NCAN_RAT
ID NCAN_RAT Reviewed; 1257 AA.
AC P55067;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Neurocan core protein;
DE AltName: Full=245 kDa early postnatal core glycoprotein;
DE AltName: Full=Chondroitin sulfate proteoglycan 3;
DE Contains:
DE RecName: Full=150 kDa adult core glycoprotein;
DE Flags: Precursor;
GN Name=Ncan; Synonyms=Cspg3;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1326557; DOI=10.1016/s0021-9258(18)41808-x;
RA Rauch U., Karthikeyan L., Maurel P., Margolis R.U., Margolis R.K.;
RT "Cloning and primary structure of neurocan, a developmentally regulated,
RT aggregating chondroitin sulfate proteoglycan of brain.";
RL J. Biol. Chem. 267:19536-19547(1992).
RN [2]
RP CHARACTERIZATION.
RX PubMed=7513709; DOI=10.1083/jcb.125.3.669;
RA Friedlander D.R., Milev P., Karthikeyan L., Margolis R.K., Margolis R.U.,
RA Grumet M.;
RT "The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural
RT cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, and inhibits neuronal
RT adhesion and neurite outgrowth.";
RL J. Cell Biol. 125:669-680(1994).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121, AND IDENTIFICATION BY MASS
RP 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: May modulate neuronal adhesion and neurite growth during
CC development by binding to neural cell adhesion molecules (NG-CAM and N-
CC CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic acid.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Early postnatal and adult brain; not expressed in
CC kidney, lung, liver and muscle.
CC -!- PTM: Contains mostly chondroitin sulfate, but also N-linked and O-
CC linked oligosaccharides. {ECO:0000250}.
CC -!- PTM: Two isoforms were found that probably arise by proteolytic
CC processing. The large isoform is predominant in early postnatal brain,
CC the small isoform is found in adult brain.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
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DR EMBL; M97161; AAC37679.1; -; mRNA.
DR PIR; S28764; S28764.
DR AlphaFoldDB; P55067; -.
DR SMR; P55067; -.
DR IntAct; P55067; 1.
DR MINT; P55067; -.
DR STRING; 10116.ENSRNOP00000062123; -.
DR GlyGen; P55067; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P55067; -.
DR SwissPalm; P55067; -.
DR PaxDb; P55067; -.
DR PRIDE; P55067; -.
DR UCSC; RGD:619941; rat.
DR RGD; 619941; Ncan.
DR eggNOG; ENOG502QQ78; Eukaryota.
DR InParanoid; P55067; -.
DR PhylomeDB; P55067; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-RNO-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR PRO; PR:P55067; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0072534; C:perineuronal net; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000538; Link_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 1.
DR Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 3.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS01241; LINK_1; 2.
DR PROSITE; PS50963; LINK_2; 2.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Hyaluronic acid; Immunoglobulin domain;
KW Lectin; Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..22
FT CHAIN 23..1257
FT /note="Neurocan core protein"
FT /id="PRO_0000017519"
FT CHAIN 639..1257
FT /note="150 kDa adult core glycoprotein"
FT /id="PRO_0000017520"
FT DOMAIN 37..157
FT /note="Ig-like V-type"
FT DOMAIN 159..254
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 258..356
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 949..985
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 987..1023
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1025..1154
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1154..1214
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1242
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 944
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:1326557"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..139
FT /evidence="ECO:0000250"
FT DISULFID 181..252
FT /evidence="ECO:0000250"
FT DISULFID 205..226
FT /evidence="ECO:0000250"
FT DISULFID 279..354
FT /evidence="ECO:0000250"
FT DISULFID 303..324
FT /evidence="ECO:0000250"
FT DISULFID 953..964
FT /evidence="ECO:0000250"
FT DISULFID 958..973
FT /evidence="ECO:0000250"
FT DISULFID 975..984
FT /evidence="ECO:0000250"
FT DISULFID 991..1002
FT /evidence="ECO:0000250"
FT DISULFID 996..1011
FT /evidence="ECO:0000250"
FT DISULFID 1013..1022
FT /evidence="ECO:0000250"
FT DISULFID 1029..1040
FT /evidence="ECO:0000250"
FT DISULFID 1057..1149
FT /evidence="ECO:0000250"
FT DISULFID 1125..1141
FT /evidence="ECO:0000250"
FT DISULFID 1156..1199
FT /evidence="ECO:0000250"
FT DISULFID 1185..1212
FT /evidence="ECO:0000250"
SQ SEQUENCE 1257 AA; 135545 MW; 992B33DCFA19EE1B CRC64;
MGAESVWASG LLVLWLLLLV SGDQDTQDTT TTEKGLHMLK SGSGPIQAAL AELVALPCFF
TLQPRQSPLG DIPRIKWTKV QTASGQRQDL PILVAKDNVV RVAKGWQGRV SLPAYPRHRA
NATLLLGPLR ASDSGLYRCQ VVKGIEDEQD LVTLEVTGVV FHYRAARDRY ALTFAEAQEA
CHLSSATIAA PRHLQAAFED GFDNCDAGWL SDRTVRYPIT QSRPGCYGDR SSLPGVRSYG
RRDPQELYDV YCFARELGGE VFYVGPARRL TLAGARALCQ RQGAALASVG QLHLAWHEGL
DQCDPGWLAD GSVRYPIQTP RRRCGGSAPG VRTVYRFANR TGFPAPGARF DAYCFRAHHH
TPQRGDSEIP SSGDEGEIVS AEGPPAPELK PRLGEQEVIT PDFQEPLVSS GEDEPLDLTR
TQASQETLAS TPGGPTLASW LLTGVTSSTG VPSPSSLGVD MEETTPSGTQ VAPTPTMRRG
RFKGLNGRHF QQQGPEDQLL EAAEASAQPP TLEVTADHMG PSAATEALES DQSHSPWAIL
TNEVDVPGAG SLGSRSLPES RKWSPSLISP STVPSTDSTP GLKPGADEAP GVKSAIHHPP
WLPSEPAVPS SIPSEALSAV SLQASPGDGS PDFPIVAMLR APKLWLLPHS TLVPNVSPIP
LSPASPLPSS VPEEQAVRPV SFGAEDPETP FQTTMAAPGE ASHGSPEADS IEIEGISSMQ
ATKHPISGPW ASLDSSNVTV NPVPSDAGIL GTESGVLDLP GSPTSDGQAT VDMVLATWLP
LPGHGLDTGS QSTPMEAHGV TMSVEPTVAL EGGATKDPME ATMDVVPSTV DATSGSEPKS
SISSTHVVVT AAGDQGTPTL TPTSSEGQVV AQESLGTLTS LPSHPWSSLA SSMDEVASVS
SGEPTRLWDI PSTLIPVSLG LDESDLKVVA ESPGLEGFWE EVASGQEDPT DPCENNPCLH
GGTCRTNGTM YGCSCDQGYA GENCEIDIDD CLCSPCENGG TCIDEVNGFI CLCLPSYGGN
LCEKDTEGCD RGWHKFQGHC YRYFAHRRAW EDAERDCRRR AGHLTSVHSP EEHKFINSFG
HENSWIGLND RTVERDFQWT DNTGLQYENW REKQPDNFFA GGEDCVVMVA HENGRWNDVP
CNYNLPYVCK KGTVLCGPPP AVENASLVGV RKVKYNVHAT VRYQCDEGFS QHHVATIRCR
SNGKWDRPQI VCTKPRRSHR MRRHHHHPHR HHKPRKEHRK HKRHPAEDWE KDEGDFC
