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Protein

Neuronal cell adhesion molecule

Gene

Nrcam

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding (PubMed:11564762). Plays a role in mediating cell-cell contacts between Schwann cells and axons (PubMed:20188654). Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters (PubMed:14602817, PubMed:20188654). Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier (PubMed:24719088).5 Publications

GO - Molecular functioni

  • ankyrin binding Source: UniProtKB
  • protein binding involved in heterotypic cell-cell adhesion Source: MGI

GO - Biological processi

  • angiogenesis Source: Ensembl
  • axon guidance Source: UniProtKB
  • central nervous system development Source: UniProtKB
  • clustering of voltage-gated sodium channels Source: UniProtKB
  • heterotypic cell-cell adhesion Source: GOC
  • neuronal action potential propagation Source: MGI
  • protein localization Source: MGI
  • regulation of neuron projection development Source: MGI
  • retinal ganglion cell axon guidance Source: MGI
  • single organismal cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-447043. Neurofascin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuronal cell adhesion molecule
Short name:
Nr-CAM
Alternative name(s):
Neuronal surface protein Bravo
Short name:
mBravo
NgCAM-related cell adhesion molecule
Short name:
Ng-CAM-related
Gene namesi
Name:Nrcam
Synonyms:Kiaa0343
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:104750. Nrcam.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 11191090ExtracellularSequence analysisAdd
BLAST
Transmembranei1120 – 114223HelicalSequence analysisAdd
BLAST
Topological domaini1143 – 1256114CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: MGI
  • extracellular region Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: MGI
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are born at the expected Mendelian rate, are viable and fertile. They present no obvious phenotype excepting subtle size differences of cerebellar lobes IV and V. Contrary to wild-type, cerebellar cells do not form neurites when plated on a surface coated with contactin (in vitro) (PubMed:11564762). Neonates present delayed formation of sodium channel clusters at developing nodes of Ranvier, but are indistiguishable from wild-type at 10 days after birth (PubMed:14602817, PubMed:20188654). Mice lacking both Gldn and Nrcam are born at the expected Mendelian rate, but are smaller than control littermates and display important neurological impairments, in spite of seemingly normal nerve myelination. Motor abnormalities vary betweeen individuals, ranging from ataxia, uncoordinated movements and premature death to weakness of the hind limbs, hypomotility, strongly impaired ability to hang from a horizontal bar with their forelimbs and a tendency to stumble. The motor defects correlate with decreased velocity of nerve conduction and slower propagation of action potentials. Most mice die within 60 days after birth, and none are fertile. Mutant mice display delayed formation of mature nodes of Ranvier; 15 days after birth about 20% of the nodes lack detectable sodium channel clusters. Sodium channel clustering and nerve conduction appear normal 60 and 75 days after birth, but subsequently a gradual disintegration of the nodal protein complexes is seen. About 70% of the mutant nodes present high-density sodium channel clustering at 120 days after birth, as opposed to nearly 100% for wild-type. Contrary to wild-type, in adult nodes of Ranvier the sodium channels are often clustered near the paranode border with an empty gap in the middle. At nodes of Ranvier, Schwann cell microvilli are sparse or absent and show defects in their orientation, resulting in various structural abnormalities at the node and the paranode border (PubMed:24719088).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Chaini30 – 12561227Neuronal cell adhesion moleculePRO_0000015058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 117PROSITE-ProRule annotation
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi161 ↔ 212PROSITE-ProRule annotation
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence analysis
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence analysis
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi286 ↔ 334PROSITE-ProRule annotation
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence analysis
Disulfide bondi376 ↔ 426PROSITE-ProRule annotation
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence analysis
Disulfide bondi470 ↔ 519PROSITE-ProRule annotation
Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence analysis
Disulfide bondi561 ↔ 610PROSITE-ProRule annotation
Glycosylationi613 – 6131N-linked (GlcNAc...)Sequence analysis
Glycosylationi710 – 7101N-linked (GlcNAc...)Sequence analysis
Glycosylationi796 – 7961N-linked (GlcNAc...)Sequence analysis
Glycosylationi852 – 8521N-linked (GlcNAc...)Sequence analysis
Glycosylationi987 – 9871N-linked (GlcNAc...)Sequence analysis
Glycosylationi1003 – 10031N-linked (GlcNAc...)Sequence analysis
Glycosylationi1013 – 10131N-linked (GlcNAc...)Sequence analysis
Glycosylationi1067 – 10671N-linked (GlcNAc...)Sequence analysis
Modified residuei1173 – 11731PhosphothreonineCombined sources
Modified residuei1177 – 11771PhosphotyrosineCombined sources
Modified residuei1178 – 11781PhosphoserineCombined sources
Modified residuei1203 – 12031PhosphoserineCombined sources
Modified residuei1206 – 12061PhosphoserineCombined sources
Modified residuei1223 – 12231PhosphoserineBy similarity
Modified residuei1242 – 12421PhosphoserineCombined sources
Modified residuei1243 – 12431PhosphoserineCombined sources
Modified residuei1247 – 12471PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ810U4.
PaxDbiQ810U4.
PRIDEiQ810U4.

