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Database: UniProt
Entry: A0A1A9X4G8_9MUSC
LinkDB: A0A1A9X4G8_9MUSC
Original site: A0A1A9X4G8_9MUSC 
ID   A0A1A9X4G8_9MUSC        Unreviewed;       569 AA.
AC   A0A1A9X4G8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
OS   Glossina brevipalpis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI043899-PA, ECO:0000313|Proteomes:UP000091820};
RN   [1] {ECO:0000313|Proteomes:UP000091820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GBRI043899-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI043899-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   -!- SIMILARITY: Belongs to the scoloptoxin-05 family.
CC       {ECO:0000256|ARBA:ARBA00025739}.
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DR   AlphaFoldDB; A0A1A9X4G8; -.
DR   STRING; 37001.A0A1A9X4G8; -.
DR   EnsemblMetazoa; GBRI043899-RA; GBRI043899-PA; GBRI043899.
DR   VEuPathDB; VectorBase:GBRI043899; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000091820; 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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF72; RECEPTOR PROTEIN SERINE_THREONINE KINASE; 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   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   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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..569
FT                   /note="receptor protein serine/threonine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008400979"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          226..255
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          256..555
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   569 AA;  64094 MW;  F830D26AF6DB8D62 CRC64;
     MAAIIKLIIL LIVLQINKAK GEISGRSMDD YRKNMSHEIS YTNNSKEYPS LLPQNSIQTH
     PRFKCFSCEP PCHNASQHAH MCQNAIQCFK SRVRNAFGEE EVSRGCINSP DQTPLICSAN
     NIKTLNPRKR HTASPVNVAC CAGDYCNGGE FPELLNTEIT RLSDDHSNLL KLFFAILGPI
     VAISVLAYIA IYFIRRKHRK RLPSSRTKQD PDTYLMNDEQ VTIGDSTLRE YLQHSVTSGS
     GSGLPVFIQR TLNKQVSLIE CIGRGKYGQV WRGQWHGENV AVKIFTSRDE NSWRRETEIY
     CTVALRHENI LGFIGSDIAS QNSCTQLWLL THYHPNGSLM DYLSRNTLSH RDMILICLSI
     ANGLVHIHSE ITHSEISGIE GRSAKPAMAH RDLKSKNILV KSNGTCVIAD FGLAVTHSNV
     TGKLDLGNNP KVGTKRYMAP EVLDESIDMQ KFDSLRPTDI YALGLILWEV CRRTISSGKV
     EEYKVPYYDV VPADPSFEDM RKVVCVDNYR PSIPNRWSSD PLLAGMSKLM KECWRQNPIA
     RVAVLRVKKT IQKLAAADEK LRLEDEICV
//
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