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Database: UniProt
Entry: A0A3Q2V639_HAPBU
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ID   A0A3Q2V639_HAPBU        Unreviewed;       685 AA.
AC   A0A3Q2V639;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Activin receptor type-1 {ECO:0000256|ARBA:ARBA00039914};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
DE   AltName: Full=Activin receptor type I {ECO:0000256|ARBA:ARBA00041365};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000002743.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000002743.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane 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}.
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DR   RefSeq; XP_005918300.1; XM_005918238.2.
DR   RefSeq; XP_005918301.1; XM_005918239.2.
DR   RefSeq; XP_014187867.1; XM_014332381.1.
DR   AlphaFoldDB; A0A3Q2V639; -.
DR   Ensembl; ENSHBUT00000011579.1; ENSHBUP00000002743.1; ENSHBUG00000004035.1.
DR   GeneID; 102296235; -.
DR   GeneTree; ENSGT00940000164733; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd14142; STKc_ACVR1_ALK1; 1.
DR   Gene3D; 2.10.60.10; CD59; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR003605; GS_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF69; ACTIVIN RECEPTOR TYPE-1; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF01064; Activin_recp; 3.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 3.
DR   PROSITE; PS51256; GS; 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}; Kinase {ECO:0000256|ARBA:ARBA00022527};
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:UP000264840};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..685
FT                   /note="Activin receptor type-1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018662374"
FT   TRANSMEM        300..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          354..383
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          384..678
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   685 AA;  75305 MW;  F2B2799DD8C85A8E CRC64;
     MTSVDMFLLV VIPLVLPCSS LEGEGGVRNE CLCDGSSCSS GDRCFGQECF SSLAVINGTS
     VVRKGCILGD EDRSLSCRST PTPQLVVKCC YGHLCNMNIS LNFPLKDVQL SAGRPVLRDQ
     ECVCEGGVCE HGHRCTGQHC FSALKMIDGA AVQQKGCLRD DEEGKATCAM PPSSAHVVKC
     CQGHLCNMNV TVQAPGKGTV VQSKSLSKEE HECVCEGGSC GTQNRCLGYQ CFSSLTVSGG
     IIMSQKGCFK VLEQSTMTCK TPPSTDQIVD CCQGHLCNMN ITVELPVKAD EQSSYSVTTL
     AVVIVAPIIV LIILSAVAIL VFRRIHHNQM ERLTSRDAEY GTIDGLIASN VGESTLADLL
     DHSCTSGSGS GLPFLVQRTV ARQITLNECV GKGRYGEVWR GQWQGENVAV KIFSSRDEKS
     WFRETEIYNT VLLRHENILG FIGSDMTSRN SSTQLWLITH FHEMGSLYDY LQLNTLDATS
     CLRMALSIAS GLAHLHVEIF GTHGKPAIAH RDLKSKNILV KKNGQCSIAD LGLAVMHFQD
     TNELDVGNNP KVGTKRYMAP EVLDDSIQMD CFESYKRVDI WALGLVLWEI ARRTVSNGIV
     EDYKPPFHDV VPNDPSFEDM RKVVCVDQQR PNIPNRWFSD PTLTSMAKLM KECWYQNPSA
     RLTALRIKKT LTKIDNSLDK IKTDI
//
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