PTM databases

iPTMnetiQ810U4.
PhosphoSiteiQ810U4.

Expressioni

Tissue specificityi

Detected in sciatic nerve (PubMed:14602817, PubMed:20188654, PubMed:24719088). Detected in brain, especially in the cerebellum Purkinje cell layer, inner granule cell layer and molecular layer (at protein level) (PubMed:11564762). Detected in neurons and Schwann cells (PubMed:20188654).4 Publications

Gene expression databases

BgeeiQ810U4.
CleanExiMM_NRCAM.
GenevisibleiQ810U4. MM.

Interactioni

Subunit structurei

Constituent of a NFASC/NRCAM/ankyrin-G complex (Probable). Detected in a complex with CNTN1 and PTPRB (PubMed:11564762). Interacts with GLDN/gliomedin and MYOC (PubMed:16039564, PubMed:23897819).1 Publication3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg1Q811D06EBI-8321816,EBI-514290
Dlg4Q621082EBI-8321816,EBI-300895

Protein-protein interaction databases

BioGridi235320. 2 interactions.
IntActiQ810U4. 3 interactions.
MINTiMINT-3090404.
STRINGi10090.ENSMUSP00000020939.

Structurei

3D structure databases

ProteinModelPortaliQ810U4.
SMRiQ810U4. Positions 632-746, 836-951.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 12889Ig-like C2-type 1Add
BLAST
Domaini135 – 22995Ig-like C2-type 2Add
BLAST
Domaini261 – 35090Ig-like C2-type 3Add
BLAST
Domaini355 – 44288Ig-like C2-type 4Add
BLAST
Domaini448 – 53588Ig-like C2-type 5Add
BLAST
Domaini539 – 62688Ig-like C2-type 6Add
BLAST
Domaini643 – 73896Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini740 – 83798Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini842 – 944103Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini948 – 104598Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
GeneTreeiENSGT00760000118840.
HOGENOMiHOG000231380.
HOVERGENiHBG000144.
InParanoidiQ810U4.
KOiK06756.
OMAiAEGDSGF.
OrthoDBiEOG7R56RM.
PhylomeDBiQ810U4.
TreeFamiTF351098.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR026966. Neurofascin/L1/NrCAM_C.
[Graphical view]
PfamiPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 4 hits.
PF07679. I-set. 4 hits.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q810U4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQLKIMPKKK HLSAGGVPLI LFLCQMISAL DVPLDLVQPP TITQQSPKDY
60 70 80 90 100
IIDPRENIVI QCEAKGKPPP SFSWTRNGTH FDIDKDPLVT MKPGSGTLVI
110 120 130 140 150
NIMSEGKAET YEGVYQCTAR NERGAAVSNN IVVRPSRSPL WTKERLEPIV
160 170 180 190 200
