M3K13_BOVIN
ID M3K13_BOVIN Reviewed; 966 AA.
AC A7MBB4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 13;
DE EC=2.7.11.25;
GN Name=MAP3K13;
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 (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activates the JUN N-terminal pathway through activation of
CC the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to
CC regulate the activation of NF-kappa-B in the cytosol. This activation
CC is kinase-dependent and involves activating the IKK complex, the IKBKB-
CC containing complex that phosphorylates inhibitors of NF-kappa-B (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=2.7.11.25;
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=2.7.11.25;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation and
CC homodimerization. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; forms dimers through the leucine-zipper motif.
CC Interacts with the C-terminus of MAPK8IP1 through the kinase catalytic
CC domain. Binds PRDX3. Associates with the IKK complex through the kinase
CC domain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BC151464; AAI51465.1; -; mRNA.
DR RefSeq; NP_001095323.1; NM_001101853.2.
DR AlphaFoldDB; A7MBB4; -.
DR SMR; A7MBB4; -.
DR STRING; 9913.ENSBTAP00000022739; -.
DR PaxDb; A7MBB4; -.
DR PRIDE; A7MBB4; -.
DR GeneID; 505369; -.
DR KEGG; bta:505369; -.
DR CTD; 9175; -.
DR eggNOG; KOG4721; Eukaryota.
DR InParanoid; A7MBB4; -.
DR OrthoDB; 938929at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
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:0007254; P:JNK cascade; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017419; MAP3K12_MAP3K13.
DR InterPro; IPR027258; MAPKKK13.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR PIRSF; PIRSF500742; MAPKKK13; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..966
FT /note="Mitogen-activated protein kinase kinase kinase 13"
FT /id="PRO_0000366128"
FT DOMAIN 168..409
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..454
FT /note="Leucine-zipper 1"
FT REGION 486..507
FT /note="Leucine-zipper 2"
FT REGION 561..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..828
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 937..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..496
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 174..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 966 AA; 108152 MW; 4D632EAC6AF13FF5 CRC64;
MANPQEHLSC SSSPRLPLSE NKTFNGLQDD LAPMGSHASP KLLKDQQEKG MVQTELAEGT
NSPITTTVLT SISEDSRDQF ENSVLQLREQ DESEMAMSHG NSNTVDGEGT SGTEDIKIQF
SRSGSGSGGF LEGLFGCLRP VWNIIGKAYS TDYKLQQQDT WEVPFEEISE LQWLGSGAQG
AVFLGKFRAE EVAIKKVREQ NETDIKHLRK LKHPNIIAFK GVCTQAPCYC IIMEYCAHGQ
LYEVLRAGRK ITPRLLVDWS TGIASGMNYL HLHKIIHRDL KSPNVLVTHT DAVKISDFGT
SKELSDKSTK MSFAGTVAWM APEVIRNEPV SEKVDIWSFG VVLWELLTGE IPYKDVDSSA
IIWGVGSNSL HLPVPSTCPD GFKILMKQTW QSKTRNRPSF RQTLMHLDIA SADVLATPQE
TYFKSQAEWR EEVKKHFEKI KSEGTCIHRL DEELIRRRRE ELRHALDIRE HYERKLERAN
NLYMELSAIM LQLEMREKEL IKREQAVEKK YPGTYKRHPV RPIIHPNAME KLMKRKGMPH
RPGMQAKRPD LLRSEGIPSV EVAPTASPLS GSPKLSSSSS KSRYRSKPRH RRGNSRGSHG
DFAAILKNQP AQEDSPHPTS LHQAEPQYPS SQHHNLLQQQ YQQPPPAMSQ SHHPRLNMHG
QDIATCPNNL RYFGPAAALR SPLSNHSQRQ MPGSSPDLIS TAMAADCWRS SEPDKGQAGP
WGCCQADPYD PCLQCRPEQH GSLDVPSAKP VGRSPSLFKP PAHNPLLENA QGSEKMEENE
FSGYRSASSL GASHHITPPV LPRKTRPLQK SGDDSSEEEE GEVDSEVEFP RRQRPHRCIS
SCQSYSTFSS ENFSVSDGEE GNTSDHSNSP DELADKLEDH LAEKLDDLLS QTPEIPIEIS
SHSDGLSDKE CAVRRVKTQM SLGKLCAEER GYENPMQFEE SDCDSSDGEC SDATVRTNKH
YSSATW
