ID   NCAN_MOUSE              Reviewed;        1268 AA.
AC   P55066; Q6P1E3; Q8C4F8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Neurocan core protein;
DE   AltName: Full=Chondroitin sulfate proteoglycan 3;
DE   Flags: Precursor;
GN   Name=Ncan; Synonyms=Cspg3;
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].
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=7490074; DOI=10.1006/geno.1995.1168;
RA   Rauch U., Grimpe B., Kulbe G., Arnold-Ammer I., Beier D., Faessler R.;
RT   "Structure and chromosomal localization of the mouse neurocan gene.";
RL   Genomics 28:405-410(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1052-1268.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
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 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 {ECO:0000250|UniProtKB:O14594}.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate.
CC       {ECO:0000250|UniProtKB:O14594}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Neurocan;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_156";
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DR   EMBL; X84727; CAA59216.1; -; mRNA.
DR   EMBL; BC065118; AAH65118.1; -; mRNA.
DR   EMBL; AK082298; BAC38458.1; -; mRNA.
DR   CCDS; CCDS22358.1; -.
DR   PIR; S52781; S52781.
DR   RefSeq; NP_031815.2; NM_007789.3.
DR   AlphaFoldDB; P55066; -.
DR   SMR; P55066; -.
DR   BioGRID; 198950; 9.
DR   IntAct; P55066; 7.
DR   MINT; P55066; -.
DR   STRING; 10090.ENSMUSP00000002412; -.
DR   GlyConnect; 2545; 29 N-Linked glycans (4 sites).
DR   GlyCosmos; P55066; 5 sites, 13 glycans.
DR   GlyGen; P55066; 8 sites, 13 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P55066; -.
DR   PhosphoSitePlus; P55066; -.
DR   SwissPalm; P55066; -.
DR   CPTAC; non-CPTAC-3484; -.
DR   MaxQB; P55066; -.
DR   PaxDb; 10090-ENSMUSP00000002412; -.
DR   PeptideAtlas; P55066; -.
DR   ProteomicsDB; 287451; -.
DR   GeneID; 13004; -.
DR   KEGG; mmu:13004; -.
DR   UCSC; uc009lys.2; mouse.
DR   AGR; MGI:104694; -.
DR   CTD; 1463; -.
DR   MGI; MGI:104694; Ncan.
DR   eggNOG; ENOG502QQ78; Eukaryota.
DR   InParanoid; P55066; -.
DR   OrthoDB; 5402504at2759; -.
DR   PhylomeDB; P55066; -.
DR   TreeFam; TF332134; -.
DR   Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR   Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR   Reactome; R-MMU-2024101; CS/DS degradation.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   BioGRID-ORCS; 13004; 4 hits in 77 CRISPR screens.
DR   ChiTaRS; Ncan; mouse.
DR   PRO; PR:P55066; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P55066; Protein.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0072534; C:perineuronal net; ISO:MGI.
DR   GO; GO:0098966; C:perisynaptic extracellular matrix; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
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:0010001; P:glial cell differentiation; IBA:GO_Central.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR   GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR   CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR   PANTHER; PTHR22804:SF24; NEUROCAN CORE PROTEIN; 1.
