MK15_XENLA
ID MK15_XENLA Reviewed; 586 AA.
AC Q501Q9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Mitogen-activated protein kinase 15 {ECO:0000250|UniProtKB:Q8TD08};
DE EC=2.7.11.24;
GN Name=mapk15 {ECO:0000312|Xenbase:XB-GENE-1010341};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J;
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH DVL2.
RX PubMed=25823377; DOI=10.1038/ncomms7666;
RA Miyatake K., Kusakabe M., Takahashi C., Nishida E.;
RT "ERK7 regulates ciliogenesis by phosphorylating the actin regulator CapZIP
RT in cooperation with Dishevelled.";
RL Nat. Commun. 6:6666-6666(2015).
CC -!- FUNCTION: Atypical MAPK protein that regulates ciliogenesis by
CC phosphorylating rcsd1 through its binding with dvl2.
CC {ECO:0000269|PubMed:25823377}.
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=2.7.11.24;
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=2.7.11.24;
CC -!- SUBUNIT: Interacts with dvl2. {ECO:0000269|PubMed:25823377}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:25823377}. Cell projection, cilium
CC {ECO:0000269|PubMed:25823377}. Cell junction
CC {ECO:0000269|PubMed:25823377}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the hemisphere. Highly expressed in
CC ciliated tissues. At stage 12 (late gastrula), detected in the dorsal
CC involuting marginal zone. Expressed in the gastrocoel roof plate (GRP)
CC at stage 16 (neurula stage;). At stage 25 (early tailbud stage) and
CC stage 33/34 (late tailbud stage), expressed in the floor plate, cloaca
CC and ear vesicle. At stage 33/34 (late tailbud stage), detected in
CC nephrostomes. Expressed in the epidermis at stage 13 and thereafter.
CC Specifically expressed in multiciliated cells (MCCs) on the epidermis.
CC {ECO:0000269|PubMed:25823377}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in reduced head
CC structures, close-set eyes and dorsal curvature. and loss of fin. At
CC higher dose Morpholino knockdown results in the inhibition of antero-
CC posterior axis elongation and breakdown of the epidermis, which
CC resulted in exposure of the inner tissues to the outer environment and
CC causes a loss of epidermal cells such as small secretory cells.
CC {ECO:0000269|PubMed:25823377}.
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DR EMBL; CM004476; OCT77367.1; -; Genomic_DNA.
DR EMBL; BC095915; AAH95915.1; -; mRNA.
DR RefSeq; NP_001089435.1; NM_001095966.1.
DR AlphaFoldDB; Q501Q9; -.
DR SMR; Q501Q9; -.
DR STRING; 8355.Q501Q9; -.
DR DNASU; 734485; -.
DR GeneID; 734485; -.
DR KEGG; xla:734485; -.
DR CTD; 734485; -.
DR Xenbase; XB-GENE-1010341; mapk15.L.
DR OMA; PDQEWTR; -.
DR OrthoDB; 741207at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 734485; Expressed in testis and 12 other tissues.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell projection; Cytoplasm; Cytoskeleton;
KW Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..586
FT /note="Mitogen-activated protein kinase 15"
FT /id="PRO_0000444600"
FT DOMAIN 14..305
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 354..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 586 AA; 64989 MW; 64C99B24017FF4A8 CRC64;
MSGPEVEDHI SQKYDIKKRL GKGAYGIVWK AIDRKSGEIV AVKKIFDAFR NRTDAQRTFR
EIMFLQEFGE HPNIIKLLNV IRAQNDKDIY LVFEHMETDL HAVIKKGNLL KDIHMRYILY
QLLKATKFIH SGNVIHRDQK PSNILLDGDC LVKLCDFGLA RSLYQIQEDV GNPALTEYVA
TRWYRAPEIL LASNRYTKGV DMWSVGCILG EMLLGKPLFP GTSTINQIER IMSIIEPPTH
EDIVSIKSEY GASVISRMSS KHKVPMAELF PASCPREALD LLSKLLVFNP GKRLTAEEAL
EHPYVSRFHS PAREPALDYD VILPVDDDIQ LSVAEYRNKL YEMILERKMN IRRQKRESLK
ESVSSSANGA KDRQDTDTSK TPAPPAGTNP APQPTSSTVP QRAAIAAPNQ PPAQKDSTQQ
SPKIKAPSSN PITHSTTHGS TEDWRTSHNK KAGQQGAAGT TAQEVRKEVE SRSRTAPIGR
ARSFSHSQQA RAAATNSALI RKDAPPTGTV SVAAVSARLN QRTAPIQGRD PRSAPRFGRK
MFQGKTNVES AGDPKATLHS YTQAYGTISK AALQNLPQQG GAFKGK
