ID W5KIB7_ASTMX Unreviewed; 1261 AA.
AC W5KIB7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 5 {ECO:0000313|Ensembl:ENSAMXP00000007329.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000007329.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000007329.2}
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};
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DR AlphaFoldDB; W5KIB7; -.
DR Ensembl; ENSAMXT00000007329.2; ENSAMXP00000007329.2; ENSAMXG00000007103.2.
DR eggNOG; KOG4279; Eukaryota.
DR GeneTree; ENSGT00940000159155; -.
DR HOGENOM; CLU_003687_1_0_1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000007103; Expressed in olfactory epithelium and 14 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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 PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000018467}.
FT DOMAIN 646..904
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1144..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1261 AA; 141456 MW; 009B1149A91D3559 CRC64;
MNPEPECVSL PVPCREDCSR PAVPAAGTFW QDASSAVAAA AAGVIAGCPA ESGLGAGLGG
LLTPGKCKNR RASVAYVLNS ETGAESMALQ CLRDACEAVG TALEIVLFGK LDFGETAVLD
RFYNADIAVV EMTDAFRQPS LFYHLGVRES FSMANNIILY CDSNSDSLQS LQTCAANYLF
IPYMVTPQNK VYCCESSLMK GLSELMQPSF EALLGPICMP LLDRLIQILT VTQTSSCQYF
RETILNEIRK ARELYTGAEL AAELGRIQQR LDNVECLSAD IVINLLLSYR DIQDYESIVK
LVETLEKLPT FDPVANPHVK FHYAFALNRR NQPGDRPKAL DIMLPLVESE EQVASDIYCL
VGRIYKDMFL DSHFTDTESR DSSIQWFRRG FESEPTLHSG INYAVLLLAA GHQFDSSFEL
RKVGVKLSSL LGKKGSLDKL QSYWDVGFFL GASILACDNT RVIQASEKLF KLKAPVWYLC
SLVETILIYQ HFRKPSSEPP GPRQELVDFW MDFMVEATKK DVSSVRFPVL ILEPTKVYQP
SYLSINNDVE ENTLSIWHVA PDDKNKGIHE WNFSAASVRG VSISKFDERS SFLYVVNNSE
DFQIYFCTEM HCKRFCELVN SLTEETWRGP DEAECDSEYD YEYDEHGERV VLGKGTFGVV
YAGRDLSNQV RLAIKEIPER DSRYSQPLHE EIALHKHLKH KNIVQYLGSI SENGFIKIFM
EQVPGGSLSA LLRSKWGPLK NNEPTIGFYT KQILEGLKYL HDNQIAHRDI KGDNVLINTY
SGVLKISDFG TSKRLAGINP CTETFTGTLQ YMAPEIIDKG PRGYGKPADI WSLGCTIIEM
ATGKPPFYEL GEPQAAMFKV GMFKIHPEIP DSMSSEAKAF ILRCFEPDPD LRATANELLT
HEFLTVTSRK KKPFFYALFG AEYLRSISLP VPVVVEDTSS SSEYGSVSPD NELNTNPFLF
KPSTKCYSER EVKGHRSLFL SIPVEQFEDH SAPPSPEEKD AGFFMLRKDS ERRATLHRIL
TEDKDKIVIN LQEALTQGSE ETKLKHEHIS ALVASLGEFV RMADRKIIAN TLSQLKLELD
FDSTAISQLQ VALFGFQDAL NKVLRNHNIK PHWMFALDNI IRKAVQTAIT ILVPELRPHF
SLASESDAAD QEDDDDDDDA VPHGSPTHKN RAPPTASHDD TVATSGVSTL SSTVSHESHT
AQHSVSMELG RMKLETNRLL EELLEREREY QCILQQVLDE KEQEIKLLKM RSEPIGQSLF
I
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