NCAM1_RAT
ID NCAM1_RAT Reviewed; 858 AA.
AC P13596;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Neural cell adhesion molecule 1;
DE Short=N-CAM-1;
DE Short=NCAM-1;
DE AltName: CD_antigen=CD56;
DE Flags: Precursor;
GN Name=Ncam1; Synonyms=Ncam;
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].
RC TISSUE=Brain;
RX PubMed=3680385; DOI=10.1083/jcb.105.5.2335;
RA Small S.J., Shull G.E., Santoni M.-J., Akeson R.;
RT "Identification of a cDNA clone that contains the complete coding sequence
RT for a 140-kD rat NCAM polypeptide.";
RL J. Cell Biol. 105:2335-2345(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 340-381.
RX PubMed=1699951; DOI=10.1083/jcb.111.5.2089;
RA Small S.J., Akeson R.;
RT "Expression of the unique NCAM VASE exon is independently regulated in
RT distinct tissues during development.";
RL J. Cell Biol. 111:2089-2096(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 355-364.
RX PubMed=2483093; DOI=10.1016/0896-6273(88)90158-4;
RA Small S.J., Haines S.L., Akeson R.A.;
RT "Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold
RT is developmentally regulated through alternative splicing.";
RL Neuron 1:1007-1017(1988).
RN [4]
RP PROTEIN SEQUENCE OF 38-48 AND 594-605, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780 AND SER-784, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC -!- SUBUNIT: Interacts with MDK. {ECO:0000250|UniProtKB:P13595}.
CC -!- INTERACTION:
CC P13596; Q63237: Fgfr2; NbExp=2; IntAct=EBI-916499, EBI-8523405;
CC P13596; P16092: Fgfr1; Xeno; NbExp=2; IntAct=EBI-916499, EBI-7953898;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1; Synonyms=N-CAM 140;
CC IsoId=P13596-1; Sequence=Displayed;
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; X06564; CAA29809.1; -; mRNA.
DR EMBL; M32611; AAA41679.1; -; Genomic_DNA.
DR PIR; S00846; IJRTNC.
DR RefSeq; NP_113709.1; NM_031521.1. [P13596-1]
DR PDB; 1EPF; X-ray; 1.85 A; A/B/C/D=20-208.
DR PDB; 1LWR; NMR; -; A=612-705.
DR PDB; 1QZ1; X-ray; 2.00 A; A=20-308.
DR PDBsum; 1EPF; -.
DR PDBsum; 1LWR; -.
DR PDBsum; 1QZ1; -.
DR AlphaFoldDB; P13596; -.
DR BMRB; P13596; -.
DR SMR; P13596; -.
DR BioGRID; 246729; 18.
DR CORUM; P13596; -.
DR IntAct; P13596; 4.
DR MINT; P13596; -.
DR STRING; 10116.ENSRNOP00000048442; -.
DR GlyGen; P13596; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P13596; -.
DR PhosphoSitePlus; P13596; -.
DR SwissPalm; P13596; -.
DR jPOST; P13596; -.
DR PaxDb; P13596; -.
DR PRIDE; P13596; -.
DR GeneID; 24586; -.
DR KEGG; rno:24586; -.
DR UCSC; RGD:67378; rat. [P13596-1]
DR CTD; 4684; -.
DR RGD; 67378; Ncam1.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; P13596; -.
DR OrthoDB; 129648at2759; -.
DR PhylomeDB; P13596; -.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-419037; NCAM1 interactions.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR EvolutionaryTrace; P13596; -.
DR PRO; PR:P13596; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:RGD.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; TAS:RGD.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0030275; F:LRR domain binding; IPI:RGD.
DR GO; GO:0019902; F:phosphatase binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0007413; P:axonal fasciculation; IMP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; TAS:RGD.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0071241; P:cellular response to inorganic substance; IEP:RGD.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IEP:RGD.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISO:RGD.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; IDA:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0033555; P:multicellular organismal response to stress; IDA:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0048666; P:neuron development; IDA:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:RGD.
DR GO; GO:0001928; P:regulation of exocyst assembly; ISO:RGD.
DR GO; GO:2001260; P:regulation of semaphorin-plexin signaling pathway; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IDA:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0021794; P:thalamus development; IDA:RGD.
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; IPR033019; Ncam1.
DR InterPro; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR12231:SF239; PTHR12231:SF239; 2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
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 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparin-binding;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..858
FT /note="Neural cell adhesion molecule 1"
FT /id="PRO_0000015015"
FT TOPO_DOM 20..721
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 722..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..111
FT /note="Ig-like C2-type 1"
FT DOMAIN 116..205
FT /note="Ig-like C2-type 2"
FT DOMAIN 212..302
FT /note="Ig-like C2-type 3"
FT DOMAIN 309..414
FT /note="Ig-like C2-type 4"
FT DOMAIN 417..502
FT /note="Ig-like C2-type 5"
FT DOMAIN 510..609
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 611..706
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 765..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152..156
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT BINDING 161..165
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000255"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 139..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 235..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 330..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 437..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 22..32
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1EPF"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1EPF"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1EPF"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:1EPF"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:1EPF"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1QZ1"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:1QZ1"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1QZ1"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1QZ1"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:1QZ1"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1QZ1"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:1QZ1"
FT STRAND 295..306
FT /evidence="ECO:0007829|PDB:1QZ1"
FT STRAND 616..622
FT /evidence="ECO:0007829|PDB:1LWR"
FT TURN 623..626
FT /evidence="ECO:0007829|PDB:1LWR"
FT STRAND 627..633
FT /evidence="ECO:0007829|PDB:1LWR"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:1LWR"
FT STRAND 642..654
FT /evidence="ECO:0007829|PDB:1LWR"
FT STRAND 667..673
FT /evidence="ECO:0007829|PDB:1LWR"
FT STRAND 679..688
FT /evidence="ECO:0007829|PDB:1LWR"
FT STRAND 691..701
FT /evidence="ECO:0007829|PDB:1LWR"
SQ SEQUENCE 858 AA; 94658 MW; EA1A06A4EA0550F6 CRC64;
MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE
KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF
KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK
KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF
PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS
IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKASWTRP
EKQETLDGHM VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEVQYAPKLQ
GPVAVYTWEG NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD
SENDFGNYNC TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP
ILKYKAEWKS LGEEAWHSKW YDAKEANMEG IVTIMGLKPE TRYAVRLAAL NGKGLGEISA
ATEFKTQPVR EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI
RLPSGSDHVM LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTAGLS
TGAIVGILIV IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC GKAGPGAKGK DMEEGKAAFS
KDESKEPIVE VRTEEERTPN HDGGKHTEPN ETTPLTEPEK GPVETKSEPQ ESEAKPAPTE
VKTVPNEATQ TKENESKA
