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Database: UniProt
Entry: A0A2K5IHM1_COLAP
LinkDB: A0A2K5IHM1_COLAP
Original site: A0A2K5IHM1_COLAP 
ID   A0A2K5IHM1_COLAP        Unreviewed;      1320 AA.
AC   A0A2K5IHM1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Neurocan {ECO:0008006|Google:ProtNLM};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000016046.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000016046.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000256|ARBA:ARBA00006838}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   RefSeq; XP_011781257.1; XM_011925867.1.
DR   STRING; 336983.ENSCANP00000016046; -.
DR   Ensembl; ENSCANT00000038982.1; ENSCANP00000016046.1; ENSCANG00000031467.1.
DR   GeneID; 105500372; -.
DR   KEGG; cang:105500372; -.
DR   CTD; 1463; -.
DR   OMA; HESGHWN; -.
DR   OrthoDB; 5402504at2759; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:InterPro.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd05902; Ig_Neurocan; 1.
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; 1.
DR   PROSITE; PS50963; LINK_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hyaluronic acid {ECO:0000256|ARBA:ARBA00023290};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1320
FT                   /note="Neurocan"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014388887"
FT   DOMAIN          55..153
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          160..255
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          259..357
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          1007..1043
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1045..1081
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1094..1208
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1212..1272
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   REGION          362..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          986..1008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1274..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        937..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1305
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1306..1320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        206..227
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        304..325
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        1033..1042
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1071..1080
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1214..1257
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        1243..1270
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   1320 AA;  142868 MW;  E07AB2F194343107 CRC64;
     MGATFVWALG LLMLQMLLFV AGEQSTQDIA DASERGLHMQ KLGSGSVRAA LAELVALPCL
     FTLQPRPSAA RDAPRIKWTK VRTASGQRQD LPILVAKDNV VRVAKSWQGR VSLPAYPRRR
     ANATLLLGPL RASDSGLYRC QVVRGIEDEQ DLVPLEVTGV VFHYRAAQDR YALTFAEAQE
     ACHLSSAIIA APRHLQAAFE DGFDNCDAGW LSDRTVRYPI TQSRPGCYGD RSSLPGVRSY
     GRRNPQELYD VYCFARELGG EVFYVGPARR LTLAGARAQC RRQGAALASV GQLHLAWHEG
     LDQCDPGWLA DGSVRYPIQT PRRRCGGPAP GVRTVYRFAN RTGFPSPAAR FDAYCFRAHH
     PTSQHGDLET PSSGDEGEIL SAEGPPVREL EPTLEEEEVV TPDFQEPLVS SGEEEPLILA
     EKQESQQTLR PTPGDPMLAS WPTGEVWLST VAPSPSDTGA GTTASSHTEV APTDPTARRR
     GRFKGLNGRY FQQQEPEPGL QEGMEASAQA PTSEAVGNQV EPPLAIAVTE MLGSGHSRSP
     WADLTNEVDM PGAGSAGGKS SPEPWLWPPT MVPPSISGHI RAPVPELEKA EGPSARPATP
     DLFWSPLEAT VSAPSPAPWE ASPLATSPDL PMMAMLRGPK QWMLPHPTSV STEASRVEGH
     SEAMAMAPPS PAAETKVYSL PPFSTLTGQG GEAMPTTPES PRADFREIGE TSLAQVNKAE
     HPSSSPWPSV NRNVAVGFVP TETATELTGL RGISGSESGV FDTAESPTSD LQATVDEVQD
     PWPSVYSKGL DASSPSAPSG SPGVFLLPKV TPSLEPQVAK DEGPTVNPMD STVTPAPSDA
     SGIWEPGSQL FEEAESTTLS PQVALDTSIV TSLTTEQGDK VGVPAVSTLA SSSSQPHPEP
     EDQVETQGTS GTSAPPHQSS PLGKPAVPPG TPTAASVGES ALVSSGEPTV PWDPSSTLLP
     VTLGIEDFKL EVLAGGPGVE SFWEEVASGE EPALSGTPTN EGAEEAHSDP CENNPCLHGG
     TCNANGTMYG CSCDQGFTGE NCEIDIDDCL CGPCENGGTC IDEVNGFVCL CLPSYGGSLC
     EKDTEGCDRG WHKFQGHCYR YFAHRRAWED AERDCRRRSG HLTSVHSPEE HSFINSFGHE
     NTWIGLNDRI VERDFQWTDN TGLQFENWRE NQPDNFFAGG EDCVVMVAHE SGRWNDVPCN
     YNLPYVCKKG TVLCGPPPAV ENASLIGTRK AKYNVHATVR YQCNEGFAQH HVATIRCRSN
     GKWDRPQIVC TKPRRSHRMR RHHHHHQHHH QHHHHKSRKE RRKHKKHPTE DWEKDEGNFC
//
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