LQNGQSLVLP CRPPIGLPPA IIFWMDNSFQ RLPQSERVSQ GLNGDLYFSN
210 220 230 240 250
VLPEDTREDY ICYARFNHTQ TIQQKQPISL KVISVDELND TIAANLSDTE
260 270 280 290 300
FYGAKSSKER PPTFLTPEGN ESHKEELRGN VLSLECIAEG LPTPIIYWIK
310 320 330 340 350
EDGMLPANRT FYRNFKKTLQ ITHVSEADSG NYQCIAKNAL GAVHHTISVT
360 370 380 390 400
VKAAPYWIVA PQNLVLSPGE NGTLICRANG NPKPRISWLT NGVPIEIALD
410 420 430 440 450
DPSRKIDGDT IIFSNVQESS SAVYQCNASN KYGYLLANAF VNVLAEPPRI
460 470 480 490 500
LTSANTLYQV IANRPALLDC AFFGSPMPTI EWFKGTKGSA LHEDIYVLHD
510 520 530 540 550
NGTLEIPVAQ KDSTGTYTCV ARNKLGMAKN EVHLEIKDPT RIIKQPEYAV
560 570 580 590 600
VQRGSKVSFE CRVKHDHTLI PTIMWLKDNG ELPNDERFST DKDHLVVSDV
610 620 630 640 650
KDDDGGTYTC TANTTLDSAS ASAVLRVVAP TPTPAPIYDV PNPPFDLELT
660 670 680 690 700
NQLDKSVQLT WTPGDDNNSP ITKFIIEYED AMHDAGLWRH QAEVSGTQTT
710 720 730 740 750
AQLKLSPYVN YSFRVMAENS IGRSMPSEAS EQYLTKAAEP DQNPMAVEGL
760 770 780 790 800
GTEPDNLVIT WKPLNGFQSN GPGLQYKVSW RQKDGDDEWT SVVVANVSKY
810 820 830 840 850
IVSGTPTFVP YLIKVQALND VGFAPEPAAV MGHSGEDLPM VAPGNVRVSV
860 870 880 890 900
VNSTLAEVHW DPVPPKSVRG HLQGYRIYYW KTQSSSKRNR RHIEKKILTF
910 920 930 940 950
QGTKTHGMLP GLQPYSHYAL NVRVVNGKGE GPASTDRGFH TPEGVPSAPS
960 970 980 990 1000
SLKIVNPTLD SLTLEWDPPS HPNGILTEYI LQYQPINSTH ELGPLVDLKI
1010 1020 1030 1040 1050
PANKTRWTLK NLNFSTRYKF YFYAQTSVGP GSQITEEAIT TVDEAGIPPP
1060 1070 1080 1090 1100
DVGAGKGKEE WRKEIVNGSR SFFGLKGLMP GTAYKVRVGA EGDSGFVSSE
1110 1120 1130 1140 1150
DVFETGPAMA SRQVDIATQG WFIGLMCAVA LLILILLIVC FIRRNKGGKY
1160 1170 1180 1190 1200
PVKEKEDAHA DPEIQPMKED DGTFGEYSDA EDHKPLKKGS RTPSDRTVKK
1210 1220 1230 1240 1250
EDSDDSLVDY GEGVNGQFNE DGSFIGQYSG KKEKEPAEGN ESSEAPSPVN

AMNSFV
Length:1,256
Mass (Da):138,522
Last modified:November 14, 2003 - v2
Checksum:iF3F698C2AF3FCFFA
GO
Isoform 2 (identifier: Q810U4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-638: Missing.
     1045-1107: AGIPPPDVGAGKGKEEWRKEIVNGSRSFFGLKGLMPGTAYKVRVGAEGDSGFVSSEDVFETGP → GKK

Note: No experimental confirmation available.
Show »
Length:1,186
Mass (Da):131,274
Checksum:i959FBD8D4384F861
GO
Isoform 3 (identifier: Q810U4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1177-1177: Y → YRSFE

Note: No experimental confirmation available.
Show »
Length:1,260
Mass (Da):139,041
Checksum:iD1CF15B186D22420
GO
Isoform 4 (identifier: Q810U4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     254-259: AKSSKE → GELQWL
     260-1256: Missing.

