LOCUS       NP_001106679             837 aa            linear   ROD 27-APR-2025
DEFINITION  neural cell adhesion molecule 2 isoform a precursor [Mus musculus].
ACCESSION   NP_001106679
VERSION     NP_001106679.1
DBSOURCE    REFSEQ: accession NM_001113208.1
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 837)
  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   2  (residues 1 to 837)
  AUTHORS   Ortega-Gasco,A., Parcerisas,A., Hino,K., Herranz-Perez,V.,
            Ulloa,F., Elias-Tersa,A., Bosch,M., Garcia-Verdugo,J.M., Simo,S.,
            Pujadas,L. and Soriano,E.
  TITLE     Regulation of young-adult neurogenesis and neuronal differentiation
            by neural cell adhesion molecule 2 (NCAM2)
  JOURNAL   Cereb Cortex 33 (21), 10931-10948 (2023)
   PUBMED   37724425
  REMARK    GeneRIF: Regulation of young-adult neurogenesis and neuronal
            differentiation by neural cell adhesion molecule 2 (NCAM2).
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Sah,S., Keable,R., Pfundstein,G., Clemens,K.J., Begg,D.,
            Schachner,M., Leshchyns'ka,I. and Sytnyk,V.
  TITLE     Deficiency in the neural cell adhesion molecule 2 (NCAM2) reduces
            axonal levels of beta-site amyloid precursor protein cleaving
            enzyme 1 (BACE1), affects axonal organization in the hippocampus,
            and leads to behavioral deficits
  JOURNAL   Cereb Cortex 33 (18), 10047-10065 (2023)
   PUBMED   37522285
  REMARK    GeneRIF: Deficiency in the neural cell adhesion molecule 2 (NCAM2)
            reduces axonal levels of beta-site amyloid precursor protein
            cleaving enzyme 1 (BACE1), affects axonal organization in the
            hippocampus, and leads to behavioral deficits.
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Keable,R., Hu,S., Pfundstein,G., Kozlova,I., Su,F., Du,X., Yang,H.,
            Gunnersen,J., Schachner,M., Leshchyns'ka,I. and Sytnyk,V.
  TITLE     The BACE1-generated C-terminal fragment of the neural cell adhesion
            molecule 2 (NCAM2) promotes BACE1 targeting to Rab11-positive
            endosomes
  JOURNAL   Cell Mol Life Sci 79 (11), 555 (2022)
   PUBMED   36251052
  REMARK    GeneRIF: The BACE1-generated C-terminal fragment of the neural cell
            adhesion molecule 2 (NCAM2) promotes BACE1 targeting to
            Rab11-positive endosomes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 837)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Yang,A., Walker,N., Bronson,R., Kaghad,M., Oosterwegel,M.,
            Bonnin,J., Vagner,C., Bonnet,H., Dikkes,P., Sharpe,A., McKeon,F.
            and Caput,D.
  TITLE     p73-deficient mice have neurological, pheromonal and inflammatory
            defects but lack spontaneous tumours
  JOURNAL   Nature 404 (6773), 99-103 (2000)
   PUBMED   10716451
REFERENCE   7  (residues 1 to 837)
  AUTHORS   O'Leary,D.D., Yates,P.A. and McLaughlin,T.
  TITLE     Molecular development of sensory maps: representing sights and
            smells in the brain
  JOURNAL   Cell 96 (2), 255-269 (1999)
   PUBMED   9988220
  REMARK    Review article
REFERENCE   8  (residues 1 to 837)
  AUTHORS   Alenius,M. and Bohm,S.
  TITLE     Identification of a novel neural cell adhesion molecule-related
            gene with a potential role in selective axonal projection
  JOURNAL   J Biol Chem 272 (42), 26083-26086 (1997)
   PUBMED   9334170
REFERENCE   9  (residues 1 to 837)
  AUTHORS   Yoshihara,Y., Kawasaki,M., Tamada,A., Fujita,H., Hayashi,H.,
            Kagamiyama,H. and Mori,K.
  TITLE     OCAM: A new member of the neural cell adhesion molecule family
            related to zone-to-zone projection of olfactory and vomeronasal
            axons
  JOURNAL   J Neurosci 17 (15), 5830-5842 (1997)
   PUBMED   9221781
REFERENCE   10 (residues 1 to 837)
  AUTHORS   Reeves,R.H., Rue,E.E., Citron,M.P. and Cabin,D.E.
