ID A0A3M0L024_HIRRU Unreviewed; 434 AA.
AC A0A3M0L024;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=TGF-beta receptor type-2 {ECO:0000256|ARBA:ARBA00017567};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
DE AltName: Full=TGF-beta type II receptor {ECO:0000256|ARBA:ARBA00032053};
DE AltName: Full=Transforming growth factor-beta receptor type II {ECO:0000256|ARBA:ARBA00033122};
GN ORFNames=DUI87_04641 {ECO:0000313|EMBL:RMC18745.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC18745.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC18745.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC18745.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC18745.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000256|ARBA:ARBA00004285}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMC18745.1}.
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DR EMBL; QRBI01000096; RMC18745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0L024; -.
DR STRING; 333673.A0A3M0L024; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0009888; P:tissue development; IEA:UniProt.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
DR PANTHER; PTHR23255:SF51; TGF-BETA RECEPTOR TYPE-2; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF08917; ecTbetaR2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 156..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..434
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 414..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 434 AA; 48574 MW; A236573220DB3966 CRC64;
MPPPTPWLTS SGGKARDEGV NYYRRSTSQA SCSARRSLKT NLCKWCDSTA PACEEKVCYS
NCNLNSYCED PYEICVAIWR QDNESIRIST LCHNPQRPIE NLMVPNYNTS RCVMSHQPSE
DGIIYICGCV DEQECNDKLI FENHTNGYSM LQSKEVIPVA AISLLPPLLV AVMITVIFYL
CRTQKRRKRA KAWAGKQGQP PALLEQGKAT EREEKLSVLM DESPAGTSAG RRPAELLPIE
LDEMVGKGQF AEVWRAKLSR SHSGQYETVA VKIFPCEEYS SWKNESQIFT DSSLRHDSVL
QFLTAEDRGA GPRREYWLIT AYHSRGNLKD YLSRHVLSWM DLQKMAGSLV SGVAHLHSDY
TACGRPKIPI AHRDIKSTNV LVKNEQECVL CDFGIAIRLD PSLTVDDFAN SGQASMSCQP
SLEEPFAATP TSRG
//