Note: No experimental confirmation available.
Show »
Length:259
Mass (Da):29,063
Checksum:iEB3687E24A1CABED
GO
Isoform 5 (identifier: Q810U4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     35-35: D → DPKLLHD
     235-254: VDELNDTIAANLSDTEFYGA → GKSSASGLSFNGVYLCGSNY
     255-1256: Missing.

Note: No experimental confirmation available.
Show »
Length:260
Mass (Da):28,964
Checksum:i1794BD3DC8E9A6E2
GO

Sequence cautioni

The sequence BAC65534.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAD65848.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei35 – 351D → DPKLLHD in isoform 5. 1 PublicationVSP_008921
Alternative sequencei235 – 25420VDELN…EFYGA → GKSSASGLSFNGVYLCGSNY in isoform 5. 1 PublicationVSP_008922Add
BLAST
Alternative sequencei254 – 2596AKSSKE → GELQWL in isoform 4. 1 PublicationVSP_008923
Alternative sequencei255 – 12561002Missing in isoform 5. 1 PublicationVSP_008924Add
BLAST
Alternative sequencei260 – 1256997Missing in isoform 4. 1 PublicationVSP_008925Add
BLAST
Alternative sequencei629 – 63810Missing in isoform 2. 1 PublicationVSP_008926
Alternative sequencei1045 – 110763AGIPP…FETGP → GKK in isoform 2. 1 PublicationVSP_008927Add
BLAST
Alternative sequencei1177 – 11771Y → YRSFE in isoform 3. 1 PublicationVSP_008930

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ543321 mRNA. Translation: CAD65848.1. Different initiation.
AK122252 mRNA. Translation: BAC65534.1. Different initiation.
AK039322 mRNA. Translation: BAC30318.1.
AK048567 mRNA. Translation: BAC33377.1.
AK045259 mRNA. Translation: BAC32284.1.
CCDSiCCDS49056.1. [Q810U4-1]
CCDS49057.1. [Q810U4-2]
RefSeqiNP_001139503.1. NM_001146031.1. [Q810U4-2]
NP_795904.3. NM_176930.4. [Q810U4-1]
UniGeneiMm.208439.

Genome annotation databases

EnsembliENSMUST00000020939; ENSMUSP00000020939; ENSMUSG00000020598. [Q810U4-1]
ENSMUST00000110748; ENSMUSP00000106376; ENSMUSG00000020598. [Q810U4-2]
GeneIDi319504.
KEGGimmu:319504.
UCSCiuc007nls.2. mouse. [Q810U4-5]
uc007nlt.2. mouse. [Q810U4-2]
uc007nlu.2. mouse. [Q810U4-1]
uc007nlw.1. mouse. [Q810U4-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ543321 mRNA. Translation: CAD65848.1. Different initiation.
AK122252 mRNA. Translation: BAC65534.1. Different initiation.
AK039322 mRNA. Translation: BAC30318.1.
AK048567 mRNA. Translation: BAC33377.1.
AK045259 mRNA. Translation: BAC32284.1.
CCDSiCCDS49056.1. [Q810U4-1]
CCDS49057.1. [Q810U4-2]
RefSeqiNP_001139503.1. NM_001146031.1. [Q810U4-2]
NP_795904.3. NM_176930.4. [Q810U4-1]
UniGeneiMm.208439.

3D structure databases

ProteinModelPortaliQ810U4.
SMRiQ810U4. Positions 632-746, 836-951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi235320. 2 interactions.
IntActiQ810U4. 3 interactions.
MINTiMINT-3090404.
STRINGi10090.ENSMUSP00000020939.

PTM databases

iPTMnetiQ810U4.
PhosphoSiteiQ810U4.

Proteomic databases

MaxQBiQ810U4.
PaxDbiQ810U4.
PRIDEiQ810U4.

