ID   NCAM2_MOUSE             Reviewed;         837 AA.
AC   O35136; O35962; Q0VF23;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Neural cell adhesion molecule 2;
DE            Short=N-CAM-2;
DE            Short=NCAM-2;
DE   AltName: Full=Neural cell adhesion molecule RB-8;
DE   AltName: Full=R4B12;
DE   Flags: Precursor;
GN   Name=Ncam2; Synonyms=Ocam, Rncam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   STRAIN=BALB/cJ; TISSUE=Olfactory neuroepithelium;
RX   PubMed=9221781; DOI=10.1523/jneurosci.17-15-05830.1997;
RA   Yoshihara Y., Kawasaki M., Tamada A., Fujita H., Hayashi H., Kagamiyama H.,
RA   Mori K.;
RT   "OCAM: a new member of the neural cell adhesion molecule family related to
RT   zone-to-zone projection of olfactory and vomeronasal axons.";
RL   J. Neurosci. 17:5830-5842(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
RX   PubMed=9334170; DOI=10.1074/jbc.272.42.26083;
RA   Alenius M., Bohm S.;
RT   "Identification of a novel neural cell adhesion molecule-related gene with
RT   a potential role in selective axonal projection.";
RL   J. Biol. Chem. 272:26083-26086(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765; THR-780 AND SER-786, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May play important roles in selective fasciculation and zone-
CC       to-zone projection of the primary olfactory axons.
CC   -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: [Isoform Short]: Cell membrane; Lipid-anchor,
CC       GPI-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O35136-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O35136-2; Sequence=VSP_002590;
CC   -!- TISSUE SPECIFICITY: Expressed in subsets of both olfactory and
CC       vomeronasal neurons in a zone-specific manner.
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DR   EMBL; AF001287; AAB69125.1; -; mRNA.
DR   EMBL; AF001286; AAB69124.1; -; mRNA.
DR   EMBL; AF016619; AAC53375.1; -; mRNA.
DR   EMBL; BC119027; AAI19028.1; -; mRNA.
DR   EMBL; BC119029; AAI19030.1; -; mRNA.
DR   CCDS; CCDS28281.1; -. [O35136-2]
DR   CCDS; CCDS49888.1; -. [O35136-1]
DR   RefSeq; NP_001106679.1; NM_001113208.1. [O35136-1]
DR   RefSeq; NP_035084.1; NM_010954.4. [O35136-2]
DR   AlphaFoldDB; O35136; -.
DR   SMR; O35136; -.
DR   BioGRID; 201700; 8.
DR   IntAct; O35136; 1.
DR   MINT; O35136; -.
DR   STRING; 10090.ENSMUSP00000063468; -.
DR   GlyConnect; 2536; 11 N-Linked glycans (4 sites).
DR   GlyCosmos; O35136; 8 sites, 11 glycans.
DR   GlyGen; O35136; 9 sites, 11 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; O35136; -.
DR   PhosphoSitePlus; O35136; -.
DR   SwissPalm; O35136; -.
DR   MaxQB; O35136; -.
DR   PaxDb; 10090-ENSMUSP00000063468; -.
DR   PeptideAtlas; O35136; -.
DR   ProteomicsDB; 287449; -. [O35136-1]
DR   ProteomicsDB; 287450; -. [O35136-2]
DR   Antibodypedia; 22282; 359 antibodies from 38 providers.
DR   DNASU; 17968; -.
DR   Ensembl; ENSMUST00000037785.14; ENSMUSP00000049390.8; ENSMUSG00000022762.19. [O35136-2]
DR   Ensembl; ENSMUST00000067602.5; ENSMUSP00000063468.4; ENSMUSG00000022762.19. [O35136-1]
DR   GeneID; 17968; -.
DR   KEGG; mmu:17968; -.
DR   UCSC; uc007zta.2; mouse. [O35136-2]
DR   UCSC; uc007ztb.2; mouse. [O35136-1]
DR   AGR; MGI:97282; -.
DR   CTD; 4685; -.
DR   MGI; MGI:97282; Ncam2.
DR   VEuPathDB; HostDB:ENSMUSG00000022762; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   GeneTree; ENSGT00940000157860; -.
DR   HOGENOM; CLU_010961_1_0_1; -.
