ID H0XGP3_OTOGA Unreviewed; 2108 AA.
AC H0XGP3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Aggrecan core protein {ECO:0000256|ARBA:ARBA00039399};
DE AltName: Full=Cartilage-specific proteoglycan core protein {ECO:0000256|ARBA:ARBA00042947};
GN Name=ACAN {ECO:0000313|Ensembl:ENSOGAP00000015258.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000015258.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000015258.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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 EMBL; AAQR03058476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 30611.ENSOGAP00000015258; -.
DR Ensembl; ENSOGAT00000017043.2; ENSOGAP00000015258.2; ENSOGAG00000017035.2.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR GeneTree; ENSGT00940000155971; -.
DR HOGENOM; CLU_000303_2_0_1; -.
DR InParanoid; H0XGP3; -.
DR OMA; EDWIVTQ; -.
DR TreeFam; TF332134; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; IEA:Ensembl.
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:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0002063; P:chondrocyte development; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IEA:Ensembl.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd05900; Ig_Aggrecan; 1.
DR CDD; cd03517; Link_domain_CSPGs_modules_1_3; 2.
DR CDD; cd03520; Link_domain_CSPGs_modules_2_4; 2.
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; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 5.
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; IPR033987; CSPG_CTLD.
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; IPR003006; Ig/MHC_CS.
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:SF42; AGGRECAN CORE PROTEIN; 1.
DR PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 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; 4.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 4.
DR SUPFAM; SSF56436; C-type lectin-like; 5.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 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; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
DR PROSITE; PS01241; LINK_1; 3.
DR PROSITE; PS50963; LINK_2; 4.
DR PROSITE; PS50923; SUSHI; 1.
PE 3: Inferred from homology;
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}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2108
FT /note="Aggrecan core protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003545989"
FT DOMAIN 34..147
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 153..248
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 253..350
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 487..582
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 588..684
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 1856..1892
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1905..2019
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2023..2083
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 748..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2085..2108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 199..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 297..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 533..554
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 631..652
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 1882..1891
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2025..2068
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2054..2081
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 2108 AA; 219933 MW; 0BC6F2B51BAA6169 CRC64;
MTTLLFVFVT LRVITAAISI EVSDHDNSLS VSIPQPSPLK VPLGTSLTIP CYFIDPMHPV
TTAPSTAPLA PRIKWSRISK EKEVVLLVAT EGRVRVNNAY QDKVSLPNYP AIPSDATLEI
QNLRSNDSGI YRCEVMHGIE DSEATLEVVV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHIPREGC YGDKDEFPGV RTYGVRDTNE
TYDVYCFAEE MEGEVFYSTS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QSGMDVCSAG
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN
FFGVGGEEDI TIQTVTWPDV ELPLPQNITE GEARGNVILT VKPIFDVSPT VLEPEEPFTF
APDIGATLFP ETETRTREAT RPWSFPEEST SGLDSVIAYT SQDLVVQVTA VPGAVEVPGQ
PRLPGAVVFH YRPGPSRYSL TFEEAQEACL RTGAVIASPG QLQAAYEAGY EQCDAGWLQD
QSVRYPIVSP RTPCVGDKDS SPGVRTYGVR PSSETYDVYC YVDKLEGEVF FATRPEQFTF
QEALEFCVSH NATLASTGQL YAAWSRGLDK CYAGWLADGS LRYPIVTPRP ACGGDKPGVR
TVYLYPNQTG LPDPLSRHHA FCFRGVSAVP SPGEEEGGTV TSPTDVEDRI ATQLVPGVDA
IPSGEEMTAI PDFTTEPEKQ TEWEPAYTPV GTSLLPGVPP TWHPTGVATE ESTEGPFATE
LPSASEEPSP SQKPSPSEEP YTPSLPVPSG TDLPGSGEVS GAPDISGNFT GSGEVSGHFD
FSGQPSGVTA SGLPSGDLDS SGLTSTVGSG LPVESGLASG DEERIEWSST PKVSGLPSGE
SLETSASGVG DLSGLSSGGE GLETSASGVE DLSRLPSGEV LETSASGVGD LSGVPSGEVL
ETSASGVGDL SGLPSGEIPE TSASGVGDLS RFPSGEIPET SASGVGDLSG LPSGEVLETS
ASGVGDLDGL PSGEVLETSA SGVEGLDGLP SGEVLETSAS GVGDLSGLPS GVLEISASGV
GDLSGLPSGE VLETSASGVD VSRLPSGGES LETSTSGVGD DLSGLPSGRK DLETSVSGAE
DLSGLFSGKE DLEGSVSGAL DLGELPSGTL GSGHTPETSG LPSEFSGKYS GVDVGSGPSS
GLPDFSGLPS GFPTVSLVDT TLVEVVTAST AAELEGRGTI DISGAGEISG LPFSEWDISG
GPSGLPSGAE LSGQTSGTPD ISGETSGLSG VSGQPSGFPD ISGGTSGIFE VSELPSGFPD
TSGETSGVPE LSGLPSGQPG VSGEASGVVY GSGQPFGITD LSGETSGIPD LSGQPSGLPG
LFSGATSGIP DLVSSTTSGS GESSGITFVD TSLVEVTPTT FKEEEGLGSV EHSGFPSGEP
DLSSTSGIVE VSGQSSGTID FSGFTSQAPE FSGLPSGRGE VSGESSGAEI RSSMPSGAYD
SSGLSSGFPT ISLVDRTFVE SVTQAPTAQE AGEGPSGILE LSGAHSGAPD MSGDHSGLLD
LSGLQSGLLE PSGEPPSTPY FSGDFASTTD VSGESSVTGT SGEVSGLPEV TLITSEFVES
VTEPTLSQEL GQRPPVTYTP QLFESSGEAS ASGDISGVGP MLPGSGVEAS SVPESSSETS
AYPEPGVGVS AAPAASAEAS ESPDLSGTTS AFHEADLERA SGGEESGSTL TFQEAPHEGS
AATEVSGEST TSYDAGTEVS GFSSVAPTSS GDRTEISGDL SGHTSGLDVV ISTSVPEFEW
PQQSQRPAEA HLEIESSSPL YSGEDTQTVE TATFPTDASI PTSLEGTGES EPTVADIDEC
LSSPCLNGAT CVDAIDSFTC LCLPSYGGDL CEIDQEVCEE GWTKFQGYCY RHFPDRETWV
DAESQCRKHQ SHLSSIVTPE EQEFVNNNAQ DYQWIGLNDR TIEGDFRWSD GHSLQFENWR
PNQPDNFFAT GEDCVVMIWH EKGEWNDVPC NYHLPFTCKK GTVACGEPPM VEHARTFGQK
KDRYEINSLV RYQCTEGFVQ RHVPTIRCQP SGHWEEPRIT CTDPTTYKRR LQKRNSRAPR
RSRSGTAH
//
