M313A_XENLA
ID M313A_XENLA Reviewed; 961 AA.
AC A7J1T2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 13-A;
DE EC=2.7.11.25;
GN Name=map3k13-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=xLZK-A_20115;
RA Itoh A., Ryan K., Itoh T.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have a role in the JNK signaling pathway. {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 -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; DQ862006; ABK15544.1; -; mRNA.
DR RefSeq; NP_001165660.1; NM_001172189.1.
DR AlphaFoldDB; A7J1T2; -.
DR SMR; A7J1T2; -.
DR GeneID; 100337578; -.
DR KEGG; xla:100337578; -.
DR CTD; 100337578; -.
DR Xenbase; XB-GENE-5753322; map3k13.L.
DR OrthoDB; 938929at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 100337578; Expressed in testis and 9 other tissues.
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:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017419; MAP3K12_MAP3K13.
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 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; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..961
FT /note="Mitogen-activated protein kinase kinase kinase 13-A"
FT /id="PRO_0000366129"
FT DOMAIN 169..410
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 88..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..455
FT /note="Leucine-zipper 1"
FT REGION 487..508
FT /note="Leucine-zipper 2"
FT REGION 513..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..824
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT COILED 458..497
FT /evidence="ECO:0000255"
FT COMPBIAS 90..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 175..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 961 AA; 107185 MW; BD4F6FE290D4272B CRC64;
MHLNDTMASP LEPLSWSSSP NLIVDTLRED KDYRVNYGDC TTIGHHEIKE TPDKCDSLDN
ANSPVTATVL TSISEDSRDQ FENSVLQLRD QDEPENTAPQ GSSHSGDGGS YSGNEDIRIH
FGHSGSGNSG FLEGLFGCLR PVWNIIGKAY STDYKLQQQE TWEVPFEEIS ELQWLGSGAQ
GAVFLGKFRG EEVAIKKVRE QKETDIKHLR KLKHPNIIAF KGVCTQAPCY CLIMEYCAHG
QLYEVLRAGR KVSPRLLVDW SNGIASGMNY LHLHKIIHRD LKSPNVLVTH TDTVKISDFG
TSKELSDKST KMSFAGTVAW MAPEVIRNEP VSEKVDIWSF GVLLWELLTG EIPYKDVDSS
AIIWGVGSNS LHLPVPSTCP DGFKILMKQT WHSKPRNRPS FRQILMHLDI ASADVLGTPQ
ETYFKSQAEW REEVKKHFEK IKSEGTCIHR LDEELIRRRR EELRHALDIR EHYERKLERA
NNLYMELSAI MLQLEVREKE LIRREQAVEK KYPGTYKRHP VRPIVHPNSV EKLIKKKGPP
SRIPSQTKRP DLLKSDGIVS AEGSAASASP ISGSPKTSSG GGKNRYRSKP RHRRVNSKGS
HADFIGVLKH LESPALSQQS SQHQTLASPP VTSCSPYHET SQVMPTFHQT LNVHGQNIAN
CANNLRYFGP AAALRSPLSS HAQRRMSGSS PDLLSSTLEA DSHIQPEREY EYCQQDPYNR
CPGCTEAVQQ DTDTGNWDST NVVTAEYRTS GGDPPESPRH NLVQENNEKL ESGGEQFSSF
KAAIGVSALT VPTPPALPRR IRTLRKNGDE SSEEEEGEVD SEVEFPRRHR PPRGMSKCQS
YSTFSSENFS VSDGEEGNTS DHSNSPDDVA GGGKVWHGDK LDDLSQTPEI PIEISMQSDG
LSDKECAVRR VKTQMSLGKL CTEEHNYENA GNFAESDCDS SEGECSDATV LTNNPVNSST
W
