M3K1B_PHYPA
ID M3K1B_PHYPA Reviewed; 764 AA.
AC A9RVK2;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 1b {ECO:0000305};
DE Short=PpMEKK1b {ECO:0000303|PubMed:27268428};
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:Q39008};
DE AltName: Full=MAP kinase kinase kinase 1b {ECO:0000303|PubMed:27268428};
GN Name=MEKK1b; ORFNames=PHYPADRAFT_24585 {ECO:0000312|EMBL:EDQ77074.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Gransden 2004 {ECO:0000303|PubMed:27268428};
RX PubMed=27268428; DOI=10.1105/tpc.15.00774;
RA Bressendorff S., Azevedo R., Kenchappa C.S., Ponce de Leon I., Olsen J.V.,
RA Rasmussen M.W., Erbs G., Newman M.A., Petersen M., Mundy J.;
RT "An innate immunity pathway in the Moss Physcomitrella patens.";
RL Plant Cell 28:1328-1342(2016).
RN [2] {ECO:0000312|EMBL:EDQ77074.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (PARTIAL).
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
CC -!- FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are
CC involved in pathogen defense. The pathway induces rapid growth
CC inhibition, cell wall depositions and accumulation of defense-related
CC transcripts. This protein is required for responses to chitin and acts
CC redundantly with MEKK1a. {ECO:0000269|PubMed:27268428}.
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:0000250|UniProtKB:Q39008};
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:0000250|UniProtKB:Q39008};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q39008}.
CC -!- INDUCTION: Up-regulated in response to chitosan.
CC {ECO:0000269|PubMed:27268428}.
CC -!- DISRUPTION PHENOTYPE: Reduced chitin-induced MPK phosphorylation.
CC Exhibits chitin-induced cell wall-associated depositions comparable to
CC wild-type. Reduced accumulation of PAL4 and CHS transcripts in response
CC to chitin. Double deletion mutant MEKK1a/MEKK1b does not phosphorylate
CC MPK and is unable to induce the depositions in response to chitin. The
CC growth of the double mutant is inhibited within 1 min after chitin
CC exposure as in wild-type. {ECO:0000269|PubMed:27268428}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDQ77074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS544920; EDQ77074.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001758252.1; XM_001758200.1.
DR AlphaFoldDB; A9RVK2; -.
DR SMR; A9RVK2; -.
DR STRING; 3218.PP1S31_252V6.1; -.
DR EnsemblPlants; Pp3c11_21820V3.1; PAC:32956884.CDS.1; Pp3c11_21820.
DR EnsemblPlants; Pp3c11_21820V3.2; PAC:32956885.CDS.1; Pp3c11_21820.
DR Gramene; Pp3c11_21820V3.1; PAC:32956884.CDS.1; Pp3c11_21820.
DR Gramene; Pp3c11_21820V3.2; PAC:32956885.CDS.1; Pp3c11_21820.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_000288_2_6_1; -.
DR InParanoid; A9RVK2; -.
DR OMA; IIDLPWF; -.
DR OrthoDB; 630495at2759; -.
DR Proteomes; UP000006727; Chromosome 11.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010200; P:response to chitin; IMP:UniProtKB.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..764
FT /note="Mitogen-activated protein kinase kinase kinase 1b"
FT /id="PRO_0000443377"
FT DOMAIN 431..684
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 554
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 437..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 459
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 764 AA; 83151 MW; 577DA7E6C41FEED9 CRC64;
MVEERGSSRS SRGGSWGSGE DGGSSHGGKG VPKLSRTVAK KIHKYDVSAD HSDYEDDGSV
HSTSSSGSRR NPLSKSIIQQ QSFRVGANFE EDLKTLYELI GVSKPADLAI SASDWQSRGK
SIAYSQPLSS PSLSQEHGEA SHSNDLKPSI IDFRSEAPAA SPRELPVAPV KLDAHERMTY
RSDYVNSQPQ NHYGRKNSPS QRSPPPESFP AFDSSPSRLG REGYGLHRMQ SDPVMPTLGA
LSPLGTGNAH PESAGSTATR RWSFDLVPGN HEGDYANMSQ VVRDNLPSAA VAMPKNGLVR
RSPIIRDPNR SNSSVSNPYA QRQYPNLAEE AESSAKPESS AIPDSSAMPE LPAKLESTAV
PELSAKPESN AKPESEPEQD SSVEARTEHY GSVRKSKIPS ALIIDKFEEP SIVSTGRSPG
VVSKRPPWDT WFKGDFIGSG TFGSVYEGID NNGMFFAVKE VSLKDQGKVG QEAIKQLEHE
IALLSDIQHP NIVQYLGTER DDEKLYIFLE LVSKGSLASL YKKYYFVYDQ VRAYTKQILS
GLKYLHDRKI IHRDIKCANI LVDTNGVVKL ADFGMAKQVD KLGLLKSFMG SAHWMAPEVV
NPKRQYNFLA DIWSLGCTVL EMATGDAPFG ELECHSVLWK VGNGEGPLIP DDLEDEMKDF
ISKCLEVTVG NRPTCDMLLT HPFITGEPMT GPVKLVPMPE LSTISEERSI DVSESPSIAT
SSQSGSSPSV AGDAVSPASV AVRPRSMRTL RSEFSMSSPE SIAS
