ID A8WTW1_CAEBR Unreviewed; 629 AA.
AC A8WTW1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN Name=sma-6 {ECO:0000313|WormBase:CBG02627};
GN Synonyms=Cbr-sma-6 {ECO:0000313|EMBL:CAP23923.2};
GN ORFNames=CBG02627 {ECO:0000313|WormBase:CBG02627}, CBG_02627
GN {ECO:0000313|EMBL:CAP23923.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP23923.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP23923.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP23923.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 EMBL; HE601438; CAP23923.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WTW1; -.
DR STRING; 6238.A8WTW1; -.
DR EnsemblMetazoa; CBG02627.1; CBG02627.1; WBGene00025646.
DR WormBase; CBG02627; CBP31985; WBGene00025646; Cbr-sma-6.
DR eggNOG; KOG2052; Eukaryota.
DR HOGENOM; CLU_000288_8_1_1; -.
DR InParanoid; A8WTW1; -.
DR OMA; WEACTIT; -.
DR OrthoDB; 3900892at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:GOC.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036122; F:BMP binding; IEA:EnsemblMetazoa.
DR GO; GO:0046332; F:SMAD binding; IBA:GO_Central.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0040024; P:dauer larval development; IEA:EnsemblMetazoa.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblMetazoa.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:EnsemblMetazoa.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IEA:EnsemblMetazoa.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:EnsemblMetazoa.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:EnsemblMetazoa.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:EnsemblMetazoa.
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:SF68; 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 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:UP000008549};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..629
FT /note="receptor protein serine/threonine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002729518"
FT TRANSMEM 188..207
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..597
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 489..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 629 AA; 72135 MW; 5BA1BC6CCB68B137 CRC64;
MNIVFLFLLV FGFSHCAVDY DQYDDEDLAL SIPKDAVGVP KEFRRRVLKE MAIRQKPNDI
PKNRCYCNYD ESICGKNMTC VKMDGAACYH AVEEKYNKHE KRMETQHKWG CATLERGSGA
SHLTCNSWRA AHHSPKSIGC CYEGNFCNKD LVPPPYVHHH KEKVLQEEDN SYNETNSSFN
NVINGIEMFF IIIAVGMIAF GVVWWAYRRR SRSAKEKPVS LSTESSYWDE KRAMMEDSGS
GSGQAALLQR TVRQDLTIIQ TIGQGRYGEV RKALYRGSYV AVKTFYTTDE DSWKNERDVY
QTNMINHENI LQFVAADIWS EEDSMTKMLL ITDYHELGSL SDYLCREETL TTEEALRLIH
SCLCGIEHLH ASVQGTGSFR KPEIAHRDIK SKNIIVKRPN VCCIADLGLA LRYQNNEIIP
QKYNVQVGTK RYMAPELLSN TLNPQDFSQF KMADIYSMAL VMWEIVIRVE VNTCEEVSAL
DETAADHSAS SGIGESISSS DNYSRIQRHQ KQKVESPASL KAKPYMPPFD GIVHNDPSFD
DMREVVYVRK VRPPPELAWK KVPVLHKLSK LMEDSWHAMP HFRHTALKLK KETTKLIEMT
DRQKQQQGKE MFQQQDSCLV ESATNRYAC
//
