NRCAM_RAT
ID NRCAM_RAT Reviewed; 1214 AA.
AC P97686;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Neuronal cell adhesion molecule;
DE Short=Nr-CAM;
DE AltName: Full=Ankyrin-binding cell adhesion molecule NrCAM;
DE AltName: Full=Neuronal surface protein Bravo;
DE Short=rBravo;
DE AltName: Full=NgCAM-related cell adhesion molecule;
DE Short=Ng-CAM-related;
DE Flags: Precursor;
GN Name=Nrcam;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE OF 30-1214
RP (ISOFORMS 2 AND 3), CHARACTERIZATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8947556; DOI=10.1083/jcb.135.5.1355;
RA Davis J.Q., Lambert S., Bennett V.;
RT "Molecular composition of the node of Ranvier: identification of ankyrin-
RT binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-)
RT and NrCAM at nodal axon segments.";
RL J. Cell Biol. 135:1355-1367(1996).
RN [2]
RP FUNCTION, AND INTERACTION WITH GLDN.
RX PubMed=16039564; DOI=10.1016/j.neuron.2005.06.026;
RA Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I.,
RA Bermingham J.R. Jr., Peles E.;
RT "Gliomedin mediates Schwann cell-axon interaction and the molecular
RT assembly of the nodes of Ranvier.";
RL Neuron 47:215-229(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1131; SER-1136; SER-1200;
RP SER-1201 AND SER-1205, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-223; ASN-802 AND ASN-993, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Cell adhesion protein that is required for normal responses
CC to cell-cell contacts in brain and in the peripheral nervous system.
CC Plays a role in neurite outgrowth in response to contactin binding.
CC Plays a role in mediating cell-cell contacts between Schwann cells and
CC axons (By similarity). Plays a role in the formation and maintenance of
CC the nodes of Ranvier on myelinated axons (PubMed:16039564). Nodes of
CC Ranvier contain clustered sodium channels that are crucial for the
CC saltatory propagation of action potentials along myelinated axons.
CC During development, nodes of Ranvier are formed by the fusion of two
CC heminodes. Required for normal clustering of sodium channels at
CC heminodes; not required for the formation of mature nodes with normal
CC sodium channel clusters. Required, together with GLDN, for maintaining
CC NFASC and sodium channel clusters at mature nodes of Ranvier.
CC {ECO:0000250|UniProtKB:Q810U4, ECO:0000269|PubMed:16039564}.
CC -!- SUBUNIT: Constituent of a NFASC/NRCAM/ankyrin-G complex. Detected in a
CC complex with CNTN1 and PTPRB. Interacts with MYOC (By similarity).
CC Interacts with GLDN (PubMed:16039564). {ECO:0000250|UniProtKB:Q810U4,
CC ECO:0000269|PubMed:16039564}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8947556};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q810U4}.
CC Cell projection, axon {ECO:0000269|PubMed:8947556}. Secreted
CC {ECO:0000250|UniProtKB:Q810U4}. Note=Localized to axonal membranes at
CC the node of Ranvier of myelinated axons (PubMed:8947556).
CC {ECO:0000269|PubMed:8947556}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P97686-1; Sequence=Displayed;
CC Name=2; Synonyms=Nr-CAM 22;
CC IsoId=P97686-2; Sequence=VSP_008932;
CC Name=3; Synonyms=Nr-CAM 12;
CC IsoId=P97686-3; Sequence=VSP_008931, VSP_008933, VSP_008934;
CC -!- TISSUE SPECIFICITY: Detected in cerebellum Purkinje cells. Detected on
CC nodes of Ranvier and unmyelinated axons in sciatic nerve (at protein
CC level). {ECO:0000269|PubMed:8947556}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB47755.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U81037; AAB47755.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; P97686; -.
DR SMR; P97686; -.
DR STRING; 10116.ENSRNOP00000044341; -.
DR GlyGen; P97686; 16 sites, 17 N-linked glycans (4 sites).
DR iPTMnet; P97686; -.
DR PhosphoSitePlus; P97686; -.
DR PaxDb; P97686; -.
DR PRIDE; P97686; -.
DR ABCD; P97686; 1 sequenced antibody.
DR UCSC; RGD:3209; rat. [P97686-1]
DR RGD; 3209; Nrcam.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; P97686; -.