DR   InParanoid; O35136; -.
DR   OMA; XPPAITM; -.
DR   OrthoDB; 5233206at2759; -.
DR   PhylomeDB; O35136; -.
DR   TreeFam; TF326195; -.
DR   BioGRID-ORCS; 17968; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Ncam2; mouse.
DR   PRO; PR:O35136; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; O35136; Protein.
DR   Bgee; ENSMUSG00000022762; Expressed in subiculum and 109 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd20970; IgI_1_MuSK; 1.
DR   CDD; cd05866; IgI_1_NCAM-2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR009138; Neural_cell_adh.
DR   PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1.
DR   PANTHER; PTHR12231:SF231; NEURAL CELL ADHESION MOLECULE 2; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 4.
DR   Pfam; PF13927; Ig_3; 1.
DR   PRINTS; PR01838; NCAMFAMILY.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 5.
DR   SMART; SM00406; IGv; 3.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   Genevisible; O35136; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..837
FT                   /note="Neural cell adhesion molecule 2"
FT                   /id="PRO_0000042589"
FT   TOPO_DOM        20..697
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        698..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        719..837
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          21..108
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          113..202
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          208..297
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          302..396
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          401..491
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          495..591
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          593..688
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          764..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..784
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         765
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         780
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         786
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        419
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        474
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        562
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..93
FT                   /evidence="ECO:0000305"
FT   DISULFID        136..186
FT                   /evidence="ECO:0000305"
FT   DISULFID        232..281
FT                   /evidence="ECO:0000305"
FT   DISULFID        322..380
FT                   /evidence="ECO:0000305"
FT   DISULFID        422..475
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         694..837
FT                   /note="TLFNGLGLGAIIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSG
FT                   SSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERITNHEDGSPVNEPNETTPLTEPEKLP
FT                   LKEENGKEVLNAETIEIKVSNDIIQSKEDDIKA -> NCCEANKGENGGQSWHLNAVGF
FT                   TFVITMSLSCLF (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9221781, ECO:0000303|PubMed:9334170"
FT                   /id="VSP_002590"
FT   LIPID           O35136-2:703
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   837 AA;  93204 MW;  70473B053A2D65A5 CRC64;
     MSLLLSFYLL GLLVRSGQAL LQVTISLSKV ELSVGESKFF TCTAIGEPES IDWYNPQGEK
     IISTQRVMLQ KEGVRSRLTI YNANIEDAGI YRCQATDAKG QTQEATVVLE IYQKLTFREV
     VSPQEFKQGE DAEVVCRVSS SPAPAVSWLY HNEEVTTIPD NRFAVLANNN LQILNINKSD
     EGIYRCEGRV EARGEIDFRD IIVIVNVPPA IMMPQKSFNA TAERGEEMTL TCKASGSPDP
     TISWFRNGKL IEENEKYILK GSNTELTVRN IINKDGGSYV CKATNKAGED QKQAFLQVFV
     QPHILQLKNE TTSENGHVTL VCEAEGEPVP EITWKRAIDG VMFSEGDKSP DGRIEVKGQH
     GRSSLHIRDV KLSDSGRYDC EAASRIGGHQ RSMHLDIEYA PKFVSNQTMY YSWEGNPINI
     SCDVTANPPA SIHWRREKLL LPAKNTTHLK THSVGRKMIL EIAPTSDNDF GRYNCTATNR
     IGTRFQEYIL ELADVPSSPH GVKIIELSQT TAKISFNKPE SHGGVPIHHY QVDVKEVASE
     TWKIVRSHGV QTMVVLSSLE PNTTYEIRVA AVNGKGQGDY SKIEIFQTLP VREPSPPSIH
     GQPSSGKSFK ISITKQDDGG APILEYIVKY RSKDKEDQWL EKKVQGNKDH IILEHLQWTM
     GYEVQITAAN RLGYSEPTVY EFSMPPKPNI IKDTLFNGLG LGAIIGLGVA ALLLILVVTD
     VSCFFIRQCG LLMCITRRMC GKKSGSSGKS KELEEGKAAY LKDGSKEPIV EMRTEDERIT
     NHEDGSPVNE PNETTPLTEP EKLPLKEENG KEVLNAETIE IKVSNDIIQS KEDDIKA
//