ID NRA1_CAEEL Reviewed; 634 AA. AC Q9XUB9; Q8I4F4; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 22-FEB-2023, entry version 144. DE RecName: Full=Nicotinic receptor-associated protein 1; GN Name=nra-1; ORFNames=T28F3.1; 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 [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING. 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 [2] RP FUNCTION, INTERACTION WITH NICOTINIC ACETYLCHOLINE RECEPTOR, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=15990870; DOI=10.1038/sj.emboj.7600741; RA Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D., Yates J.R. III, RA Schafer W.R.; RT "Identification and characterization of novel nicotinic receptor-associated RT proteins in Caenorhabditis elegans."; RL EMBO J. 24:2566-2578(2005). RN [3] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16998478; DOI=10.1038/ncb1476; RA Kubagawa H.M., Watts J.L., Corrigan C., Edmonds J.W., Sztul E., Browse J., RA Miller M.A.; RT "Oocyte signals derived from polyunsaturated fatty acids control sperm RT recruitment in vivo."; RL Nat. Cell Biol. 8:1143-1148(2006). CC -!- FUNCTION: Exhibits calcium-dependent phospholipid binding properties CC (By similarity). May function in membrane trafficking. Regulates CC synaptic levels of nicotinic acetylcholine receptor subunit lev-1 and CC unc-38 in the nerve cord (PubMed:15990870). Involved in nicotinic CC acetylcholine receptor (nAChR)-mediated sensitivity to nicotine and CC levamisole (PubMed:15990870). Affects directional sperm motility CC (PubMed:16998478). {ECO:0000250|UniProtKB:Q99829, CC ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:16998478}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; CC -!- SUBUNIT: Interacts with nicotinic acetylcholine receptor. CC {ECO:0000269|PubMed:16998478}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15990870}; CC Peripheral membrane protein {ECO:0000269|PubMed:15990870}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; CC IsoId=Q9XUB9-1; Sequence=Displayed; CC Name=b; CC IsoId=Q9XUB9-2; Sequence=VSP_039297; CC -!- TISSUE SPECIFICITY: Expressed in head and tail neurons, ventral cord CC moto-neurons, body wall muscles and hypodermal cells of the vulva. CC {ECO:0000269|PubMed:15990870}. CC -!- DOMAIN: C2 domains are necessary for calcium-dependent cell membrane CC association. C2 domains are necessary for neuronal progenitor cell CC differentiation in a calcium-independent manner. CC {ECO:0000250|UniProtKB:Q99829}. CC -!- DISRUPTION PHENOTYPE: Sperm directional motility defects CC (PubMed:16998478). RNAi-mediated knockdown causes a moderate resistance CC to nicotine-induced paralysis and a decrease in unc-38 synaptic CC expression along nerve cords without affecting lev-1 cellular CC expression levels in muscles (PubMed:15990870). CC {ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:16998478}. CC -!- SIMILARITY: Belongs to the copine family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z82285; CAB05302.1; -; Genomic_DNA. DR EMBL; Z82285; CAD56248.1; -; Genomic_DNA. DR PIR; T25425; T25425. DR RefSeq; NP_503069.1; NM_070668.5. [Q9XUB9-1] DR RefSeq; NP_872104.1; NM_182304.3. [Q9XUB9-2] DR AlphaFoldDB; Q9XUB9; -. DR SMR; Q9XUB9; -. DR BioGRID; 43584; 1. DR IntAct; Q9XUB9; 2. DR MINT; Q9XUB9; -. DR STRING; 6239.T28F3.1a; -. DR iPTMnet; Q9XUB9; -. DR EPD; Q9XUB9; -. DR PaxDb; Q9XUB9; -. DR PeptideAtlas; Q9XUB9; -. DR EnsemblMetazoa; T28F3.1a.1; T28F3.1a.1; WBGene00012128. [Q9XUB9-1] DR