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; SSF56436; C-type lectin-like; 3.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 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; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hyaluronic acid; Immunoglobulin domain; Lectin; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1268
FT                   /note="Neurocan core protein"
FT                   /id="PRO_0000017517"
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          960..996
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          998..1034
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1036..1165
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DOMAIN          1165..1225
FT                   /note="Sushi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          363..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1228..1268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1228..1253
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1254..1268
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:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:O14594"
FT   CARBOHYD        410
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:O14594"
FT   CARBOHYD        742
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        978
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1175
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        964..975
FT                   /evidence="ECO:0000250"
FT   DISULFID        969..984
FT                   /evidence="ECO:0000250"
FT   DISULFID        986..995
FT                   /evidence="ECO:0000250"
FT   DISULFID        1002..1013
FT                   /evidence="ECO:0000250"
FT   DISULFID        1007..1022
FT                   /evidence="ECO:0000250"
FT   DISULFID        1024..1033
FT                   /evidence="ECO:0000250"
FT   DISULFID        1040..1051
FT                   /evidence="ECO:0000250"
FT   DISULFID        1068..1160
FT                   /evidence="ECO:0000250"
FT   DISULFID        1136..1152
FT                   /evidence="ECO:0000250"
FT   DISULFID        1167..1210
FT                   /evidence="ECO:0000250"
FT   DISULFID        1196..1223
FT                   /evidence="ECO:0000250"
FT   CONFLICT        582
FT                   /note="E -> D (in Ref. 2; AAH65118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        587
FT                   /note="P -> A (in Ref. 2; AAH65118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        936
FT                   /note="V -> D (in Ref. 2; AAH65118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        947
FT                   /note="E -> K (in Ref. 2; AAH65118)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1268 AA;  137200 MW;  3014E8E202A2FAEC CRC64;
     MGAGSVWASG LLLLWLLLLV AGDQDTQDTT ATEKGLRMLK SGSGPVRAAL AELVALPCFF
     TLQPRLSSLR DIPRIKWTKV QTASGQRQDL PILVAKDNVV RVAKGWQGRV SLPAYPRHRA
     NATLLLGPLR ASDSGLYRCQ VVKGIEDEQD LVTLEVTGVV FHYRAARDRY ALTFAEAQEA
     CRLSSATIAA PRHLQAAFED GFDNCDAGWL SDRTVRYPIT QSRPGCYGDR SSLPGVRSYG
     RRDPQELYDV YCFARELGGE VFYVGPARRL TLAGARAQCQ RQGAALASVG QLHLAWHEGL
     DQCDPGWLAD GSVRYPIQTP RRRCGGPAPG VRTVYRFANR TGFPAPGARF DAYCFRAHHH
     TAQHGDSEIP SSGDEGEIVS AEGPPGRELK PSLGEQEVIA PDFQEPLMSS GEGEPPDLTW
     TQAPEETLGS TPGGPTLASW PSSEKWLFTG APSSMGVSSP SDMGVDMEAT TPLGTQVAPT
     PTMRRGRFKG LNGRHFQQQG PEDQLPEVAE PSAQPPTLGA TANHMRPSAA TEASESDQSH
     SPWAILTNEV DEPGAGSLGS RSLPESLMWS PSLISPSVPS TESTPSPKPG AAEAPSVKSA
     IPHLPRLPSE PPAPSPGPSE ALSAVSLQAS SADGSPDFPI VAMLRAPKLW LLPRSTLVPN
     MTPVPLSPAS PLPSWVPEEQ AVRPVSLGAE DLETPFQTTI AAPVEASHRS PDADSIEIEG
     TSSMRATKHP ISGPWASLDS SNVTMNPVPS DAGILGTESG VLDLPGSPTS GGQATVEKVL
     ATWLPLPGQG LDPGSQSTPM EAHGVAVSME PTVALEGGAT EGPMEATREV VPSTADATWE
     SESRSAISST HIAVTMARAQ GMPTLTSTSS EGHPEPKGQM VAQESLEPLN TLPSHPWSSL
     VVPMDEVASV SSGEPTGLWD IPSTLIPVSL GLDESVLNVV AESPSVEGFW EEVASGQEDP
     TDPCENNPCL HGGTCHTNGT VYGCSCDQGY AGENCEIDID DCLCSPCENG GTCIDEVNGF
     ICLCLPSYGG SLCEKDTEGC DRGWHKFQGH CYRYFAHRRA WEDAERDCRR RAGHLTSVHS
     PEEHKFINSF GHENSWIGLN DRTVERDFQW TDNTGLQYEN WREKQPDNFF AGGEDCVVMV
     AHESGRWNDV PCNYNLPYVC KKGTVLCGPP PAVENASLVG VRKIKYNVHA TVRYQCDEGF
     SQHRVATIRC RNNGKWDRPQ IMCIKPRRSH RMRRHHHHPH RHHKPRKEHR KHKRHPAEDW
     EKDEGDFC
//