GenomeNet

Database: UniProt
Entry: P55066
LinkDB: P55066
Original site: P55066 
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   13-FEB-2019, entry version 169.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   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
CC       and N-CAM). Chondroitin sulfate proteoglycan; binds to hyaluronic
CC       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";
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   UniGene; Mm.268079; -.
DR   ProteinModelPortal; P55066; -.
DR   SMR; P55066; -.
DR   BioGrid; 198950; 5.
DR   IntAct; P55066; 8.
DR   MINT; P55066; -.
DR   STRING; 10090.ENSMUSP00000002412; -.
DR   PhosphoSitePlus; P55066; -.
DR   MaxQB; P55066; -.
DR   PaxDb; P55066; -.
DR   PeptideAtlas; P55066; -.
DR   PRIDE; P55066; -.
DR   GeneID; 13004; -.
DR   KEGG; mmu:13004; -.
DR   UCSC; uc009lys.2; mouse.
DR   CTD; 1463; -.
DR   MGI; MGI:104694; Ncan.
DR   eggNOG; ENOG410IJ1R; Eukaryota.
DR   eggNOG; ENOG410YR39; LUCA.
DR   HOGENOM; HOG000170487; -.
DR   HOVERGEN; HBG078994; -.
DR   InParanoid; P55066; -.
DR   KO; K06794; -.
DR   OrthoDB; 174823at2759; -.
DR   PhylomeDB; P55066; -.
DR   TreeFam; TF332134; -.
DR   PRO; PR:P55066; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IPR013032; EGF-like_CS.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hyaluronic acid; Immunoglobulin domain;
KW   Lectin; Proteoglycan; Reference proteome; Repeat; Secreted; Signal;
KW   Sushi.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23   1268       Neurocan core protein.
FT                                /FTId=PRO_0000017517.
FT   DOMAIN       37    157       Ig-like V-type.
FT   DOMAIN      159    254       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      258    356       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      960    996       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      998   1034       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1036   1165       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN     1165   1225       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    339    339       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    742    742       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    978    978       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1175   1175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     58    139       {ECO:0000250}.
FT   DISULFID    181    252       {ECO:0000250}.
FT   DISULFID    205    226       {ECO:0000250}.
FT   DISULFID    279    354       {ECO:0000250}.
FT   DISULFID    303    324       {ECO:0000250}.
FT   DISULFID    964    975       {ECO:0000250}.
FT   DISULFID    969    984       {ECO:0000250}.
FT   DISULFID    986    995       {ECO:0000250}.
FT   DISULFID   1002   1013       {ECO:0000250}.
FT   DISULFID   1007   1022       {ECO:0000250}.
FT   DISULFID   1024   1033       {ECO:0000250}.
FT   DISULFID   1040   1051       {ECO:0000250}.
FT   DISULFID   1068   1160       {ECO:0000250}.
FT   DISULFID   1136   1152       {ECO:0000250}.
FT   DISULFID   1167   1210       {ECO:0000250}.
FT   DISULFID   1196   1223       {ECO:0000250}.
FT   CONFLICT    582    582       E -> D (in Ref. 2; AAH65118).
FT                                {ECO:0000305}.
FT   CONFLICT    587    587       P -> A (in Ref. 2; AAH65118).
FT                                {ECO:0000305}.
FT   CONFLICT    936    936       V -> D (in Ref. 2; AAH65118).
FT                                {ECO:0000305}.
FT   CONFLICT    947    947       E -> K (in Ref. 2; AAH65118).
FT                                {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
//
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