. May be important for endothelial function and
CC maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact
CC specifically with one another and not with MEK1/ERK1 or MEK2/ERK2
CC pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth
CC factor-induced cell cycle progression (By similarity). Involved in the
CC regulation of p53/TP53 by disrupting the PML-MDM2 interaction (By
CC similarity). {ECO:0000250}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC phosphorylation. Activated in response to hyperosmolarity, hydrogen
CC peroxide, and epidermal growth factor (EGF) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAP2K5. Forms oligomers (By similarity).
CC Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates
CC the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not
CC MEF2D (By similarity). Interacts with SGK1 (By similarity). Interacts
CC with PML (By similarity). Interacts (via N-terminal half) with
CC HSP90AB1-CDC37 chaperone complex in resting cells; the interaction is
CC MAP2K5-independent and prevents MAPK7 from ubiquitination and
CC proteasomal degradation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q13164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body
CC {ECO:0000250}. Note=Translocates to the nucleus upon activation.
CC {ECO:0000250}.
CC -!- DOMAIN: The second proline-rich region may interact with actin
CC targeting the kinase to a specific location in the cell.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-219 and Tyr-221, which activates the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; BC142510; AAI42511.1; -; mRNA.
DR RefSeq; NP_001092550.1; NM_001099080.2.
DR RefSeq; XP_005220440.1; XM_005220383.3.
DR AlphaFoldDB; A5PKJ4; -.
DR SMR; A5PKJ4; -.
DR STRING; 9913.ENSBTAP00000001347; -.
DR PaxDb; A5PKJ4; -.
DR PRIDE; A5PKJ4; -.
DR Ensembl; ENSBTAT00000001347; ENSBTAP00000001347; ENSBTAG00000001014.
DR GeneID; 537703; -.
DR KEGG; bta:537703; -.
DR CTD; 5598; -.
DR VEuPathDB; HostDB:ENSBTAG00000001014; -.
DR VGNC; VGNC:31222; MAPK7.
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000160215; -.
DR HOGENOM; CLU_008789_1_0_1; -.
DR InParanoid; A5PKJ4; -.
DR OMA; NWSGQQL; -.
DR OrthoDB; 741207at2759; -.
DR TreeFam; TF105099; -.
DR Reactome; R-BTA-198753; ERK/MAPK targets.
DR Reactome; R-BTA-198765; Signalling to ERK5.
DR Reactome; R-BTA-202670; ERKs are inactivated.
DR Reactome; R-BTA-8853659; RET signaling.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000001014; Expressed in trachea and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
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:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071499; P:cellular response to laminar fluid shear stress; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0060761; P:negative regulation of response to cytokine stimulus; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IEA:Ensembl.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:Ensembl.
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 Pfam; PF00069; Pkinase; 1.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Cytoplasm; Differentiation; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
FT CHAIN 2..781
FT /note="Mitogen-activated protein kinase 7"
FT /id="PRO_0000349104"
FT DOMAIN 55..347
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..77
FT /note="Required for cytoplasmic targeting"
FT /evidence="ECO:0000250"
FT REGION 78..139
FT /note="Required for binding to MAP2K5"
FT /evidence="ECO:0000250"
FT REGION 140..406
FT /note="Necessary for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 402..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..781
FT /note="May not be required for kinase activity; required to
FT stimulate MEF2C activity"
FT /evidence="ECO:0000250"
FT MOTIF 219..221
FT /note="TXY"
FT /evidence="ECO:0000250"
FT MOTIF 505..539
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..666
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 61..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
FT MOD_RES 698
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13164"
SQ SEQUENCE 781 AA; 84832 MW; 1BDFC98A7EA3751C CRC64;
MAEPLKEDDG EDGSGEPPGP VKAEPAGTAA SVAAKNLALL KARSFDVTFD VGDEYEIIET
IGNGAYGVVS SARRRLTGQQ VAIKKIPNAF DVVTNAKRTL RELKILKHFK HDNIIAIKDI
LRPTVPYGEF KSVYVVLDLM ESDLHQIIHS SQPLTLEHVR YFLYQLLRGL KYMHSAQVIH
RDLKPSNLLV NENCELKIGD FGMARGLCTS PAEHQYFMTE YVATRWYRAP ELMLSLHEYT
QAIDLWSVGC IFGEMLARRQ LFPGKNYVHQ LQLIMTVLGT PSPAVIQAVG AERVRAYIQS
LPPRQPVPWE TVYPGADRQA LSLLGRMLRF EPSARVSAAA ALRHPFLAKY HDPDDEPDCA
PPFDFAFDRE ALTRERIKEA IVAEIEDFHA RREGIRQQIR FQPSLQPVAS EPGCPDVEMP
SPWAPSGDCA MESPPPAPLP CPGPAPDTID LTLQPPPPAS EPAPPKKEGA ISDNTKAALK
AALLKSLRSR LRDGPSAPLE APEPRKPVTA QERQREREEK RRRRQERAKE REKRRQERER
KERGAGVSGG PSADPLAGLV LSDNDRSLLE RWTRMAQPPA PAPATARPPS PPAGPATQPT
GPLPQPACPP PAPAAGPAAP QTTAASGLLA PQPLVPPPGL PGPSALSVLP YFPSGPPPPD
PGGAPQPSTS ESPDVTLVTQ QLSKSQVEDP LPPVFSGTPK GSGAGYGVGF DLEEFLNQSF
DMGVADGPQD GQADSASLSA SLLADWLEGH GMNPADIESL QREIQMDSPM LLADLPDLQE
P
