SMA6_CAEEL
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 03-AUG-2022, entry version 161.
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; -.
DR PaxDb; Q09488; -.
DR PRIDE; Q09488; -.
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 CTD; 174044; -.
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; CDGSCPN; -.
DR OrthoDB; 776697at2759; -.
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 tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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:0006468; P:protein phosphorylation; IBA:GO_Central.
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 Gene3D; 2.10.60.10; -; 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; PTHR23255; 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; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 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
