GenomeNet

Database: UniProt
Entry: A0A0A0MXI6_PAPAN
LinkDB: A0A0A0MXI6_PAPAN
Original site: A0A0A0MXI6_PAPAN 
ID   A0A0A0MXI6_PAPAN        Unreviewed;      1320 AA.
AC   A0A0A0MXI6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Neurocan {ECO:0000313|Ensembl:ENSPANP00000017817.1};
GN   Name=NCAN {ECO:0000313|Ensembl:ENSPANP00000017817.1};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000017817.1, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000017817.1, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000017817.1}
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_009192211.1; XM_009193947.1.
DR   STRING; 9555.ENSPANP00000017817; -.
DR   Ensembl; ENSPANT00000010877.3; ENSPANP00000017817.1; ENSPANG00000017942.4.
DR   GeneID; 101005836; -.
DR   CTD; 1463; -.
DR   eggNOG; ENOG502QQ78; Eukaryota.
DR   GeneTree; ENSGT00940000158649; -.
DR   HOGENOM; CLU_000303_0_1_1; -.
DR   OMA; HESGHWN; -.
DR   OrthoDB; 5402504at2759; -.
DR   Proteomes; UP000028761; Chromosome 20.
DR   Bgee; ENSPANG00000017942; Expressed in habenula and 30 other cell types or tissues.
DR   ExpressionAtlas; A0A0A0MXI6; baseline.
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:UP000028761};
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                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001967292"
FT   DOMAIN          14..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          456..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..862
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          988..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        456..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..917
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;  142723 MW;  05024FCCD806004E CRC64;
     MGATFVWALG LLMPQMLLFV AGEQGTQDIA DASERGLHMQ KLGSGSVRAA LAELVALPCL
     FTLQPRPSAA RDAPRIKWTK VRTASGQRQD LPILVAKDNV VRVAKSWQGR VSLPAYPRRR
     VNATLLLGPL 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
     EKQESQQTLS PTPGDPMLAS WPTGEVWLST VAPSPSDMGA GTTASSHTEV APTDPTARRR
     GRFKGLNGRY FQQQEPEPGL QEGMEASAQP PTSEAVGNQV EPPLAMAVTE MLGSGHSRSP
     WADLTNEVDM PGAGSAGGKS SPEPWLWPPT MVPPSISGHS RAPVPELEKA EGPSARPATP
     DLFWSPLEAT VSAPSPAPWE ASPLATSPDL PMMAMLRGPK QWMLPHPTSV STEASRVEGH
     GEATATAPPS PAAETKVYSL PPFSTPTGQG GEAMPTTPES PRPDFREIGE TSLAQVHKVE
     HPSSSPWPSV NRNVAVGFVP TETATELTGL RGISGSESGV FDTAESPTSG LQATVDEVQD
     PWPSVYSKGP GASSPSAPSG SPGLFLVPKV TPSLEPWVAT DEGPTVNPKD STVTPAPSDA
     SGIWEPGSQS FEEAESTTLS PQVALDTSVV TSLTTEQGDK VGVPAVSTLA SSSSQPHPEP
     EDQVETQGTS GTLAPPHQSS PLGKPAVPPG TPTAASVGES ALVSSGEPTV PWDPSSTLLP
     VTLGIEDFKL EVLAGSPGVE SFWEEVASGE EPALSGTPTN EGAEEAHSDP CENNPCLHGG
     TCNANGTMYG CSCDQGFAGE NCEIDIDDCL CSPCENGGTC IDEVNGFVCL CLPSYGGSLC
     EKDTEGCDRS WHKFQGHCYR YFAHRRAWED AERDCRRRSG HLTSVHSPEE HSFINSFGHE
     NTWIGLNDRI VERDFQWTDN TGLQFENWRE NQPDNFFAGG EDCVVMVAHE SGRWNDVPCN
     YNLPYVCKKG TVLCGPPPAV ENASLIGTRK AKYNVHATVR YQCNEGFAQH HVATIRCRSN
     GKWDRPQIVC TKPRRSHRMR RHHHHHQHHH QHHHHKSHKE RRKHKKHPTE DWEKDEGNFC
//
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