LOCUS       NP_001391651            1116 aa            linear   ROD 11-MAR-2025
DEFINITION  neural cell adhesion molecule 1 isoform 5 precursor [Mus musculus].
ACCESSION   NP_001391651 XP_017168683
VERSION     NP_001391651.1
DBSOURCE    REFSEQ: accession NM_001404722.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Hrncir,H.R., Goodloe,B., Bombin,S., Hogan,C.B., Jadi,O. and
            Gracz,A.D.
  TITLE     Sox9 inhibits Activin A to promote biliary maturation and branching
            morphogenesis
  JOURNAL   Nat Commun 16 (1), 1667 (2025)
   PUBMED   39955269
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Rodriguez-Perez,L.M., Lopez-de-San-Sebastian,J., de Diego,I.,
            Smith,A., Roales-Bujan,R., Jimenez,A.J. and Paez-Gonzalez,P.
  TITLE     A selective defect in the glial wedge as part of the
            neuroepithelium disruption in hydrocephalus development in the
            mouse hyh model is associated with complete corpus callosum
            dysgenesis
  JOURNAL   Front Cell Neurosci 18, 1330412 (2024)
   PUBMED   38450283
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1116)
  AUTHORS   Alderman,P.J., Saxon,D., Torrijos-Saiz,L.I., Sharief,M., Page,C.E.,
            Baroudi,J.K., Biagiotti,S.W., Butyrkin,V.A., Melamed,A., Kuo,C.T.,
            Vicini,S., Garcia-Verdugo,J.M., Herranz-Perez,V., Corbin,J.G. and
            Sorrells,S.F.
  TITLE     Delayed maturation and migration of excitatory neurons in the
            juvenile mouse paralaminar amygdala
  JOURNAL   Neuron 112 (4), 574-592 (2024)
   PUBMED   38086370
REFERENCE   5  (residues 1 to 1116)
  AUTHORS   Hara,Y., Katsuyama,T., Fukaya,M., Sugawara,T., Shiroshima,T.,
            Sadakata,T., Osumi,N. and Sakagami,H.
  TITLE     ADP Ribosylation Factor 4 (Arf4) Regulates Radial Migration through
            N-Cadherin Trafficking during Cerebral Cortical Development
  JOURNAL   eNeuro 10 (11) (2023)
   PUBMED   37848288
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1116)
  AUTHORS   Miragall,F., Hwang,T.K., Traub,O., Hertzberg,E.L. and Dermietzel,R.
  TITLE     Expression of connexins in the developing olfactory system of the
            mouse
  JOURNAL   J Comp Neurol 325 (3), 359-378 (1992)
   PUBMED   1332989
REFERENCE   7  (residues 1 to 1116)
  AUTHORS   Moller,C.J., Christgau,S., Williamson,M.R., Madsen,O.D., Niu,Z.P.,
            Bock,E. and Baekkeskov,S.
  TITLE     Differential expression of neural cell adhesion molecule and
            cadherins in pancreatic islets, glucagonomas, and insulinomas
  JOURNAL   Mol Endocrinol 6 (8), 1332-1342 (1992)
   PUBMED   1406710
REFERENCE   8  (residues 1 to 1116)
  AUTHORS   Zuber,C., Lackie,P.M., Catterall,W.A. and Roth,J.
  TITLE     Polysialic acid is associated with sodium channels and the neural
            cell adhesion molecule N-CAM in adult rat brain
  JOURNAL   J Biol Chem 267 (14), 9965-9971 (1992)
   PUBMED   1315775
REFERENCE   9  (residues 1 to 1116)
  AUTHORS   Jones,F.S., Prediger,E.A., Bittner,D.A., De Robertis,E.M. and
            Edelman,G.M.
  TITLE     Cell adhesion molecules as targets for Hox genes: neural cell
            adhesion molecule promoter activity is modulated by cotransfection
            with Hox-2.5 and -2.4
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2086-2090 (1992)
   PUBMED   1347944
REFERENCE   10 (residues 1 to 1116)
  AUTHORS   Pan,L.C., Margolskee,R.F. and Blau,H.M.
  TITLE     Cloning muscle isoforms of neural cell adhesion molecule using an
            episomal shuttle vector
  JOURNAL   Somat Cell Mol Genet 18 (2), 163-177 (1992)
   PUBMED   1315456
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT025676.10 and AC117630.11.
