ID A0A401SPB4_CHIPU Unreviewed; 536 AA.
AC A0A401SPB4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN ORFNames=chiPu_0010682 {ECO:0000313|EMBL:GCC32221.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC32221.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC32221.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
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:GCC32221.1}.
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DR EMBL; BEZZ01000420; GCC32221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401SPB4; -.
DR STRING; 137246.A0A401SPB4; -.
DR OMA; GSCPNNV; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
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 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; 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:SF50; BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-1A; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF01064; Activin_recp; 1.
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; 1.
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:UP000287033};
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..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..536
FT /note="receptor protein serine/threonine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019056420"
FT TRANSMEM 160..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..237
FT /note="GS"
FT /evidence="ECO:0000259|PROSITE:PS51256"
FT DOMAIN 238..529
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 536 AA; 59952 MW; F98F42025214D83B CRC64;
MYLLGVAWGA RTTTGMSVHR TGVLGTFLLL ILQIQGQNPD SMLMGTGMKT NGATVAPEDA
EPRLNCYCSG HCATEEANNT CKTNGNCFAI IEEDENGEIT LGSGCMRLEG ADFQCKDSTK
VRKRRTIECC NTDFCNKDLH PTLTPISDSG GLFEGDIHRL GLLISLIVCI FVLIIITTAF
YFRYKGQADR RRYNRDLEQD VAFIPPGESL KDLIDQSQSS GSGSGLPLLV QRTIAKQIQM
VRLVGKGRYG EVWMGRWRGE KVAVKVFPSA EEASWFRETE IYQTVLMRHE SILGFIAADI
EGKGSSTWLY LITDYHENGS LYDYLKCTVL DTKALLKLAY SAASGLCHLH TEIYGTQGKP
AIAHRDLKSK NILVKKNGTC SIADLGLTVK FNSDTNEVDI PLNTRVGTKR YMAPEVLDES
LNKNQFQAYL MADIYSFGLV IWEMSRRCLT GGIVEDYQLP YYDMVPNDPS YEDMREVTCV
KCLRPTVSNR WNSDECLRAV LKLMSECWAH NPASRLTALR VKKTLAKMVE SQDIKI
//
