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Entry: O42338_XENLA
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Original site: O42338_XENLA 
ID   O42338_XENLA            Unreviewed;       527 AA.
AC   O42338;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   08-MAY-2019, entry version 134.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   Name=LOC397711 {ECO:0000313|EMBL:AAH70551.1};
GN   ORFNames=XELAEV_18034945mg {ECO:0000313|EMBL:OCT71967.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:BAA22437.1};
RN   [1] {ECO:0000313|EMBL:BAA22437.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Suzuki A., Shioda N., Ueno N.;
RT   "Bone morphogenetic protein acts as a ventral mesoderm modifier in
RT   early Xenopus embryos.";
RL   Dev. Growth Differ. 37:581-588(1995).
RN   [2] {ECO:0000313|EMBL:AAH70551.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH70551.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000313|Proteomes:UP000186698};
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.,
RA   Quigley I., Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B.,
RA   Simakov O., Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T.,
RA   Watanabe M., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S.,
RA   van Kruijsbergen I., Shu S., Carlson J., Kinoshita T., Ohta Y.,
RA   Mawaribuchi S., Jenkins J., Grimwood J., Schmutz J., Mitros T.,
RA   Mozaffari S.V., Suzuki Y., Haramoto Y., Yamamoto T.S., Takagi C.,
RA   Heald R., Miller K., Haudenschild C., Kitzman J., Nakayama T.,
RA   Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., Karimi K.,
RA   Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., Shendure J.,
RA   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.,
RA   Veenstra G.J., 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   [4] {ECO:0000313|EMBL:OCT71967.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J {ECO:0000313|EMBL:OCT71967.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OCT71967.1};
RA   Session A., Uno Y., Kwon T., Chapman J., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Putnam N., Stites J., Van Heeringen S.,
RA   Quigley I., Heinz S., Hellsten U., Lyons J., Suzuki A., Kondo M.,
RA   Ogino H., Ochi H., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.,
RA   Van Kruijsbergen I., Mozaffari S., Shu S., Schmutz J., Jenkins J.,
RA   Grimwood J., Carlson J., Mitros T., Simakov O., Heald R., Miller K.,
RA   Haudenschild C., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Kinoshita T., Ohta Y., Mawaribuchi S., Suzuki Y., Haramoto Y.,
RA   Yamamoto T., Takagi C., Kitzman J., Shendure J., Nakayama T.,
RA   Izutsu Y., Robert J., Dichmann D., Flajnik M., Houston D.,
RA   Marcotte E., Wallingford J., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Jan Veenstra G., Fujiyama A., Harland R., Taira M., Rokhsar D.S.;
RT   "WGS assembly of Xenopus laevis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
CC         phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
CC         COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|SAAS:SAAS01128400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-threonine + ATP = [receptor-
CC         protein]-O-phospho-L-threonine + ADP + H(+);
CC         Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-
CC         COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30; Evidence={ECO:0000256|SAAS:SAAS01128404};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|SAAS:SAAS00595019}.
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DR   EMBL; BC070551; AAH70551.1; -; mRNA.
DR   EMBL; D32066; BAA22437.1; -; mRNA.
DR   EMBL; CM004478; OCT71967.1; -; Genomic_DNA.
DR   RefSeq; NP_001081207.1; NM_001087738.1.
DR   RefSeq; XP_018079820.1; XM_018224331.1.
DR   RefSeq; XP_018079821.1; XM_018224332.1.
DR   RefSeq; XP_018079822.1; XM_018224333.1.
DR   GeneID; 397711; -.
DR   KEGG; xla:397711; -.
DR   KO; K04673; -.
DR   OrthoDB; 776697at2759; -.
DR   Proteomes; UP000186698; Chromosome 7l.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR003605; GS_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51256; GS; 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 {ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186698};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:BAA22437.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00138186};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00138220,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00488859,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    527       Receptor protein serine/threonine kinase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010503318.
FT   TRANSMEM    149    173       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      199    228       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      229    520       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   527 AA;  59786 MW;  BDAECE9DA566B408 CRC64;
     MRERLFIACF GALLLVIHTQ GQDFNILPHR TGMKSNSDPK KQENGVTLAP EDTLPFLNCY
     CSGYCPQNAV NNTCITNGQC FAMIEEDDHG DIILTSGCMK MEGSDFQCKD SPKALSRRTI
     ECCRTDFCNR DLEPTLSPKI SDGEYGLRFI ALIISLVVCL ILIVGFILII WIYKHKLHSQ
     RMLYNRNLDP DDAFIPAGES LKALIDISQS SGSGSGLPLL VQRTIAKQIQ MVRQIGKGRY
     GEVWMGKWRG EKVAVKVFFT AEEASWFRET EIYQTVLMRH ENILGFIAAD IKGTGSWTQM
     YLITEYHENG SLYDFLKCTT LDTRSLLKLA YSAACGLCHL HTEIYGTQGK PAIAHRDLKS
     KNILIKENWT CCIADLGLAV KFNSDTHEVD IPLNTRVGTK RYMAPEVLDE SLNKNHFQAY
     IMADIYSFSL IIWEMTRRCI TGGIVEEYQL PYYDMVPNDP SFEDMREVVC MKCLRPTVSN
     RWNSDECLRA VLKLMAECWA QNPASRLTAL RIKKTLAKMV ESQDVKI
//
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