NCAM2_MOUSE
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 03-AUG-2022, entry version 179.
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; 7.
DR IntAct; O35136; 1.
DR MINT; O35136; -.
DR STRING; 10090.ENSMUSP00000063468; -.
DR GlyConnect; 2536; 11 N-Linked glycans (4 sites).
DR GlyGen; O35136; 8 sites, 11 N-linked glycans (4 sites).
DR iPTMnet; O35136; -.
DR PhosphoSitePlus; O35136; -.
DR SwissPalm; O35136; -.
DR MaxQB; O35136; -.
DR PaxDb; O35136; -.
DR PeptideAtlas; O35136; -.
DR PRIDE; O35136; -.
DR ProteomicsDB; 287449; -. [O35136-1]
DR ProteomicsDB; 287450; -. [O35136-2]
DR Antibodypedia; 22282; 310 antibodies from 38 providers.
DR DNASU; 17968; -.
DR Ensembl; ENSMUST00000037785; ENSMUSP00000049390; ENSMUSG00000022762. [O35136-2]
DR Ensembl; ENSMUST00000067602; ENSMUSP00000063468; ENSMUSG00000022762. [O35136-1]
DR GeneID; 17968; -.
DR KEGG; mmu:17968; -.
DR UCSC; uc007zta.2; mouse. [O35136-2]
DR UCSC; uc007ztb.2; mouse. [O35136-1]
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; CEANKGE; -.
DR PhylomeDB; O35136; -.
DR TreeFam; TF326195; -.
DR BioGRID-ORCS; 17968; 2 hits in 76 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 108 other tissues.
DR Genevisible; O35136; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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 GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 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 Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 4.
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; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
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