Protocols and materials databases

DNASUi319504.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020939; ENSMUSP00000020939; ENSMUSG00000020598. [Q810U4-1]
ENSMUST00000110748; ENSMUSP00000106376; ENSMUSG00000020598. [Q810U4-2]
GeneIDi319504.
KEGGimmu:319504.
UCSCiuc007nls.2. mouse. [Q810U4-5]
uc007nlt.2. mouse. [Q810U4-2]
uc007nlu.2. mouse. [Q810U4-1]
uc007nlw.1. mouse. [Q810U4-4]

Organism-specific databases

CTDi4897.
MGIiMGI:104750. Nrcam.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
GeneTreeiENSGT00760000118840.
HOGENOMiHOG000231380.
HOVERGENiHBG000144.
InParanoidiQ810U4.
KOiK06756.
OMAiAEGDSGF.
OrthoDBiEOG7R56RM.
PhylomeDBiQ810U4.
TreeFamiTF351098.

Enzyme and pathway databases

ReactomeiR-MMU-447043. Neurofascin interactions.

Miscellaneous databases

ChiTaRSiNrcam. mouse.
NextBioi394866.
PROiQ810U4.
SOURCEiSearch...

Gene expression databases

BgeeiQ810U4.
CleanExiMM_NRCAM.
GenevisibleiQ810U4. MM.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003006. Ig/MHC_CS.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR026966. Neurofascin/L1/NrCAM_C.
[Graphical view]
PfamiPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 4 hits.
PF07679. I-set. 4 hits.
PF13895. Ig_2. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
PS00290. IG_MHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression patterns of L1-family cell recognition molecules L1, CHL1, NrCAM, and neurofascin in the mouse brain."
    Dirks P., Montag-Sallaz M., Montag D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Swiss Webster.
    Tissue: Brain.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1094-1256 (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Spinal cord.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 432-449 AND 705-723, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Overlapping functions of the cell adhesion molecules Nr-CAM and L1 in cerebellar granule cell development."
    Sakurai T., Lustig M., Babiarz J., Furley A.J., Tait S., Brophy P.J., Brown S.A., Brown L.Y., Mason C.A., Grumet M.
    J. Cell Biol. 154:1259-1273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBUNIT.
  6. "The role of the ankyrin-binding protein NrCAM in node of Ranvier formation."
    Custer A.W., Kazarinova-Noyes K., Sakurai T., Xu X., Simon W., Grumet M., Shrager P.
    J. Neurosci. 23:10032-10039(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. "Gliomedin mediates Schwann cell-axon interaction and the molecular assembly of the nodes of Ranvier."
    Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I., Bermingham J.R. Jr., Peles E.
    Neuron 47:215-229(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GLDN.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1173; TYR-1177; SER-1178; SER-1203; SER-1206; SER-1242; SER-1243 AND SER-1247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Lung.
  9. "A glial signal consisting of gliomedin and NrCAM clusters axonal Na+ channels during the formation of nodes of Ranvier."
    Feinberg K., Eshed-Eisenbach Y., Frechter S., Amor V., Salomon D., Sabanay H., Dupree J.L., Grumet M., Brophy P.J., Shrager P., Peles E.
    Neuron 65:490-502(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
  10. "Myocilin mediates myelination in the peripheral nervous system through ErbB2/3 signaling."
    Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C., Tomarev S.I.
    J. Biol. Chem. 288:26357-26371(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYOC.
  11. "Long-term maintenance of Na+ channels at nodes of Ranvier depends on glial contact mediated by gliomedin and NrCAM."
    Amor V., Feinberg K., Eshed-Eisenbach Y., Vainshtein A., Frechter S., Grumet M., Rosenbluth J., Peles E.
    J. Neurosci. 34:5089-5098(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNRCAM_MOUSE
AccessioniPrimary (citable) accession number: Q810U4
Secondary accession number(s): Q80U33
, Q8BLG8, Q8BX92, Q8BYJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: January 20, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.