LOCUS       NP_001380622            1770 aa            linear   ROD 28-APR-2025
DEFINITION  sodium leak channel NALCN isoform 1 [Rattus norvegicus].
ACCESSION   NP_001380622
VERSION     NP_001380622.1
DBSOURCE    REFSEQ: accession NM_001393693.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1770)
  AUTHORS   Kang,Y., Wu,J.X. and Chen,L.
  TITLE     Structure of voltage-modulated sodium-selective NALCN-FAM155A
            channel complex
  JOURNAL   Nat Commun 11 (1), 6199 (2020)
   PUBMED   33273469
  REMARK    GeneRIF: Structure of voltage-modulated sodium-selective
            NALCN-FAM155A channel complex.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1770)
  AUTHORS   Al-Sayed,M.D., Al-Zaidan,H., Albakheet,A., Hakami,H., Kenana,R.,
            Al-Yafee,Y., Al-Dosary,M., Qari,A., Al-Sheddi,T., Al-Muheiza,M.,
            Al-Qubbaj,W., Lakmache,Y., Al-Hindi,H., Ghaziuddin,M., Colak,D. and
            Kaya,N.
  TITLE     Mutations in NALCN cause an autosomal-recessive syndrome with
            severe hypotonia, speech impairment, and cognitive delay
  JOURNAL   Am J Hum Genet 93 (4), 721-726 (2013)
   PUBMED   24075186
REFERENCE   3  (residues 1 to 1770)
  AUTHORS   Koroglu,C., Seven,M. and Tolun,A.
  TITLE     Recessive truncating NALCN mutation in infantile neuroaxonal
            dystrophy with facial dysmorphism
  JOURNAL   J Med Genet 50 (8), 515-520 (2013)
   PUBMED   23749988
REFERENCE   4  (residues 1 to 1770)
  AUTHORS   Lu,B., Su,Y., Das,S., Liu,J., Xia,J. and Ren,D.
  TITLE     The neuronal channel NALCN contributes resting sodium permeability
            and is required for normal respiratory rhythm
  JOURNAL   Cell 129 (2), 371-383 (2007)
   PUBMED   17448995
REFERENCE   5  (residues 1 to 1770)
  AUTHORS   Nash,H.A., Scott,R.L., Lear,B.C. and Allada,R.
  TITLE     An unusual cation channel mediates photic control of locomotion in
            Drosophila
  JOURNAL   Curr Biol 12 (24), 2152-2158 (2002)
   PUBMED   12498692
REFERENCE   6  (residues 1 to 1770)
  AUTHORS   Lee,J.H., Cribbs,L.L. and Perez-Reyes,E.
  TITLE     Cloning of a novel four repeat protein related to voltage-gated
            sodium and calcium channels
  JOURNAL   FEBS Lett 445 (2-3), 231-236 (1999)
   PUBMED   10094463
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000015.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360194.2232786.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760386 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1770
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="15"
                     /map="15q25"
     Protein         1..1770
                     /product="sodium leak channel NALCN isoform 1"
                     /note="sodium leak channel non-selective protein; sodium
                     leak channel NALCN; brain voltage-gated cation channel;
                     voltage gated channel-like protein 1; four domain-type
                     voltage-gated ion channel alpha-1 subunit; voltage gated
                     channel like 1; rb21-channel"
                     /calculated_mol_wt=203844
     Region          36..331
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            37..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            66..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            107..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            174..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            295..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          383..603
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            417..439
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            448..468
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            473..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            503..530
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            570..599
