ID   SMA6_CAEEL              Reviewed;         636 AA.
AC   Q09488;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Serine/threonine-protein kinase receptor sma-6 {ECO:0000305};
DE            EC=2.7.11.30;
DE   Flags: Precursor;
GN   Name=sma-6; ORFNames=C32D5.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=Bristol N2;
RX   PubMed=9847239; DOI=10.1242/dev.126.2.251;
RA   Krishna S., Maduzia L.L., Padgett R.W.;
RT   "Specificity of TGFbeta signaling is conferred by distinct type I receptors
RT   and their associated SMAD proteins in Caenorhabditis elegans.";
RL   Development 126:251-260(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=20534671; DOI=10.1242/dev.051615;
RA   Tian C., Sen D., Shi H., Foehr M.L., Plavskin Y., Vatamaniuk O.K., Liu J.;
RT   "The RGM protein DRAG-1 positively regulates a BMP-like signaling pathway
RT   in Caenorhabditis elegans.";
RL   Development 137:2375-2384(2010).
RN   [4]
RP   INTERACTION WITH SMA-10.
RX   PubMed=20502686; DOI=10.1371/journal.pgen.1000963;
RA   Gumienny T.L., Macneil L., Zimmerman C.M., Wang H., Chin L., Wrana J.L.,
RA   Padgett R.W.;
RT   "Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein
RT   that enhances bone morphogenetic protein signaling.";
RL   PLoS Genet. 6:E1000963-E1000963(2010).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH DRAG-1.
RX   PubMed=24004951; DOI=10.1242/dev.099838;
RA   Tian C., Shi H., Xiong S., Hu F., Xiong W.C., Liu J.;
RT   "The neogenin/DCC homolog UNC-40 promotes BMP signaling via the RGM protein
RT   DRAG-1 in C. elegans.";
RL   Development 140:4070-4080(2013).
CC   -!- FUNCTION: Serine/threonine-protein kinase receptor which binds TGF-
CC       beta-like ligands dbl-1 and perhaps daf-7 (PubMed:9847239,
CC       PubMed:24004951). Upon ligand binding, probably activates a TGF-beta-
CC       like signaling pathway (PubMed:9847239, PubMed:24004951).
CC       {ECO:0000269|PubMed:24004951, ECO:0000269|PubMed:9847239}.
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   -!- 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;
CC   -!- SUBUNIT: Interacts with sma-10 (PubMed:20502686). Interacts with drag-1
CC       (PubMed:24004951). {ECO:0000269|PubMed:20502686,
CC       ECO:0000269|PubMed:24004951}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in pharyngeal, hypodermal and intestinal
CC       cells. {ECO:0000269|PubMed:20534671}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR   EMBL; AF104017; AAD12261.1; -; mRNA.
DR   EMBL; FO080708; CCD66028.1; -; Genomic_DNA.
DR   PIR; T15734; T15734.
DR   RefSeq; NP_495271.1; NM_062870.5.
DR   AlphaFoldDB; Q09488; -.
DR   SMR; Q09488; -.
DR   BioGRID; 39384; 87.
DR   STRING; 6239.C32D5.2.1; -.
DR   GlyCosmos; Q09488; 2 sites, No reported glycans.
DR   PaxDb; 6239-C32D5-2; -.
DR   EnsemblMetazoa; C32D5.2.1; C32D5.2.1; WBGene00004860.
DR   GeneID; 174044; -.
DR   KEGG; cel:CELE_C32D5.2; -.
DR   UCSC; C32D5.2.1; c. elegans.
DR   AGR; WB:WBGene00004860; -.
DR   WormBase; C32D5.2; CE01842; WBGene00004860; sma-6.
DR   eggNOG; KOG2052; Eukaryota.
DR   GeneTree; ENSGT00940000168285; -.
DR   HOGENOM; CLU_000288_8_1_1; -.
DR   InParanoid; Q09488; -.
DR   OMA; GSCPNNV; -.
DR   OrthoDB; 3900892at2759; -.
DR   PhylomeDB; Q09488; -.
DR   BRENDA; 2.7.10.2; 1045.
DR   Reactome; R-CEL-201451; Signaling by BMP.
DR   SignaLink; Q09488; -.
DR   PRO; PR:Q09488; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004860; Expressed in pharyngeal muscle cell (C elegans) and 6 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; ISS:WormBase.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0036122; F:BMP binding; IDA:WormBase.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
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; ISS:WormBase.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR   GO; GO:0050832; P:defense response to fungus; IMP:WormBase.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR   GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:WormBase.
DR   GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:WormBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IGI:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; IMP:WormBase.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IMP:WormBase.
DR   GO; GO:0000003; P:reproduction; IMP:WormBase.
DR   CDD; cd14056; STKc_TGFbR_I; 1.
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   PRINTS; PR00653; ACTIVIN2R.
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   1: Evidence at protein level;
KW   ATP-binding; Developmental protein; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..636
FT                   /note="Serine/threonine-protein kinase receptor sma-6"
FT                   /id="PRO_0000024432"
FT   TOPO_DOM        21..190
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..636
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          235..264
FT                   /note="GS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT   DOMAIN          265..606
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          491..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        397
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         271..279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   636 AA;  72235 MW;  3349C85944E6AE24 CRC64;
     MNITFIFILI FGFFNTQKCS KDYDHFDDED LALSIPKNAI GVPKEFRQQV LKEMKLRNRP
     NDILKNRCYC NYDQSICGNN MTCVKQDGAA CYHAVEEVYN KAEKRMETLH KWGCATLERG
     SGASHLTCNS WRAAHHSPKS IGCCYEGNYC NKNLIPPAYV HHHKEKALQE KTDNPEDYDS
     PLENMTRGGK MFIMVFATVM SVFAVIGCIY LCITRAEEKS KARARAKTVS LKTESTYMES
     KSMLEDSGSG SGQAALIQRT VRQDLTIIKT IGQGRYGEVR KALYRGSYVA VKTFYTTDED
     SWKNERDVYQ TNMINHENIL QFVAADIWSE EDSMTKMLLI TDYHELGSLS DYLCREETLT
     TDEALRLIHS CICGIEHLHA AVHGTGSFRK PEIAHRDIKS KNIIVKRPNV CCIADLGLAL
     RYQNDKILPE KFNVQVGTKR YMAPELISNK LNPKDFSQFK MADIYSMALV MWEVAIRVEV
     NTCEEVLTVD ETSPDHSASS GIGESVSSSG NISRMHLQKT NVEGHSTSLK AKQHVPPFDG
     IVHNDPNFDE MNDVICVRRI RPPPDLAWKN VPALNELSKL MEDSWHSIPH FRHSALKLKK
     EMAELIKNPD RQNQSQRKVE FQQQDSGLVE SATNQS
//