ID H2SS87_TAKRU Unreviewed; 978 AA.
AC H2SS87;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 24-JAN-2024, entry version 72.
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:ENSTRUP00000015274.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000015274.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000015274.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000015274.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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; H2SS87; -.
DR STRING; 31033.ENSTRUP00000061028; -.
DR Ensembl; ENSTRUT00000015343.3; ENSTRUP00000015274.3; ENSTRUG00000006256.3.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000156449; -.
DR TreeFam; TF314724; -.
DR Proteomes; UP000005226; Chromosome 8.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR017441; Protein_kinase_ATP_BS.
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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 156..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..512
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 525..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 978 AA; 106987 MW; C0547ED97FBDE915 CRC64;
APPFPRNPTP SLPMNSAQIS VFPAAQGEER ECAFTDQQQQ WEVERMAGGE GRISPENTTV
RCGKGSHCFG LWEKSPPGEV RLVKQGCWTH LGDHQGCRDD RCVVTNLPPQ IQNGTYHFCC
CGSDMCNVNF TEDFPQPSPT TAQPIYSRTL GYEETVIITV ATVSVLAVLA VAAFFGYRMM
HGDGKQGLHN LNMMEAAGSE SSLDLDNLKL LELIGRGRYG TVYCGSLDER PVAVKVFTAT
NRQNFLNECS IYRLPLLEHD NIARFVAADE RTGSEGRTEY LLVMEYYPHG SLNRYLSVQT
NDWVSSCRLA HSVTRGLAYL HTELFKGDLY KPAVSHRDLN SRNVLVKADG TCVIIDFGLS
MKLTGNRPAR HGEEENAAIS EVGTIRYMAP EVLEGAVNLR DCESALKQVD MYALGLLYWE
TFMRCTDLFP GEAVPEYQMA FQAETEAGNH PTFEDMQVLV SREKQRPKFP EAWKENSLAV
RSLKETMEDC WDQDAEARLT AQCAEERLAE LLLIWDRSKS VSPTLNPMST TLHNERNRMT
PKTGTYTDHP STYIEEHDGV AKNAQGDNTS SVTGRAGTGT GERNRNSINQ ERQQQANARL
PSPEGSSTSM GLRGSPSTST TTTTIISESE GPVGVATVPA CLHLTQEDLE TTKLDPKEVD
KNLKESSDEN LMEHSQKQFC SPDPLSPGSS SLLYPLIKMA TEASGVSDPA ASMPATIFPL
PKQQNLPKRP SSLQLRTKPT KKESSSSSLR FKFGRSGKSN LRQVEGSKIN IGSGAGTNVA
ADAQESTSTN NTPALREVHL NGNINGVVNG HANAGIPPMP SGGMASFGGT GTAQSDPASS
RTDDGHLSLG TITASPDEHE PLLSREREQL DRRDAPSSVA ALRSARPNTN NNNRSAPFVR
NVILIKVLSC LPGVQPDAVL EGAGEKIKKR VKTPYSLKKW RPTTWVISTD ARGPEVNNNG
SAHVLPVPTT TMVSKRKR
//