ID   O42124_CHICK            Unreviewed;      1031 AA.
AC   O42124;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN   Name=BRK-3 {ECO:0000313|EMBL:BAA22057.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:BAA22057.1};
RN   [1] {ECO:0000313|EMBL:BAA22057.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryo {ECO:0000313|EMBL:BAA22057.1};
RX   PubMed=8951071;
RA   Kawakami Y., Ishikawa T., Shimabara M., Tanda N., Enomoto-Iwamoto M.,
RA   Iwamoto M., Kuwana T., Ueki A., Noji S., Nohno T.;
RT   "BMP signaling during bone pattern determination in the developing limb.";
RL   Development 122:3557-3566(1996).
RN   [2] {ECO:0000313|EMBL:BAA22057.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryo {ECO:0000313|EMBL:BAA22057.1};
RA   Nohno T.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|ARBA:ARBA00009605}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L77660; AAL40035.1; -; mRNA.
DR   EMBL; AB006785; BAA22057.1; -; mRNA.
DR   RefSeq; NP_001001465.1; NM_001001465.1.
DR   AlphaFoldDB; O42124; -.
DR   SMR; O42124; -.
DR   STRING; 9031.ENSGALP00000058326; -.
DR   PaxDb; 9031-ENSGALP00000013771; -.
DR   GeneID; 374147; -.
DR   KEGG; gga:374147; -.
DR   CTD; 659; -.
DR   VEuPathDB; HostDB:geneid_374147; -.
DR   InParanoid; O42124; -.
DR   TreeFam; TF314724; -.
DR   Reactome; R-GGA-201451; Signaling by BMP.
DR   Bgee; ENSGALG00000008459; Expressed in spermatocyte and 13 other cell types or tissues.
DR   ExpressionAtlas; O42124; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005024; F:transforming growth factor beta receptor activity; IBA:GO_Central.
DR   GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0002063; P:chondrocyte development; ISS:AgBase.
DR   GO; GO:0060350; P:endochondral bone morphogenesis; IMP:AgBase.
DR   GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISS:AgBase.
DR   GO; GO:0061036; P:positive regulation of cartilage development; IMP:AgBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:AgBase.
DR   CDD; cd14054; STKc_BMPR2_AMHR2; 1.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF63; BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-2; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:BAA22057.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:AAL40035.1};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        144..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          196..497
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          585..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1031 AA;  114639 MW;  EF6F7B53CC2D302E CRC64;
     MKSVTKNIFH SLSKAAQSEE RLCAFKDPYQ QDHGISESRI SQENGTILCM KGSTCYGLWE
     KTREGDIHLV KQGCWSHIGD PQECHFEECI VTTTPSLIQN GTYRFCCCST DLCNVNFTEN
     FPPPDPTDTT PYNSSHSFHR DETIVIVLAS VSVLAVLIAA LFFGYRMLAG DRKQGLHSMN
     MMEAAASEPS LDLDNLKLLE LIGRGRYGAV YKGSLDERPV AVKVFSFANR QNFVNERNIY
     RIPLMEHDNI ARFIVGDERF TADGRMEYLL VMEYYPNGSL CKYLSLHTSD WVSSCRLAHS
     ITRGLAYLHT ELPRGDHYKP AISHRDLNSR NVLVKNDGTC VISDFGLSMK LTGNRLVRPG
     EEDNAAISEV GTIRYMAPEV LEGAVNLRDC ESALKQVDMY ALGLIYWEIF MRCTDLFPGE
     SVPEYQMAFQ TEVGNHPTFE DMQVLVSREK QRPKFPEAWK ENSLAVRSLK ETIEDCWDQD
     AEARLTAQCA EERMAELMMI WERNKSVSPT VNPMSTAMQN ERNLSHHRRV SKIRPYPDYS
     SSSYIEDSIH HTDSIVKNIS SEHSMSTTPL TSGEKNRNSI NYERQQAQAR IPSPETSVTS
     LSTNTTTTNT TGLTPSTGMT TISEIPYSDE TNLHTTNVMQ PGGPTPVCLQ LTEEDLETNK
     LDPKEVDKNL KESSDENLME HSLKQFSGPD PLSSTSSSLL YPLIKLAVEV TGQQDFTQAS
     NGQACLIPDV PSAQVYPLPK QQNLPKRPTS LPLNTKNSTK EPRLKFGGKH KSNLKQVETG
     VAKMNTINAA EPHVVTVTMN GVAGRTHSIN SHAGTTQYAN GAVPSGQTAS SVAQRAQEML
     QNQFSGEDSR LNINSSPDEH EPLLRREQQV GHDEGVLDRL VDRRERQLDN GRTNVNNNNS
     NPCPVQDTAT LSIQNVARNP GQTQTRRAQR PNSLDLSATN SLDSSSMQLG DSSQDGKSGS
     GEKIKKRVKT PYSLKRWRPS TWVISTEPLH CEVNNNGGDR AVHSKSSTAV YLAEGGTATT
     MVSKDAGVNC L
//