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 16-DEC-2008, entry version 69. DE RecName: Full=Serine/threonine-protein kinase sma-6; DE EC=2.7.11.30; DE Flags: Precursor; GN Name=sma-6; ORFNames=C32D5.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Bristol N2; RX MEDLINE=99065496; PubMed=9847239; RA Krishna S., Maduzia L.L., Padgett R.W.; RT "Specificity of TGFbeta signaling is conferred by distinct type I RT receptors and their associated SMAD proteins in Caenorhabditis RT elegans."; RL Development 126:251-260(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; 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 RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Involved in TGF-beta pathway. May be a receptor for daf- CC 7. CC -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor- CC protein] phosphate. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein (Potential). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. CC -!- SIMILARITY: Contains 1 GS domain. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF104017; AAD12261.1; -; mRNA. DR EMBL; U23511; AAC46790.1; -; Genomic_DNA. DR PIR; T15734; T15734. DR RefSeq; NP_495271.1; -. DR UniGene; Cel.5733; -. DR HSSP; P36897; 1IAS. DR Ensembl; C32D5.2; Caenorhabditis elegans. DR GeneID; 174044; -. DR KEGG; cel:C32D5.2; -. DR NMPDR; fig|6239.3.peg.5860; -. DR WormBase; WBGene00004860; sma-6. DR WormPep; C32D5.2; CE01842. DR NextBio; 882265; -. DR ArrayExpress; Q09488; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0005024; F:transforming growth factor beta receptor ac...; IEA:InterPro. DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase. DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase. DR GO; GO:0040018; P:positive regulation of multicellular organi...; IMP:WormBase. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR GO; GO:0007178; P:transmembrane receptor protein serine/threo...; IEA:InterPro. DR InterPro; IPR000333; Activin_II_recpt. DR InterPro; IPR000472; Activin_rcpt. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_bd_CS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR003605; TGF_beta_rcpt_GS. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08515; TGF_beta_GS; 1. DR PRINTS; PR00653; ACTIVIN2R. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00467; GS; 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 2: Evidence at transcript level; KW ATP-binding; Complete proteome; Developmental protein; Glycoprotein; KW Kinase; Membrane; Nucleotide-binding; Receptor; KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane. FT SIGNAL 1 20 Potential. FT CHAIN 21 636 Serine/threonine-protein kinase sma-6. FT /FTId=PRO_0000024432. FT TOPO_DOM 21 190 Extracellular (Potential). FT TRANSMEM 191 211 Potential. FT TOPO_DOM 212 636 Cytoplasmic (Potential). FT DOMAIN 235 264 GS. FT DOMAIN 265 606 Protein kinase. FT NP_BIND 271 279 ATP (By similarity). FT ACT_SITE 397 397 Proton acceptor (By similarity). FT BINDING 292 292 ATP (By similarity). FT CARBOHYD 80 80 N-linked (GlcNAc...) (Potential). FT CARBOHYD 184 184 N-linked (GlcNAc...) (Potential). 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 //