  TITLE     High-resolution recombinational map of mouse chromosome 16
  JOURNAL   Genomics 43 (2), 202-208 (1997)
   PUBMED   9244437
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AW121550.1, BC119027.1, AF016620.1, BB663005.1 and BM933307.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            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 :: AF001287.1, SRR1660811.94494.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164132
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 45.89 cM"
     Protein         1..837
                     /product="neural cell adhesion molecule 2 isoform a
                     precursor"
                     /note="neural cell adhesion molecule RB-8; olfactory axon
                     cell adhesion molecule; R4B12 antigen"
                     /calculated_mol_wt=91141
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2082
     mat_peptide     20..837
                     /product="Neural cell adhesion molecule 2.
                     /id=PRO_0000042589"
                     /note="propagated from UniProtKB/Swiss-Prot (O35136.1)"
                     /calculated_mol_wt=91141
     Region          21..113
                     /region_name="IgI_1_NCAM-2"
                     /note="First immunoglobulin (Ig)-like domain of neural
                     cell adhesion molecule NCAM-2; member of the I-set of Ig
                     superfamily (IgSF) domains; cd05866"
                     /db_xref="CDD:409452"
     Region          21..26
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409452"
     Region          29..33
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409452"
     Region          35..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409452"
     Site            order(36,38..39)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409452"
     Region          49..55
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409452"
     Region          58..60
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409452"
     Region          66..72
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409452"
     Region          74..82
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409452"
     Region          89..96
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409452"
     Region          101..112
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409452"
     Region          122..187
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          132..136
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          145..152
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          169..173
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Region          183..187
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          191..194
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          209..298
                     /region_name="IgI_1_MuSK"
                     /note="agrin-responsive first immunoglobulin-like domains
                     (Ig1) of the MuSK ectodomain; a member of the I-set of
                     IgSF domains; cd20970"
                     /db_xref="CDD:409562"
     Region          209..212
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409562"
     Region          217..222
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409562"
     Site            219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Region          228..235
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409562"
     Region          241..246
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409562"
     Region          248..250
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409562"
     Region          257..260
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409562"
     Region          264..270
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409562"
     Region          277..284
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409562"
     Region          290..298
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409562"
     Region          300..397
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            309
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Region          318..322
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..335
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          363..367
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          377..382
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          390..393
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          401..479
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Site            419
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Site            445
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Site            474
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Region          496..588
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(496,561,576)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            562
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Site            order(577..578,580..581)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          594..678
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(594,658,673)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(674..675,677..678)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            698..718
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O35136.1)"
     Region          764..810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O35136.1)"
     Site            765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (O35136.1)"
     CDS             1..837
                     /gene="Ncam2"
                     /gene_synonym="Ncam-2; Ocam; RNCAM"
                     /coded_by="NM_001113208.1:218..2731"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS49888.1"
                     /db_xref="GeneID:17968"
                     /db_xref="MGI:MGI:97282"
ORIGIN      
        1 mslllsfyll gllvrsgqal lqvtislskv elsvgeskff tctaigepes idwynpqgek
       61 iistqrvmlq kegvrsrlti ynaniedagi yrcqatdakg qtqeatvvle iyqkltfrev
      121 vspqefkqge daevvcrvss spapavswly hneevttipd nrfavlannn lqilninksd
      181 egiyrcegrv eargeidfrd iivivnvppa immpqksfna taergeemtl tckasgspdp
      241 tiswfrngkl ieenekyilk gsnteltvrn iinkdggsyv ckatnkaged qkqaflqvfv
      301 qphilqlkne ttsenghvtl vceaegepvp eitwkraidg vmfsegdksp dgrievkgqh
      361 grsslhirdv klsdsgrydc eaasrigghq rsmhldieya pkfvsnqtmy yswegnpini
      421 scdvtanppa sihwrrekll lpakntthlk thsvgrkmil eiaptsdndf grynctatnr
      481 igtrfqeyil eladvpssph gvkiielsqt takisfnkpe shggvpihhy qvdvkevase
      541 twkivrshgv qtmvvlssle pnttyeirva avngkgqgdy skieifqtlp vrepsppsih
      601 gqpssgksfk isitkqddgg apileyivky rskdkedqwl ekkvqgnkdh iilehlqwtm
      661 gyevqitaan rlgyseptvy efsmppkpni ikdtlfnglg lgaiiglgva alllilvvtd
      721 vscffirqcg llmcitrrmc gkksgssgks keleegkaay lkdgskepiv emrtederit
      781 nhedgspvne pnettpltep eklplkeeng kevlnaetie ikvsndiiqs keddika
//
