ID M3W947_FELCA Unreviewed; 1366 AA.
AC M3W947;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 68.
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:ENSFCAP00000007586.5,
GN ECO:0000313|VGNC:VGNC:68159};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000007586.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000007586.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007586.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000007586.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007586.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000007586.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000007586.5};
RG Ensembl;
RL Submitted (SEP-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 -!- 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 EMBL; AANG04000169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000007586; -.
DR PaxDb; 9685-ENSFCAP00000007586; -.
DR Ensembl; ENSFCAT00000008188.6; ENSFCAP00000007586.5; ENSFCAG00000008186.6.
DR VGNC; VGNC:68159; MAP3K5.
DR eggNOG; KOG4279; Eukaryota.
DR GeneTree; ENSGT00940000159155; -.
DR HOGENOM; CLU_003687_2_0_1; -.
DR InParanoid; M3W947; -.
DR OMA; ICLAHSK; -.
DR Proteomes; UP000011712; Chromosome B2.
DR Bgee; ENSFCAG00000008186; Expressed in brain and 10 other cell types or tissues.
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:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; 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:1902170; P:cellular response to reactive nitrogen species; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IBA:GO_Central.
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:0038066; P:p38MAPK cascade; 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:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0097300; P:programmed necrotic cell death; IEA:Ensembl.
DR CDD; cd06624; STKc_ASK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046872; DRHyd-ASK.
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; PF20309; DRHyd-ASK; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 672..930
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1237..1268
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1366 AA; 153386 MW; CD912DB682E9547C CRC64;
MSTEAGEGIT FSVPPFAEGG SCRRGAAAAA AEGEESQLPP PPPGSFWNVE SAAAPGTGCP
AATSGSSATR CRGNSGGGGG RRTTVAYVIN EASQGQLVMA ESEALQSLRE ACETVGATLE
TVHFGKLDFG ETAVLDRFYN ADIAVVEMSD AFRQPSLFYH LGVRESFSMA NNIILYCDNN
SDSLQSLKEI ICQKNTMCTG NYTFVPYMIT PHNKVYCCDS SFMKGLTELM QPNFELLLGP
ICLPLVDRFI QLLKVAQASS SQYFRESILN DIRKARNLYT GKELAAELAR IRQRVDNIEV
LTADIVINLL LSYRDIQDYD SIVKLVETLE KLPTFDLASH HHVKFHYAFA LNRRNLPGDR
AKALDIMIPL VQSEGQVASD MYCLVGRIYK DMFLDSNFLD TESRDYGASW FKKAFESEPS
LQSGINYAVL LLAAGHQFES SFELRKVGVK LSSLLGKKGN LEKLQSYWEV GFFLGASVLA
NDHMRVIQAS EKLFKLKTPA WYLKSIVETI LIYKHFVKLT TEQPVAKQEL VDFWMDFLVE
ATKTDVTVVR FPVLILEPTK IYQPSYLSIN NEVEEKTISI WHVLPDDKKG IHEWNFSASS
VRGVSISKFE ERCCFLYVLH NSDDFQIYFC TELHCKKFFE MVNTITEEKG RSTEEGDCEG
DSLEYDYEYD ENGDRVVLGK GTYGIVYAGR DLSNQVRIAI KEIPERDSRY SQPLHEEIAL
HKHLKHKNIV QYLGSFSENG FIKIFMEQVP GGSLSALLRS KWGPLKDNEQ TIGFYTKQIL
EGLKYLHDNQ IVHRDIKGDN VLINTYSGVL KISDFGTSKR LAGINPCTET FTGTLQYMAP
EIIDKGPRGY GKAADIWSLG CTIIEMATGK PPFYELGEPQ AAMFKVGMFK VHPEIPESMS
AEAKAFILKC FEPDPDKRAC ANDLLIDEFL KVSSKKKKTQ PKLSALSAGS NEYLRSISLP
VPVLVEDTSS SSEYGSVSPD TELKVDPFSF KTRAKSCGER DVKGIRTLFL GIPDENFEDH
SAPPSPEEKD SGFFMLRKDS ERRATLHRIL TEDQDKVVRN LMESLAQGAE EPKLKWEHIT
TLIASLREFV RSTDRKIIAT TLSKLKLELD FDSHGISQVQ VVLFGFQDAV NKVLRNHNIK
PHWMFALDSI IRKAVQTAIT ILVPELRPHF SLASESDTAD QEDLDAEDER EEQPSNQTVQ
RPHAVIEDAV ATSGVSTLSS TVSHDSQNAH RSLNVQLGRM KIETNRLLEE LVQKEKELQA
LLHQAIEEKD HEIKHLKLKS QPIDIPGVPV CHRDSLGTNA EESELAEWLR EKGADEDTIS
RFLAEDYSLE DVLYYVTRDD LKCLRLRGGI LCTLWKAITD FRDKQT
//