ID H9BFG7_RAT Unreviewed; 1493 AA.
AC H9BFG7;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 1 {ECO:0000313|EMBL:AFD32168.1};
DE EC=2.7.11.25 {ECO:0000313|EMBL:AFD32168.1};
GN Name=Map3k1 {ECO:0000313|EMBL:AFD32168.1, ECO:0000313|RGD:620966};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AFD32168.1};
RN [1] {ECO:0000313|EMBL:AFD32168.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFD32168.1};
RA Eppinger M., Nur H.A., Sengamalay N., Hine E., Su Q., Daugherty S.C.,
RA Young S., Sadzewicz L., Tallon L., Cebula T.A., Ravel J., Colwell R.R.;
RT "Genome sequence of Vibrio cholerae HC-64A1.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFD32168.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFD32168.1};
RX PubMed=22993404; DOI=10.1158/0008-5472.CAN-12-0748;
RA DenDekker A.D., Xu X., Vaughn M.D., Puckett A.H., Gardner L.L.,
RA Lambring C.J., Deschenes L., Samuelson D.J.;
RT "Rat Mcs1b Is Concordant to the Genome-Wide Association-Identified Breast
RT Cancer Risk Locus at Human 5q11.2 and MIER3 is a Candidate Cancer
RT Susceptibility Gene.";
RL Cancer Res. 72:6002-6012(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; JQ013733; AFD32168.1; -; mRNA.
DR RGD; 620966; Map3k1.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16494; RING-CH-C4HC3_ZSWM2; 1.
DR CDD; cd06630; STKc_MEKK1; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF21040; CEP104-like_TOG; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04434; SWIM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFD32168.1};
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}; Transferase {ECO:0000313|EMBL:AFD32168.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 328..356
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 433..482
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1224..1489
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1493 AA; 161341 MW; FB89B5BB82F0225B CRC64;
MAAAAGDRAS SSGFPGAAAA SPEAGGGGGA LQGSGAPAAG AGLLRETGSA GRERADWRRQ
QLRKVRSVEL DQLPEQPLFL TASPPCPSTS PSPEPADAAA GASGFQPAAG PPPPGAASRC
GSHSAELAAA RDSGARSPAG AEPPSAAAPS GREMENKETL KGLHKMDDRP EERMIREKLK
ATCMPAWKHE WLERRNRRGP VVVKPIPIKG DGSEMSNLAA ELQGEGQAGS AAPAPKGRRS
PSPGSSPSGR SGKPESPGVR RKRVSPVPFQ SGRITPPRRA PSPDGFSPYS PEETSRRVNK
VMRARLYLLQ QIGPNSFLIG GDSPDNKYRV FIGPQNCSCG RGTFCIHLLF VMLRVFQLEP
SDPMLWRKTL KNFEVESLFQ KYHSRRSSRI KAPSRNTIQK FVSRMSNCHT LSSSSTSTSS
SENSIKDEEE QMCPICLLGM LDEESLTVCE DGCRNKLHHH CMSIWAEECR RNREPLICPL
CRSKWRSHDF YSHELSSPVD SPTSLRGVQQ PSSPQQPVAG SQRRNQESNF NLTHYGTQQI
PPAYKDLAEP WIQAFGMELV GCLFSRNWNV REMALRRLSH DVSGALLLAN GESTGTSGGG
SGGSLSAGAA SGSSQPSISG DVVEACCSVL SIVCADPVYK VYVAALKTLR AMLVYTPCHS
LAERIKLQRL LRPVVDTILV KCADANSRTS QLSISTLLEL CKGQAGELAV GREILKAGSI
GVGGVDYVLS CILGNQAESN NWQELLGRLC LIDRLLLEFP AEFYPHIVST DVSQAEPVEI
RYKKLLSLLA FALQSIDNSH SMVGKLSRRI YLSSARMVTT VPALFSKLVT MLSASGSSHF
ARMRRRLMAI ADEVEIAEVI QLGSEDTLDG QQDSSQALAP PRYPESSSLE HTAHVEKTGK
GLKATRLSAS SEDISDRLAG VSVGLPSSAT TEQPKPTVQT KGRPHSQCLN SSPLSPPQLM
FPAISAPCSS APSVPAGSVT DASKHRPRAF VPCKIPSASP QTQRKFSLQF QRTCSENRDS
EKLSPVFTQS RPPPSSNIHR PKPSRPVPGS TSKLGDASKN SMTLDLNSAS QCDDSFGSGS
NSGSAVIPSE ETAFTPAEDK CRLDVNPELN SSIEDLLEAS MPSSDTTVTF KSEVAVLSPE
KAESDDTYKD DVNHNQKCKE KMEAEEEEAL AIAMAMSASQ DALPIVPQLQ VENGEDIIII
QQDTPETLPG HTKAKQPYRE DTEWLKGQQI GLGAFSSCYQ AQDVGTGTLM AVKQVTYVRN
TSSEQEEVVE ALREEIRMMS HLNHPNIIRM LGATCEKSNY NLFIEWMAGG SVAHLLSKYG
AFKESVVINY TEQLLRGLSY LHENQIIHRD VKGANLLIDS TGQRLRIADF GAAARLASKG
TGAGEFQGQL LGTIAFMAPE VLRGQQYGRS CDVWSVGCAI IEMACAKPPW NAEKHSNHLA
LIFKIASATT APSIPSHLSP GLRDVALRCL ELQPQDRPPS RELLKHPVFR TTW
//
