ID A0A3B3SWL9_9TELE Unreviewed; 543 AA.
AC A0A3B3SWL9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN Name=ACVR2B {ECO:0000313|Ensembl:ENSPKIP00000035064.1};
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:ENSPKIP00000035064.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000035064.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30; Evidence={ECO:0000256|ARBA:ARBA00023945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC Evidence={ECO:0000256|ARBA:ARBA00023948,
CC ECO:0000256|RuleBase:RU361271};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU361271};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU361271};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}.
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DR AlphaFoldDB; A0A3B3SWL9; -.
DR STRING; 1676925.ENSPKIP00000035064; -.
DR Ensembl; ENSPKIT00000015989.1; ENSPKIP00000035064.1; ENSPKIG00000014125.1.
DR GeneTree; ENSGT00940000156210; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF70; ACTIVIN RECEPTOR TYPE-2B; 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 PRINTS; PR00653; ACTIVIN2R.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 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|RuleBase:RU361271};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000256|RuleBase:RU361271};
KW Magnesium {ECO:0000256|RuleBase:RU361271};
KW Manganese {ECO:0000256|RuleBase:RU361271};
KW Membrane {ECO:0000256|RuleBase:RU361271};
KW Metal-binding {ECO:0000256|RuleBase:RU361271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361271};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361271};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU361271};
KW Transmembrane {ECO:0000256|RuleBase:RU361271};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361271}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..543
FT /note="Serine/threonine-protein kinase receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017349525"
FT TRANSMEM 169..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361271"
FT DOMAIN 221..509
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 543 AA; 61452 MW; B4F5925EBFA664BC CRC64;
MPKHFQHVTR ISVAICWFFL GSLRPDRFPD PTPSPPVPVL TSPARSFPGQ SHGDTETRVC
VFYNGSWEVE KTNQSGVERC EGERDKRSHC YASWRNTSGT IELVRKGCWL DDFNCYDRQE
CVATEENPQV FFCCCEGNYC NERFTHMPDA NGTPVKIRPP PPTPSLLNVL VYSLLPITVL
SMAMLLAFWM YRHRKPPYGQ VDISEDPGPP PPSPLAGLKP LQLLEIKARG RFGCVWKAQL
LNEYVAVKIF PIQDKQSWQN EWDIFITPGM KHESILRYIA AEKRGTNLEM ELWLITEFHE
KGSLTDYLKG NVVSWNDLCH VAETMSRGLA YLHEDVPRCK GEGPKPAIAH RDFKSKNVML
KGDLSAVIGD FGLAVRFEPG KPPGDTHGQV GTRRYMAPEV LEGAINFQRD AFLRIDMYAM
GLVLWELVSR CKAADGPVDE YMLPFEEEIG QHPSLEDLQE VVVHKKMRPS FKDCWLKHAG
LSQMCETIEE CWDHDAEARL SAGCVEERIN QISRQSNAPT SDCLVSMVTS LTNVDLPSKE
SSI
//
