NCAN_PANTR
ID NCAN_PANTR Reviewed; 1321 AA.
AC Q5IS41;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Neurocan core protein;
DE AltName: Full=Chondroitin sulfate proteoglycan 3;
DE Flags: Precursor;
GN Name=NCAN; Synonyms=CSPG3;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
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DR EMBL; AY665287; AAV74325.1; -; mRNA.
DR RefSeq; NP_001029342.1; NM_001034170.1.
DR AlphaFoldDB; Q5IS41; -.
DR SMR; Q5IS41; -.
DR STRING; 9598.ENSPTRP00000018312; -.
DR PaxDb; Q5IS41; -.
DR GeneID; 468775; -.
DR KEGG; ptr:468775; -.
DR CTD; 1463; -.
DR eggNOG; ENOG502QQ78; Eukaryota.
DR InParanoid; Q5IS41; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 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 2: Evidence at transcript 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..1321
FT /note="Neurocan core protein"
FT /id="PRO_0000017518"
FT DOMAIN 38..153
FT /note="Ig-like V-type"
FT DOMAIN 160..255
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 259..357
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 1008..1044
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1046..1082
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1084..1213
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1213..1273
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 362..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1306
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..140
FT /evidence="ECO:0000250"
FT DISULFID 182..253
FT /evidence="ECO:0000250"
FT DISULFID 206..227
FT /evidence="ECO:0000250"
FT DISULFID 280..355
FT /evidence="ECO:0000250"
FT DISULFID 304..325
FT /evidence="ECO:0000250"
FT DISULFID 1012..1023
FT /evidence="ECO:0000250"
FT DISULFID 1017..1032
FT /evidence="ECO:0000250"
FT DISULFID 1034..1043
FT /evidence="ECO:0000250"
FT DISULFID 1050..1061
FT /evidence="ECO:0000250"
FT DISULFID 1055..1070
FT /evidence="ECO:0000250"
FT DISULFID 1072..1081
FT /evidence="ECO:0000250"
FT DISULFID 1088..1099
FT /evidence="ECO:0000250"
FT DISULFID 1116..1208
FT /evidence="ECO:0000250"
FT DISULFID 1184..1200
FT /evidence="ECO:0000250"
FT DISULFID 1215..1258
FT /evidence="ECO:0000250"
FT DISULFID 1244..1271
FT /evidence="ECO:0000250"
SQ SEQUENCE 1321 AA; 142867 MW; 754E0B1D2D9C23D8 CRC64;
MGTPFVWALG LLMLQMLLFV AGEQGTQDIA DASERGLHMQ KLGSGSVQAA LAELVALPCL
FTLQPQPSAA RDAPRIKWTK VRTASGQRQD LPILVAKDNV VKVAKSWQGR VSLPSYPRRR
ANATLLLGPL RASDSGLYRC QVVRGIEDEQ DLVPLEVTGV VFHYRSARDR YALTFAEAQE
ACRLSSAIIA APRHLQAAFE DGFDNCDAGW LSDRTVRYPI TQSRPGCYGD RSSLPGVRSY
GRRNPQELYD VYCFARELGG EVFYVGPARR LTLAGARAQC RRQGAALASV GQLHLAWHEG
LDQCDPGWLA DGSVRYPIQT PRRRCGGPAP GVRTVYRFAN RTGFPSPAER FDAYCFRAHH
PTSQHGDLET PSSGDEGEIL SAEGPPVREL EPTLEEEEVV TPDFQEPLVS SGEEEPLILE
EKQESQQTLS PTPGDPMLAS WPTGEVWLST VAPSPSDMGA GTAASSHTEV APTDPMPRRR
GRFKGLNGRY FQQQEPEPGL QGGMEASAQP PTSEAAGNQM EPPLAMAVTE MLGSGQSRSP
WADLTNEVDM PGAGSAGGKS SPEPWLWPPT MVPPSISGHS RAPVLELEKA EGPSARPATP
DLFWSPLEAT VSAPSPAPWE AFPVATSPDL PMMAMLRGPK EWMLPHPTPI STEANRVEAH
GEATTTPPPS PAAETKVYSL PLSLTPTGQG GEAMPTTPES PGADFRETGE TSPAQVNKAE
HSSSSPWPSV NRNVAVGFVP TETATEPTGL RGISGSESGV LDTAESPTSG LQATVDEVQD
PWPSVYSKGL GASSPSAPLG SPGVFLVPKV TPSLEPWVAT DEGPTVNPMD STVTLAPSDA
SGIWEPGSQV FEEAESTTLS PQVALDTSIV TPLTTLEQGD KVGVPAMSTL GSSSSQPHPE
PEDQVETQGT SGASVPPHQS SPLGKPAVPP GTPTAASVGE SASVSSGEPT VPWDPSSTLL
PVTLGIEDFE LEVLAGSPGV ESFWEEVASG EEPALPGTPM KAGAEEVHSD PCENNPCLHG
GTCNANGTMY GCSCDQGFAG ENCEIDIDDC LCSPCENGGT CIDEVNGFVC LCLPSYGGSF
CEKDTEGCDR GWHKFQGHCY RYFAHRRAWE DAERDCRRRS GHLTSVHSSE EHSFINSFGH
ENTWIGLNDR IVERDFQWTD NTGLQFENWR ENQPDNFFAG GEDCVVMVAH ESGRWNDVPC
NYNLPYVCKK GTVLCGPPPA VENASLIGAR KAKYNVHATV RYQCNEGFAQ HHVATIRCRS
NGKWDRPQIV CTKPRRSHRM RRHHHHHQHH HQHHHHKSRK ERRKHKKHPT EDWEKDEGNF
C
