ID A0A3B3RIZ4_9TELE Unreviewed; 1021 AA.
AC A0A3B3RIZ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:ENSPKIP00000018409.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000018409.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000018409.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3B3RIZ4; -.
DR Ensembl; ENSPKIT00000036243.1; ENSPKIP00000018409.1; ENSPKIG00000003884.1.
DR GeneTree; ENSGT00940000156449; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C: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:UniProtKB-EC.
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; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF103; RECEPTOR PROTEIN SERINE_THREONINE KINASE; 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; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022527}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 181..503
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 581..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 112036 MW; C914A42589A48841 CRC64;
CLAGQLVVFK VPQFKWSLSS VPVCAAAPNE ERECAFYDHQ QQLDEQHVDG VGHVLRENTT
VRCVQESRCY GLWEKAHDGG IRLVKQGCWA HVSDQQDCHD DRCVVTTTPL LIQNGTYRFC
CCSSNMCNLN FTEDFPLFGP TSTQPLYPQP LYREEAIVIA LAAVSLVAVL IVAIILGFRV
LTGDRKQGLH NLDKMEAAAS EPSLDLDSLK LLEPTFSGSL DERPVAVKVF NYTNRQNFVN
ERAIYRVLSQ EHDNIARFII GDERMTADGR MEYFLVMEYY PHGSLSQYLS LHTGDWVSCC
RLAHSVTRGL AYLHTELMPG DTYKPAVSHR DLNSRNVLVK NDGTCVISDF GLSMKLTGNR
LTRPGEEENA AISEVGTIRY MAPEVLEGAV NLRDCESALK QVDMYALGLI YWEIFMRCVD
LFPGEAVPDY QMAFQAEAGN HPSFEDMQVL VSREKQRPKF PEAWKENSLA VRSLKETVED
CWDQDAEARL TAQCAEERMA ELLVIWDRNK SVSPTVNPMS TAVQNERNLS HSRRVAKMGP
YPDFSTSSYI EDHETMVKNL PSDLSNSGEK NRNSINYERQ QAQARLPSPE TGGPSLSTTS
TTSTTTTTTA TTTGLMSGTT MATISESDCP DNGPANGMPV CLQLTEEDLE TTKLDPKEVD
KNLKESSDEN LMEHSQKQFS APDPLSSGSS NLLYPLIKLA AEVSGANGTG GLVQADPAVP
AGIACDPPAA VFPLPKQQNL PKRPSSLPLN TKNPAKDSSL RLRFSKLGKS NLKQVETGVA
KINTSSGAEP HLVMVTNHGQ GSRGTGNGYA GLSSSRGTQY GNVNPAGPQV DGTAPLLQTQ
LSGEDNRLNI NCSPDEHEPL LRGEQPAARE RQHASRPNTN NNNSNGNGQD DVESQEKPVL
RPPKPRRPER PNSLDLSVTT LGCSSAFGEG TLQDEKAGSG EKIKRRVKTP YSLKGWRPST
WVISTGSLDA EVNNNHRSMS FRESQPRSTG GRPKLSTALV PQGAGTSAPT LTSEPHNITY
L
//
