NCAN_MOUSE
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 03-AUG-2022, entry version 186.
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}.
CC -!- TISSUE SPECIFICITY: Brain.
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; 8.
DR IntAct; P55066; 7.
DR MINT; P55066; -.
DR STRING; 10090.ENSMUSP00000002412; -.
DR GlyConnect; 2545; 13 N-Linked glycans (2 sites).
DR GlyGen; P55066; 5 sites, 13 N-linked glycans (2 sites).
DR PhosphoSitePlus; P55066; -.
DR CPTAC; non-CPTAC-3484; -.
DR MaxQB; P55066; -.
DR PaxDb; P55066; -.
DR PeptideAtlas; P55066; -.
DR PRIDE; P55066; -.
DR ProteomicsDB; 287451; -.
DR GeneID; 13004; -.
DR KEGG; mmu:13004; -.
DR UCSC; uc009lys.2; mouse.
DR CTD; 1463; -.
DR MGI; MGI:104694; Ncan.
DR eggNOG; ENOG502QQ78; Eukaryota.
DR InParanoid; P55066; -.
DR OrthoDB; 174823at2759; -.
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 72 CRISPR screens.
DR ChiTaRS; Ncan; mouse.
DR PRO; PR:P55066; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P55066; protein.
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; ISO:MGI.
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: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 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; 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 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