EnsemblMetazoa; T28F3.1b.1; T28F3.1b.1; WBGene00012128. [Q9XUB9-2] DR GeneID; 178508; -. DR KEGG; cel:CELE_T28F3.1; -. DR UCSC; T28F3.1a; c. elegans. DR AGR; WB:WBGene00012128; -. DR CTD; 178508; -. DR WormBase; T28F3.1a; CE19806; WBGene00012128; nra-1. [Q9XUB9-1] DR WormBase; T28F3.1b; CE09683; WBGene00012128; nra-1. [Q9XUB9-2] DR eggNOG; KOG1327; Eukaryota. DR GeneTree; ENSGT00940000170481; -. DR InParanoid; Q9XUB9; -. DR OMA; DMHATIR; -. DR OrthoDB; 672483at2759; -. DR PhylomeDB; Q9XUB9; -. DR PRO; PR:Q9XUB9; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00012128; Expressed in germ line (C elegans) and 4 other tissues. DR GO; GO:0005886; C:plasma membrane; IDA:WormBase. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central. DR GO; GO:0097120; P:receptor localization to synapse; IMP:WormBase. DR CDD; cd04048; C2A_Copine; 1. DR CDD; cd04047; C2B_Copine; 1. DR CDD; cd01459; vWA_copine_like; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR037768; C2B_Copine. DR InterPro; IPR045052; Copine. DR InterPro; IPR010734; Copine_C. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR10857; COPINE; 1. DR PANTHER; PTHR10857:SF136; NICOTINIC RECEPTOR-ASSOCIATED PROTEIN 1; 1. DR Pfam; PF00168; C2; 2. DR Pfam; PF07002; Copine; 1. DR SMART; SM00239; C2; 2. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS50004; C2; 2. DR PROSITE; PS50234; VWFA; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell membrane; Membrane; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1..634 FT /note="Nicotinic receptor-associated protein 1" FT /id="PRO_0000144851" FT DOMAIN 1..141 FT /note="C2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 159..295 FT /note="C2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 338..557 FT /note="VWFA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT REGION 576..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 581..595 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 29 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 30 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 30 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 36 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 105 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 105 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 107 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 107 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 119 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 195 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 271 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT VAR_SEQ 258..269 FT /note="Missing (in isoform b)" FT /evidence="ECO:0000305" FT /id="VSP_039297" SQ SEQUENCE 634 AA; 71101 MW; 9CF95130F9A2DCCE CRC64; MNQPIGIADS SRPKTNVRLT ISANNLMDLD VFSKSDPICL IYEKTSGRKA TTTEEITVPT WKDKQWTERG RTEVVMNNLN PQFTKTFLLP YFFEETQLLR FEIYDADSPT VGQDLSSHDF LGRFECVLAQ IVSYSTLKAH LGKTGQIGAQ WRNKDKNTKT GSITIYAEED EKAEKIQFDV CGEGLDKKDF FGKSDPYLNF KRKFDDGSTH LIHRTEVKPK TLDPRWATVQ INTQTLCAKD GDRPIIIECY DHDKWKKGEE PRGDAKFSRD DLIGTAQTTL NELLRGSSDA VEILLTNEKK KAKKGDKYKC SGTLKIWNSR IVIEPTFLDF ISGGTQLDFA VAVDFTASNG PPKSSSSLHF MSADRPNQYE LALRSVLSIC QHYNSSKTFE AFGFGAKLPN QSSVSAIFPL DLQRGTSEVV GITGVMTAYR HALSNVQLYG PTNFAPIIEN VARKAQNMIH DSARYQILLI ITDGIISDMH ATIRSIISAS GLPLSIIIIG VGNEDFEKMH ELDSDDALLQ QDSRIAQRDI VQFVTMREFL NNGQGLYLDP DVIQENLARE VLYEVPAQLT GYMKQRGFQP RPVDDPWRRD SPPPEFDPIL DGTGRRAPML QAPPAGFQYP VYADTSIASA PPMY //