ID   D3ZG83_RAT              Unreviewed;       940 AA.
AC   D3ZG83;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 3.
DT   23-MAY-2018, entry version 70.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|PIRNR:PIRNR000556};
DE            EC=2.7.11.25 {ECO:0000256|PIRNR:PIRNR000556};
GN   Name=Map3k10 {ECO:0000313|Ensembl:ENSRNOP00000031328,
GN   ECO:0000313|RGD:1308381};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000031328, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000031328, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031328,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000031328}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000031328};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000213|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|PIRNR:PIRNR000556}.
CC   -!- ENZYME REGULATION: Homodimerization via the leucine zipper domains
CC       is required for autophosphorylation.
CC       {ECO:0000256|PIRNR:PIRNR000556}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000556}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000556}.
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DR   EMBL; AC120811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006228638.1; XM_006228576.3.
DR   UniGene; Rn.130504; -.
DR   STRING; 10116.ENSRNOP00000031328; -.
DR   iPTMnet; D3ZG83; -.
DR   PhosphoSitePlus; D3ZG83; -.
DR   PaxDb; D3ZG83; -.
DR   Ensembl; ENSRNOT00000034609; ENSRNOP00000031328; ENSRNOG00000023521.
DR   GeneID; 308463; -.
DR   CTD; 4294; -.
DR   RGD; 1308381; Map3k10.
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00900000140790; -.
DR   InParanoid; D3ZG83; -.
DR   OMA; ARAPWEP; -.
DR   OrthoDB; EOG091G0JNI; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000023521; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR   GO; GO:0004706; F:JUN kinase kinase kinase activity; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0007257; P:activation of JUN kinase activity; IBA:GO_Central.
DR   GO; GO:0008219; P:cell death; IMP:RGD.
DR   GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   CDD; cd12059; SH3_MLK1-3; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR015785; MAP3K10.
DR   InterPro; IPR035779; MLK1-3_SH3.
DR   InterPro; IPR016231; MLK1-4.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR43997:SF5; PTHR43997:SF5; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PIRSF; PIRSF000556; MAPKKK9_11; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000556,
KW   ECO:0000256|PIRSR:PIRSR000556-2};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000556};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000556,
KW   ECO:0000256|PIRSR:PIRSR000556-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000556};
KW   SH3 domain {ECO:0000256|PROSITE-ProRule:PRU00192};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000556}.
FT   DOMAIN       16     81       SH3. {ECO:0000259|PROSITE:PS50002}.
FT   DOMAIN       98    360       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   NP_BIND     104    112       ATP. {ECO:0000256|PIRSR:PIRSR000556-2}.
FT   COILED      391    412       {ECO:0000256|SAM:Coils}.
FT   COILED      424    444       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    222    222       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000556-1}.
FT   BINDING     125    125       ATP. {ECO:0000256|PIRSR:PIRSR000556-2}.
SQ   SEQUENCE   940 AA;  103060 MW;  B39EDB486730A42D CRC64;
     MEEEEGAAAR EWGATPAGPV WTAVFDYEAV GDEELTLRRG DRVQVLSQDC AVSGDEGWWT
     GQLPSGRVGV FPSNYVAPAA PAAPTDLQLP QEIPFHELQL EEIIGVGGFG KVYRALWRGE
     EVAVKAARLD PERDPAVTAE QVRQEARLFG ALQHPNIIAL RGACLSPPNL CLVMEYARGG
     ALSRVLAGRR VPPHVLVNWA VQVARGMNYL HNDAPVPIIH RDLKSINILI LEAIENHNLA
     DTVLKITDFG LAREWHKTTK MSAAGTYAWM APEVIRLSLF SKSSDVWSFG VLLWELLTGE
     VPYREIDALA VAYGVAMNKL TLPIPSTCPE PFARLLEECW DPDPHGRPDF GSILKQLEVI
     EQSALFQMPL ESFHSLQEDW KLEIQHMFDD LRTKEKELRS REEELLRAAQ EQRFQEEQLR
     RREQELAERE MDIVERELHL LMSQLSQEKP RVRKRKGNFK RSRLLKLREG SSHISLPSGF
     EHKITVQASP TLDKRKGSDG ASPPASPSII PRLRAIRLTP VDCGSSGGSG TWSRSGPPKK
     EELVGGKKKG RTWGPSSTLQ KERAGGEERL KALGEGSKQW SSSAPNLGKS PKHTPMAPGF
     ASLNEMEEFA EADEGNNVPP SPYSTPSYLK VPLPAEASPC AQPPWEPPAA TPSRPGHGAR
     RRCDLALLGC ATLLSAVGLG ADVAEARAGD GEEQRGWLDG LFFPRPGRFP RGLSPTGRPG
     GRREETAPGF GLAPSATLVS LSSVSDCNST RSLLRSDSDE AAPTAPSPPP SLLPPSPSTN
     PLVDVELESF KKDPRQSLTP THVTAAHAVS RGHRRTPSDG ALRQREPPEL TNHGPRDPLD
     FPRLPDPQAL FPTRRRPLEF PGRPTTLTFA PRPRPAASRP RLDPWKLVSF GRTLSISPPS
     RPDTPESPGP LSVQPTLLDM DMEGQSQDNT VPLCGAYGSH
//