DR PhylomeDB; P97686; -.
DR PRO; PR:P97686; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043194; C:axon initial segment; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0033268; C:node of Ranvier; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0030506; F:ankyrin binding; ISS:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISS:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
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; IPR003006; Ig/MHC_CS.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR10075; PTHR10075; 2.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1214
FT /note="Neuronal cell adhesion molecule"
FT /id="PRO_0000015059"
FT TOPO_DOM 30..1077
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1078..1100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1101..1214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..134
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..235
FT /note="Ig-like C2-type 2"
FT DOMAIN 267..356
FT /note="Ig-like C2-type 3"
FT DOMAIN 361..448
FT /note="Ig-like C2-type 4"
FT DOMAIN 454..541
FT /note="Ig-like C2-type 5"
FT DOMAIN 545..626
FT /note="Ig-like C2-type 6"
FT DOMAIN 649..744
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 746..843
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 848..950
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 954..1051
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1109..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1135
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 167..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 292..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 382..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 476..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 567..616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 36..41
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008931"
FT VAR_SEQ 241..259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_008932"
FT VAR_SEQ 635..644
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008933"
FT VAR_SEQ 1051..1065
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008934"
SQ SEQUENCE 1214 AA; 133912 MW; 2E5EFC09F040DE68 CRC64;
MQLKTMPKKK PLSAGRAPLF LFLCQMISAL DVPLDPKLLD DLVQPPTITQ QSPKDYIIDP
RENIVIQCEA KGKPPPSFSW TRNGTHFDID KDPLVTMKPG SGTLVINIMS EGKAETYEGV
YQCTARNERG AAVSNNIVVR PSRSPLWTKE RLEPIILRSG QSLVLPCRPP IGLPPAIIFW
MDNSFQRLPQ SERVSQGLNG DLYFSNVLPE DTREDYICYA RFNHTQTIQQ KQPISLKVIS
VDELNDTIAA NLSDTEFYGA KSSKERPPTF LTPEGNESHK EELRGNVLSL ECIAEGLPTP
VIYWIKEDGT LPVNRTFYRN FKKTLQIIHV SEADSGNYQC IAKNALGAVH HTISVTVKAA
PYWIVAPHNL VLSPGENGTL ICRANGNPKP RISWLTNGVP VEIALDDPSR KIDGDTIMFS
NVQESSSAVY QCNASNKYGY LLANAFVNVL AEPPRILTSA NTLYQVIANR PALLDCAFFG
SPMPTIEWFK GTKGSALHED IYVLHDNGTL EIPVAQKDST GTYTCVARNK LGMAKNEVHL
EIKDPTRFIK QPGYAVVQRG SKVSFECKVK HDHTLIPTIL WLKDNGELPN DERFSVDKDH
LVVSDVKDED GGTYTCAANT TLDSVSASAV LRVVAPTPTP APIYDVPNPP FDLELTNQLD
KSVQLTWTPG DDNNSPITKF IIEYEDAMHE AGLWRHQAEV SGTQTTAQLK LSPYVNYSFR
VMAENSIGRS VPSEASEQYL TKAAEPDQNP TAVEGLGTEP DNLVITWKPL NGFQSNGPGL
QYKVSWRQKD GDDEWTSVVV ANVSKYIVSG TPTFVPYLIK VQALNDVGFA PEPAAVMGHS
GEDLPMVAPG NVRVSVVNST LAEAHWDPVP PKSVRGHLQG YRIYYWKAQS SSKRNRRHIE
KKILTFQGSK THGMLPGLQP YSHYVLNVRV VNGKGEGPAS ADRGFHTPEG VPSAPSSLKI
VNPTLDSLTL EWDPPSHPNG ILTEYILKYQ PINSTHELGP LVDLKIPANK TRWTLKNLNF
STRYKFYFYA QTSVGSGSQI TEEAITTVDE GKKAGILPPD VGAGKAMASR QVDIATQGWF
IGLMCAVALL ILILLIVCFI RRNKGGKYPV KEKEDAHADP EIQPMKEDDG TFGEYSDAED
HKPLKKGSRT PSDRTVKKED SDDSLVDYGE GVNGQFNEDG SFIGQYSGKK EKEPAEGNES
SEAPSPVNAM NSFV
