NRA1_CAEEL
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 03-AUG-2022, entry version 142.
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}.
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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 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; 1067545at2759; -.
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; cd04047; C2B_Copine; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 2.60.40.150; -; 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; PTHR10857; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF53300; SSF53300; 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