            
            On Apr 13, 2022 this sequence version replaced XP_017168683.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR10662772.3054360.1,
                                           SRR9219382.161173.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164141
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 26.83 cM"
     Protein         1..1116
                     /product="neural cell adhesion molecule 1 isoform 5
                     precursor"
                     /note="N-CAM-1"
                     /calculated_mol_wt=117232
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2213
     Region          20..116
                     /region_name="IgI_1_NCAM-1"
                     /note="First immunoglobulin (Ig)-like domain of neural
                     cell adhesion molecule (NCAM-1); member of the I-set of Ig
                     superfamily (IgSF) domains; cd05865"
                     /db_xref="CDD:409451"
     Region          20..25
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409451"
     Region          28..32
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409451"
     Region          34..44
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409451"
     Site            order(35,37..38)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409451"
     Region          50..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409451"
     Region          59..61
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409451"
     Region          69..75
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409451"
     Region          77..85
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409451"
     Region          92..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409451"
     Region          104..115
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409451"
     Region          124..190
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          135..139
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          148..152
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          172..176
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          186..191
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          211..308
                     /region_name="IgI_3_NCAM-1"
                     /note="Third immunoglobulin (Ig)-like domain of Neural
                     Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of
                     IgSF domains; cd05730"
                     /db_xref="CDD:143207"
     Region          211..216
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:143207"
     Region          220..226
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:143207"
     Site            order(222,239..240,242,269,272,280,304,306..307)
                     /site_type="other"
                     /note="Ig3-Ig interaction interface [polypeptide binding]"
                     /db_xref="CDD:143207"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, partial.
                     /evidence=ECO:0000269|PubMed:14658030; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Region          229..239
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:143207"
     Region          243..249
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:143207"
     Region          251..253
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:143207"
     Region          263..266
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:143207"
     Region          271..277
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:143207"
     Region          283..292
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:143207"
     Region          295..307
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:143207"
     Region          307..403
                     /region_name="IgI_NCAM-1"
                     /note="Immunoglobulin (Ig)-like I-set domain of Neural
                     Cell Adhesion Molecule 1 (NCAM-1); cd05869"
                     /db_xref="CDD:143277"
     Region          307..312
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:143277"
     Region          316..320
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:143277"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14658030; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Region          325..333
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:143277"
     Region          339..345
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:143277"
     Region          348..351
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:143277"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14658030; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Region          359..365
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:143277"
     Region          368..374
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:143277"
     Region          382..390
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:143277"
     Region          393..403
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:143277"
     Region          412..490
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          423..427
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            424
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14658030; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Region          436..440
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            450
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14658030,
                     ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770;
                     propagated from UniProtKB/Swiss-Prot (P13595.3)"
     Region          463..467
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          477..482
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            479
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14658030; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Region          502..589
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(585..586,588..589)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          603..685
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(683..684,686..687)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            713..730
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13595.3)"
     Region          757..810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13595.3)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16452087,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Region          840..913
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13595.3)"
     Region          <859..1094
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Region          925..1116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13595.3)"
     Site            927
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            959
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            1002
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            1006
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     Site            1031
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P13595.3)"
     CDS             1..1116
                     /gene="Ncam1"
                     /gene_synonym="CD56; E-NCAM; Ncam; NCAM-1"
                     /coded_by="NM_001404722.1:194..3544"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:17967"
                     /db_xref="MGI:MGI:97281"
ORIGIN      
        1 mlrtkdliwt lfflgtavsl qvdivpsqge isvgeskffl cqvagdakdk diswfspnge
       61 klspnqqris vvwndddsst ltiynanidd agiykcvvta edgtqseatv nvkifqklmf
      121 knaptpqefk egedavivcd vvsslpptii wkhkgrdvil kkdvrfivls nnylqirgik
      181 ktdegtyrce grilargein fkdiqvivnv pptvqarqsi vnatanlgqs vtlvcdadgf
      241 peptmswtkd gepieneeed dekhifsdds seltirnvdk ndeaeyvcia enkageqdas
      301 ihlkvfakpk ityvenqtam eleeqvtltc easgdpipsi twrtstrnis seektldghm
      361 vvrsharvss ltlksiqytd ageyictasn tigqdsqsmy levqyapklq gpvavytweg
      421 nqvnitcevf aypsatiswf rdgqllpssn ysnikiyntp sasylevtpd sendfgnync
      481 tavnrigqes lefilvqadt psspsidrve pysstaqvqf depeatggvp ilkykaewks
      541 lgeeswhfkw ydakeanmeg ivtimglkpe trysvrlaal ngkglgeisa atefktqpvr
      601 epsapklegq mgedgnsikv nlikqddggs pirhylvkyr aklasewkpe irlpsgsdhv
      661 mlksldwnae yevyvvaenq qgkskaahfv frtsaqptai pangsptagl stgaivgili
      721 vifvlllvvm ditcyflnkc gllmciavnl cgkagpgakg kdmeegkaaf skdeskepiv
      781 evrteeertp nhdggkhtep nettpltepe lpadttatve dmlpsvttvt tnsdtitetf
      841 ataqnsptse tttltssiap pattvpdsns vpagqatpsk gvtasssspa sapkvaplvd
      901 lsdtptsaps asnlsstvla nqgavlspst pasagetska ppaskaspap tptpagaasp
      961 laavaapatd apqakqeaps tkgpdpeptq pgtvknppea atapaspksk aattnpsqge
     1021 dlkmdegnfk tpdidlakdv faalgspapa tgasgqasel apstadsavp papaktekgp
     1081 vetkseppes eakpaptevk tvpndatqtk eneska
//
