ID H2N3D7_PONAB Unreviewed; 1040 AA.
AC H2N3D7; A0A2J8UE32;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR000556};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR000556};
GN Name=MAP3K21 {ECO:0000313|Ensembl:ENSPPYP00000000106.3};
GN ORFNames=CR201_G0028573 {ECO:0000313|EMBL:PNJ43514.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000000106.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000000106.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ43514.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ43514.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000000106.3}
RP IDENTIFICATION.
RG Ensembl;
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=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000478};
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; Evidence={ECO:0000256|ARBA:ARBA00000106,
CC ECO:0000256|PIRNR:PIRNR000556};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- ACTIVITY REGULATION: Homodimerization via the leucine zipper domains is
CC required for autophosphorylation. {ECO:0000256|PIRNR:PIRNR000556}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000556}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529, ECO:0000256|PIRNR:PIRNR000556}.
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DR EMBL; NDHI03003462; PNJ43514.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000000106; -.
DR Ensembl; ENSPPYT00000000115.3; ENSPPYP00000000106.3; ENSPPYG00000000106.3.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000159629; -.
DR HOGENOM; CLU_000288_7_14_1; -.
DR OMA; KDRASHH; -.
DR OrthoDB; 876955at2759; -.
DR TreeFam; TF105118; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12058; SH3_MLK4; 1.
DR CDD; cd14146; STKc_MLK4; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR016231; MLK1-4.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23257:SF750; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 21; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF000556; MAPKKK9_11; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000556};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|PIRNR:PIRNR000556};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000556};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000556};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|PIRNR:PIRNR000556}.
FT DOMAIN 38..102
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 128..405
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-1"
FT BINDING 134..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1040 AA; 114213 MW; DB0AE1D4D6DD9F3A CRC64;
MALPGAAGAA DTPVSSAGGA PGGSASSSST SSGGSASVGA GLWAALYDYE ARGEDELSLR
RGQLVEVLSQ DAAVSGDEGW WAGQVQRRLG IFPANYVAPC RPAASPAQPP APPPPRPSSP
VHVAFERLEL KELIGAGGFG QVYRATWQGQ EVAVKAARQD PEQDAAAAAE SVRREARLFA
MLRHPNIIEL RGVCLQQPHL CLVLEFARGG ALNRVLAAAN TAPDPRAPGP RRARRIPPHV
LVNWAVQIAR GMLYLHEEAF VPILHRDLKS SNILLLEKIE HDDICNKTLK ITDFGLAREW
HRTTKMSAAG TYAWMAPEVI KSSLFSKGSD IWSYGVLLWE LLTGEVPYRG IDGLAVAYGV
AVNKLTLPIP STCPEPFAKL MKECWEQDPH IRPSFALILE QLTAIEGAVM TEMPQESFHS
MQDDWKLEIQ QMFDELRTKE KELRSREEEL TRAALQQKSQ EELLKRREQQ LAEREIDVLE
RELNILIFQL NQEKPKVKKR KGKFKRSRLK LKDGHRISLP SDFQHKITVQ ASPNLDKRRS
LNSSSSSPPS SPTMMPRLRA IQLTSDESNK TWGRNTVFRQ EEFEDVRRNF KKKGCTWGPN
SIQMKERTDC KERIRPLSDG NSPWSTILIK NQKTMPLASL FVDQPGSCEE PKLSPDGVEH
RKPKQIKLPS QAYIDLPLGK DAQRENPAEG ESWEEATSAN AATVSTEMTP TNSLSRSPQR
KKTESALYGC TVLLASVALG LDLRELHKAQ AAEEPLPKEE KKKREGIFQR ASKSRRSASP
PTRLPSTGGE ASSPPSLPLT SALGILSTPS LSTKCLLQMD SEDPLAGSTP VTCDSEMLTP
DFCPTAPGSG CEPALMPRID TDSSVSRNLP SSFLEQTCGN VPYCASSKHR QSHHRRTMSD
GNPTPTGATT ISATGASALP LCPSPAPHSH LPREVSPKKH STVHIVPQPR PASLRSRSDL
PQAYPQTAVS QLAQTACVVG RPGPHPTQFL AAKERTKSHV PSLLEADVEG QSRDYTVPLC
RMRSKTSRPS IYELEKEFLS
//
