ID DULRD_CAEEL Reviewed; 246 AA. AC Q20432; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 44. DE RecName: Full=Serine/threonine-protein phosphatase dullard homolog; DE EC=3.1.3.16; DE AltName: Full=Small C-terminal domain phosphatase-like phosphatase 2; GN Name=scpl-2; ORFNames=F45E12.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] 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). RN [2] RP IDENTIFICATION. RX MEDLINE=22078992; PubMed=12083771; DOI=10.1016/S0006-291X(02)00641-1; RA Satow R., Chan T.C., Asashima M.; RT "Molecular cloning and characterization of dullard: a novel gene RT required for neural development."; RL Biochem. Biophys. Res. Commun. 295:85-91(2002). CC -!- FUNCTION: Serine/threonine phosphatase which may be required for CC proper nuclear membrane morphology (By similarity). CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein + CC phosphate. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the dullard family. CC -!- SIMILARITY: Contains 1 FCP1 homology 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; U29536; AAA68794.1; -; Genomic_DNA. DR PIR; T16371; T16371. DR RefSeq; NP_495529.1; -. DR UniGene; Cel.15079; -. DR Ensembl; F45E12.1; Caenorhabditis elegans. DR GeneID; 185802; -. DR KEGG; cel:F45E12.1; -. DR NMPDR; fig|6239.3.peg.6218; -. DR WormBase; WBGene00018474; scpl-2. DR WormPep; F45E12.1; CE02737. DR OMA; Q20432; DKLDNNR. DR BRENDA; 3.1.3.16; 672. DR NextBio; 929562; -. DR ArrayExpress; Q20432; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB. DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB. DR InterPro; IPR011948; Dullard. DR InterPro; IPR004274; NIF. DR Pfam; PF03031; NIF; 1. DR SMART; SM00577; CPDc; 1. DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1. DR PROSITE; PS50969; FCP1; 1. PE 2: Evidence at transcript level; KW Complete proteome; Hydrolase; Membrane; Protein phosphatase; KW Transmembrane. FT CHAIN 1 246 Serine/threonine-protein phosphatase FT dullard homolog. FT /FTId=PRO_0000297975. FT TRANSMEM 3 23 Potential. FT DOMAIN 53 220 FCP1 homology. SQ SEQUENCE 246 AA; 28414 MW; 7D60A06A050EA3EA CRC64; MTTIAQSVFC FLAGFFNFFL LYFRKTSRAY CKYQVVKYHS NIPMSPLTTH RLLTVKRKIL VLDLDETLIH SHHDGVLRQT VKPGTPSDFT IRVVIDRHPV KFSVHERPHV DYFLSVVSQW YELVVFTASM EVYGTSVADR LDRGRGILKR RYFRQHCTME VGGYTKDLSA IHPDLSSICI LDNSPGAYRK FPHNAIPIPS WFSDPNDTCL LNLLPFLDAL RFTSDVRSVL SRNMQALPET QSVQYY //