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          762..789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          887..1161
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            887..906
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            916..939
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            948..972
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            981..1003
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1016..1039
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1064
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33273469,
                     ECO:0007744|PDB:7CU3; propagated from UniProtKB/Swiss-Prot
                     (Q6Q760.1)"
     Site            1130..1159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Region          1209..1458
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1211..1227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1237..1260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1272..1293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1297..1318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1332..1357
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     Site            1421..1447
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6Q760.1)"
     CDS             1..1770
                     /gene="Nalcn"
                     /gene_synonym="Vgcnl1"
                     /coded_by="NM_001393693.1:317..5629"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:266760"
                     /db_xref="RGD:628710"
ORIGIN      
        1 mlkrkqssrv eaqpvtdfgp deslsdnadi lwinkpwvhs llricaiisv isvcmntpmt
       61 fehypplqyv tftldtllmf lytaemiakm hirgivkgds syvkdrwcvf dgfmvfclwv
      121 slvlqvfeia divdqmspwg mlriprplim irafriyfrf elprtritni lkrsgeqiws
      181 vsifllffll lygilgvqmf gtftyhcvvn dtkpgnvtwn slaipdthcs peleegyqcp
      241 pgfkcmdled lglsrqelgy sgfneigtsi ftvyeassqe gwvflmyrai dsfprwrsyf
      301 yfitliffla wlvknvfiav iietfaeirv qfqqmwgtrs sttstattqm fhedaaggwq
      361 lvavdvnkpq grapaclqkm mrssvfhmfi lsmvtvdviv aasnyykgen frrqydefyl
      421 aevaftvlfd leallkiwcl gftgyisssl hkfelllvig ttlhvypdly hsqftyfqvl
      481 rvvrlikisp aledfvykif gpgkklgslv vftasllivm saislqmfcf veeldrfttf
      541 prafmsmfqi ltqegwvdvm dqtlnavghm waplvaiyfi lyhlfatlil lslfvavild
      601 nleldedlkk lkqlkqsean adtkeklplr lrifekfpnr pqmvkisklp sdftvpkire
      661 sfmkqfidrq qqdtcclfri lpstsssscd npkrptvedn kyidqklrks vfsirarnll
      721 eketavtkil ractrqrmls gsfegqpake rsilsvqhhi rqerrslrhg snsqrisrgk
      781 sletltqdhs ntvryrnaqr edseikmiqe kkeqaemkrk vqeeelrenh pyfdkplfiv
      841 grehrfrnfc rvvvrarfna sktdpvtgav kntkyhqlyd llglvtyldw vmitvticsc
      901 ismmfespfr rvmhaptlqi aeyvfvifms ielnlkimad glfftptavi rdfggvmdif
      961 iylvsliflc wmpqnvpaes gaqllmvlrc lrplrifklv pqmrkvvrel fsgfkeiflv
     1021 sillltlmlv fasfgvqlfa gklakcndpn iirredcngi frinvsvskn lnlklrpgek
     1081 kpgfwvprvw anprnfnfdn vgnamlalfe vlslkgwvev rdviihrvgp ihgiyihvfv
     1141 flgcmigltl fvgvvianfn enkgtalltv dqrrwedlks rlkiaqplhl pprpdndgfr
     1201 akmyditqhp ffkrtiallv laqsvllsvk wdvedpvtvp latmsvvftf ifvlevtmki
     1261 iamspagfwq srrnrydllv tslgvvwvvl hfallnayty mmgacvivfr ffsicgkhvt
     1321 lkmllltvvv smyksffiiv gmfllllcya fagvvlfgtv kygeninrha nfssagkait
     1381 vlfrivtged wnkimhdcmv qppfctpdef tywatdcgny agalmyfcsf yviiayimln
     1441 llvaiivenf slfysteedq llsyndlrhf qiiwnmvddk regviptfrv kfllrllrgr
     1501 levdldkdkl lfkhmcyeme rlhnggdvtf hdvlsmlsyr svdirkslql eellareqle
     1561 ytieeevakq tirmwlkkcl krirakqqqs csiihslres qqqelsrfln ppsiettqps
     1621 edtnansqdh ntqpesssqq qllsptlsdr ggsrqdaadt gkpqrkigqw rlpsaaiaek
     1681 tapvnkmssy sqdpereeee vskgflapkp ishsvssvnl rfggrttmks vvckmnpmpd
     1741 tascgsevkk wwtrqltves desgddlldi
//
