ID A0A2K6P1L9_RHIRO Unreviewed; 1002 AA.
AC A0A2K6P1L9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN Name=BMPR2 {ECO:0000313|Ensembl:ENSRROP00000010422.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000010422.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000010422.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605}.
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DR AlphaFoldDB; A0A2K6P1L9; -.
DR STRING; 61622.ENSRROP00000010422; -.
DR Ensembl; ENSRROT00000034520.1; ENSRROP00000010422.1; ENSRROG00000029610.1.
DR GeneTree; ENSGT00940000156449; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0016362; F:activin receptor activity, type II; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036122; F:BMP binding; IEA:Ensembl.
DR GO; GO:0098821; F:BMP receptor activity; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0003176; P:aortic valve development; IEA:Ensembl.
DR GO; GO:0060413; P:atrial septum morphogenesis; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR GO; GO:0003197; P:endocardial cushion development; IEA:Ensembl.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0060426; P:lung vasculature development; IEA:Ensembl.
DR GO; GO:0001946; P:lymphangiogenesis; IEA:Ensembl.
DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0003183; P:mitral valve morphogenesis; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0003252; P:negative regulation of cell proliferation involved in heart valve morphogenesis; IEA:Ensembl.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IEA:Ensembl.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0003177; P:pulmonary valve development; IEA:Ensembl.
DR GO; GO:0014916; P:regulation of lung blood pressure; IEA:Ensembl.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IEA:Ensembl.
DR GO; GO:0003186; P:tricuspid valve morphogenesis; IEA:Ensembl.
DR GO; GO:0060841; P:venous blood vessel development; IEA:Ensembl.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000233200};
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};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 144..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..464
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 557..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..928
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 1002 AA; 111270 MW; 216FE3DF2EB3D1C8 CRC64;
KYKISQPWWH MPVMPATQEA ENQERLCAFK DPYQQDLGIG ESRISHENGT ILCSKGSTCY
GLWEKSKGDI NLVKQGCWSH IGDPQECHYE ECVVTTTPPS IQNGTYRFCC CSTDLCNVNF
TENFPPPDTT PLSPPHSFNR DETIIIALAS VSVLTVLIVA LCFGYRMLTG DRKQGLHSMN
MMEAAASEPS LDLDNLKLLE LIGRGRYGAV YKGSLDERPV AVKVFSFANR QNFINEKNIY
RVPLMEHDNI ARFIVGDERV TADGRMEYLL VMEYYPNGSL CKYLSLHTSD WVSSCRLAHS
VTRGLAYLHT ELPRGDHYKP AISHRDLNSR NVLVKNDGTC VISDFGLSMR LTGNRLVRPG
EEDNAAISEV GTIRYMAPEV LEGAVNLRDC ESALKQVDMY ALGLIYWEIF MRCTDLFPGE
SIPEYQMAFQ TEVGNHPTFE DMQVLVSREK QRPKFPEAWK ENSLTLKSEV SNLERQFIIN
VHSQCDTFFL SLSNLSHNRR VPKIGPYPDY SSSSYIEDSI HHTDNIVKNI SSEHSMSSTP
LTIGEKNRNS INYERQQAQA RIPSPETSVT SLSTNTTTTN TTGLTPSTGM TTISEMPYPD
ETNLHATNVA QSIGPTPVCL QLTEEDLETN KLDPKEVDKN LKESSDENLM EHSLKQFSGP
DPLSSTSSSL LYPLIKLAVE ATGQQDFTQA ANGQACLIPD VLPTQIYPLP KQQNLPKRPT
SLPLNTKNST KEPRLKFGSK HKSNLKQVET GVAKMNTINA AEPHVVTVTM NGVAGRNHSV
NSHAATTQYA NGTVPSGQTT NIVTHRAQEM LQNQFIGEDT RLNINSSPDE HEPLLRREQQ
AGHDEGVLDR LVDRRERPLE GGRTNSNNNN SNPCSEQDVL TQGVPSTVAD PGPSKPRRAQ
RPNSLDLSAT NVLDGSSIQI GESTQDGKSG SGEKIKKRVK TPYSLKRWRP STWVISTESL
DCEVNNNGSN RAVHSKSSTA VYLAEGGTAT TMVSKDIGMN CL
//
