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Database: UniProt
Entry: A0A452QPF4_URSAM
LinkDB: A0A452QPF4_URSAM
Original site: A0A452QPF4_URSAM 
ID   A0A452QPF4_URSAM        Unreviewed;      1212 AA.
AC   A0A452QPF4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN   Name=MAP3K5 {ECO:0000313|Ensembl:ENSUAMP00000007352.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000007352.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000007352.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
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DR   AlphaFoldDB; A0A452QPF4; -.
DR   STRING; 9643.ENSUAMP00000007352; -.
DR   Ensembl; ENSUAMT00000008325.1; ENSUAMP00000007352.1; ENSUAMG00000006263.1.
DR   GeneTree; ENSGT00940000159155; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IEA:Ensembl.
DR   GO; GO:1902911; C:protein kinase complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004706; F:JUN kinase kinase kinase activity; IEA:Ensembl.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR   GO; GO:0036480; P:neuron intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   CDD; cd06624; STKc_ASK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046873; HisK-N-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR043969; MAP3K_PH.
DR   InterPro; IPR025136; MAP3K_TRAF-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11584:SF332; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 5; 1.
DR   PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF19039; ASK_PH; 1.
DR   Pfam; PF20302; HisK-N-like; 1.
DR   Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          518..776
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1019..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1130..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1083..1117
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1212 AA;  137856 MW;  90A66A481E13F4A0 CRC64;
     SCWVSGTGCP YQKLTILSRY FNMFEFSGEL TPHPSWRLLF LQMCTGNYTF VPYMITPHNK
     VYCCDSSFMK GLTELMQPNF ELLLGPICLP LVDRFIQLLK VAQASSSQYF RESILNDIRK
     ARNLYTGKEL AAELARIRQR VDNIEVLTAD IVINLLLSYR DIQDYDSIVK LVETLEKLPT
     FDLASHHHVK FHYAFALNRR NLPGDRAKAL DVMIPLVQSE GQVASDMYCL VGRIYKDMFL
     DSNFLDTESR DHGASWFKKA FESEPSLQSG INYAVLLLAA GHQFESSFEL RKVGVKLSSL
     LGKKGNLEKL QSYWEVGFFL GASVLANDHM RVIQASEKLF KLKTPAWYLK SIVETILIYK
     HFVKLTTEQP VAKQELVDFW MDFLVEATKT DVTVVRFPVL ILEPTKIYQP SYLSINNEVE
     EKTISIWHVL PDDKKGIHEW NFSASSVRGV SISKFEERCC FLYVLHNSDD FQIYFCTELH
     CKKFFEMVNT ITEEKGRSTE EGDCESDSLE YDYEYDENGD RVVLGKGTYG IVYAGRDLSN
     QVRIAIKEIP ERDSRYSQPL HEEIALHKHL KHKNIVQYLG SFSENGFIKI FMEQVPGGSL
     SALLRSKWGP LKDNEQTIGF YTKQILEGLK YLHDNQIVHR DIKGDNVLIN TYSGVLKISD
     FGTSKRLAGI NPCTETFTGT LQYMAPEIID KGPRGYGKAA DIWSLGCTII EMATGKPPFY
     ELGEPQAAMF KVGMFKVHPE IPESMSAEAK AFILKCFEPD PDKRACANDL LIDEFLKVSS
     KKKKTQPKLS ALSAGSNEYL RSISLPVPVL VEDTSSSSEY GSVSPDTELK VDPFSFKTRA
     KSCGERDVKG IRTLFLGIPD ENFEDHSAPP SPEEKDSGFF MLRKDSERRA TLHRILTEDQ
     DKVVRNLMES LAQGAEEPKL KWEHITTLIA SLREFVRTTD RKIIATTLSK LKLELDFDSH
     GISQVQVVLF GFQDAVNKVL RNHNIKPHWM FALDSIIRKA VQTAITILVP ELRPHFSLAS
     ESDTADQEDL DAEDDHEERP SNQTIRRPHA VIEDAVATSG VSTLSSTVSH DSQNAHRSLN
     VQLGRMKIET NRLLEELVQK EKELQALLHQ AIEEKDQEIK HLKLKSQPID IPGLPECPRD
     SPGTNTEESE LTEWLREKGA DEDTISRFLA EDYSLEDVLF YVTRDDLKCL RLRGGTLCTL
     WKAITDFRDT QT
//
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