ID A0A674GM26_TAEGU Unreviewed; 1070 AA. AC A0A674GM26; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 22-FEB-2023, entry version 14. DE RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|PIRNR:PIRNR000556}; DE EC=2.7.11.25 {ECO:0000256|PIRNR:PIRNR000556}; GN Name=MAP3K21 {ECO:0000313|Ensembl:ENSTGUP00000023480.1}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae; OC Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000023480.1, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Ensembl:ENSTGUP00000023480.1, ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E., RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P., RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O., RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L., RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C., RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K., RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A., RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000023480.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-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=2.7.11.25; 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}. 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 AlphaFoldDB; A0A674GM26; -. DR Ensembl; ENSTGUT00000042241.1; ENSTGUP00000023480.1; ENSTGUG00000010194.2. DR GeneTree; ENSGT00940000159629; -. DR Proteomes; UP000007754; Chromosome 3. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. 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; PTHR44329:SF30; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 21; 1. DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF14604; SH3_9; 1. DR PIRSF; PIRSF000556; MAPKKK9_11; 2. 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:UP000007754}; 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 20..84 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 109..381 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 498..530 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 707..739 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 797..821 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 854..873 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 949..981 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 405..432 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 499..530 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 712..738 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 950..981 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 243 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000556-1" FT BINDING 115..123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2" FT BINDING 136 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000556-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 1070 AA; 118903 MW; 477CAD91CE04C972 CRC64; MALPDAGAAA AAAAAGGSGG PCPLWTALYD YEASGEDELS LRRGDVVEVL SQDAAVSGDD GWWAGKIRHR LGIFPANYVT RQPRGGAAAG GSGRGDPAGT LTEIDFQHLE LQEIIGVGGF GKVYRATWRG REVAVKAARQ DPDEDITATA ESVRQEAKLF SMLRHPNIIA LHGVCLREPN LCLVMEFARG GSLNRALAAA PGAAAARGGR RIPPHILVNW AVQIARGMLY LHDEAIVPIL HRDLKSSNIL LLEKMEHDDI CNKTLKITDF GLAREWHRTT KMSAAGTYAW MAPEVIKSSM FSKGSDIWSY GVLLWELLTG EVPYRGIDGL AVAYGVAVNK LTLPIPSTCP EPFAKLMKEC WEQDPHIRPS FALILEQLTA IEGAVMTEMP QESFHSMQDD WKLEIQQIFN ELRTKEKELR SREEELTRAA LQQKSQEELL KRREQQLAER EIDVLERELN IMIFQLNQEK PNVKKRKGKF KRSRLKLKDG HRISLPSDFQ HKITVQASPN LDKRRSLNSN NSSPSSSPTI IPRLRAIQLI PKTDTHTANG RRNSVYVYQQ DVDITSEYEL PCGVMKKGKI SLCFQVTSDE SNRTWGRSTT YHQEEFEDVK RNFKKKGCTW GPSSVQTKDR ADCKDKVRPL SDGSNPWSTV LMKNQKGVPL ASLFVDQGAC TDKKLIPEGL DSKRPKPIKL PNQAYINLPL WKDDQGENTV ENESFEEGTS ASSTNSTPQM TPTNSLSRTL HKKKTDSVLY GCAVLLASVA LGLDIRELNK SQGPDELLPK DERKKRDGIF QRASKFRRSA SPTRLQYKKE ETSIPSLDPA SDTVNLLSMP SISTKCLLQP DSEDAFLSTV LGDSGQCSST DNFSSQTSES KREQRIHLAP NTVLTQLKSQ PFSLGLKQES QNVPKDSSTK LCMLGHRRTL SDGSHFQTTA NGVASTNDVS RLPVLSVPGT LPSPSFQQRS NHSGVSNEKQ SAVNTISRPR PSSLRSKIDA WQIIPRIIKP NSKDSECSED NVDPDVNFLP DTEQRTNCHM PSLLDIDVEG QNRDCTVPLC RMKSKTCRPS IYELEREFLS //