ID A0A3B4DQC2_PYGNA Unreviewed; 513 AA.
AC A0A3B4DQC2;
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=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000025149.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000025149.1}
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:ARBA00036790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674;
CC Evidence={ECO:0000256|ARBA:ARBA00036790};
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:ARBA00036287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881;
CC Evidence={ECO:0000256|ARBA:ARBA00036287};
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 RefSeq; XP_017539967.1; XM_017684478.1.
DR AlphaFoldDB; A0A3B4DQC2; -.
DR STRING; 42514.ENSPNAP00000025149; -.
DR Ensembl; ENSPNAT00000008342.1; ENSPNAP00000025149.1; ENSPNAG00000010092.1.
DR GeneID; 108412453; -.
DR CTD; 553359; -.
DR GeneTree; ENSGT00940000157233; -.
DR OMA; YNMMLPP; -.
DR OrthoDB; 3900892at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 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:SF64; ACTIVIN RECEPTOR TYPE-2A; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SMART; SM00220; S_TKc; 1.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|RuleBase:RU361271};
KW Magnesium {ECO:0000256|RuleBase:RU361271};
KW Manganese {ECO:0000256|RuleBase:RU361271};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..513
FT /note="Serine/threonine-protein kinase receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017436649"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361271"
FT DOMAIN 192..486
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 513 AA; 57564 MW; 7C9804CB1518CC83 CRC64;
MGPATKLAFG VFLISCSSGA ILGRSETQEC VLYNYNPSSE NQGNRSIEPC VGDKDKRLHC
FATWRNVSGT VAVVKQGCWL DDVNCYDSTE CVEKKEDPEV FFCCCEGNMC NEKFYHNPDA
QAVQTTSNPF TQKPPLFNTL LYSLVPIMGI AAIVLLSFWM YRHHKLAYPP VLVPTQDPGP
MPPSPILGQK PLQLLEIKAR GRFGCVWKAQ LLSDYVAVKI FPIQDKQSWQ NEYEIYNLPG
MRHENILHFM GAEKRGANLD IELWLITAYH EKGSLSDYLK ANVVTWNELC HIAQTMARGL
AYLHADIPGL RDGHKPAIAH RDVKSKNVLL KANLTACVAD FGLALRFEAG KSAGDTHGQV
GTRRYMAPEV LEGAINFQRD AFLRIDMYAV GLVLWELASR CTAADGPVDE YMLPFEEEVG
QHPTLEDMQE VVVHKKLRPT LRECWQKHPG LSMLCETIEE CWDHEAEARL SAGCVEERVV
QMHRQTSISG PEEIVTVVTM VTNVDFPPKE SSL
//
