PGCA_CANLF
ID PGCA_CANLF Reviewed; 2333 AA.
AC Q28343; Q28310;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Aggrecan core protein;
DE AltName: Full=Cartilage-specific proteoglycan core protein;
DE Short=CSPCP;
DE Flags: Precursor;
GN Name=ACAN; Synonyms=AGC1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Glant T.T., Adams M.E., Kwok S.X.F., Huang D., Fueloep C.;
RT "Complete coding sequence and deduced amino acid sequence of aggrecan of
RT canine cartilage.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 774-833.
RC TISSUE=Cartilage;
RX PubMed=7827755; DOI=10.1016/0945-053x(94)90198-8;
RA Barry F.P., Neame P.J., Sasse J., Pearson D.;
RT "Length variation in the keratan sulfate domain of mammalian aggrecan.";
RL Matrix Biol. 14:323-328(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1830-2333.
RA Adams M.E., Kowk S.X.F., Huang D., Glant T.T., Fullop C.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2082-2118.
RC TISSUE=Cartilage;
RX PubMed=8349621; DOI=10.1016/s0021-9258(19)85345-0;
RA Fueloep C., Walcz E., Valyon M., Glant T.T.;
RT "Expression of alternatively spliced epidermal growth factor-like domains
RT in aggrecans of different species. Evidence for a novel module.";
RL J. Biol. Chem. 268:17377-17383(1993).
CC -!- FUNCTION: This proteoglycan is a major component of extracellular
CC matrix of cartilagenous tissues. A major function of this protein is to
CC resist compression in cartilage. It binds avidly to hyaluronic acid via
CC an N-terminal globular region. May play a regulatory role in the matrix
CC assembly of the cartilage.
CC -!- SUBUNIT: Interacts with FBLN1 and COMP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- DOMAIN: Two globular domains, G1 and G2, comprise the N-terminus of the
CC proteoglycan, while another globular region, G3, makes up the C-
CC terminus. G1 contains Link domains and thus consists of three
CC disulfide-bonded loop structures designated as the A, B, B' motifs. G2
CC is similar to G1. The keratan sulfate (KS) and the chondroitin sulfate
CC (CS) attachment domains lie between G2 and G3.
CC -!- PTM: Contains mostly chondroitin sulfate, but also keratan sulfate
CC chains, N-linked and O-linked oligosaccharides. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
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DR EMBL; U65989; AAB06238.2; -; mRNA.
DR EMBL; S74662; AAC60527.1; -; mRNA.
DR EMBL; L07054; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; I46998; I46998.
DR AlphaFoldDB; Q28343; -.
DR SMR; Q28343; -.
DR STRING; 9612.ENSCAFP00000016949; -.
DR PaxDb; Q28343; -.
DR PRIDE; Q28343; -.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR InParanoid; Q28343; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR CDD; cd00033; CCP; 1.
DR CDD; cd03588; CLECT_CSPGs; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 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 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; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 5.
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; 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; 4.
DR PROSITE; PS50963; LINK_2; 4.
DR PROSITE; PS50923; SUSHI; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Immunoglobulin domain; Lectin; Metal-binding; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..2333
FT /note="Aggrecan core protein"
FT /id="PRO_0000017503"
FT DOMAIN 34..147
FT /note="Ig-like V-type"
FT DOMAIN 153..248
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 253..350
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 496..591
FT /note="Link 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 597..693
FT /note="Link 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 2081..2117
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2130..2245
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 2248..2308
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 48..140
FT /note="G1-A"
FT REGION 152..247
FT /note="G1-B"
FT REGION 253..349
FT /note="G1-B'"
FT REGION 495..589
FT /note="G2-B"
FT REGION 596..691
FT /note="G2-B'"
FT REGION 694..816
FT /note="KS"
FT REGION 751..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..1394
FT /note="CS-1"
FT REGION 1395..2079
FT /note="CS-2"
FT REGION 1490..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1749..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..2006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2042..2079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2080..2333
FT /note="G3"
FT COMPBIAS 772..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1781..1800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2044..2074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 2208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 2218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 2231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 2232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 376
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..133
FT /evidence="ECO:0000250"
FT DISULFID 175..246
FT /evidence="ECO:0000250"
FT DISULFID 199..220
FT /evidence="ECO:0000250"
FT DISULFID 273..348
FT /evidence="ECO:0000250"
FT DISULFID 297..318
FT /evidence="ECO:0000250"
FT DISULFID 518..589
FT /evidence="ECO:0000250"
FT DISULFID 542..563
FT /evidence="ECO:0000250"
FT DISULFID 616..691
FT /evidence="ECO:0000250"
FT DISULFID 640..661
FT /evidence="ECO:0000250"
FT DISULFID 2085..2096
FT /evidence="ECO:0000250"
FT DISULFID 2090..2105
FT /evidence="ECO:0000250"
FT DISULFID 2107..2116
FT /evidence="ECO:0000250"
FT DISULFID 2123..2134
FT /evidence="ECO:0000250"
FT DISULFID 2151..2243
FT /evidence="ECO:0000250"
FT DISULFID 2219..2235
FT /evidence="ECO:0000250"
FT DISULFID 2250..2293
FT /evidence="ECO:0000250"
FT DISULFID 2279..2306
FT /evidence="ECO:0000250"
SQ SEQUENCE 2333 AA; 240576 MW; 8B9ED78F3508B596 CRC64;
MTTLLWVFVT LRVITAASSE ETSDHDNSLS VSIPEPSPMR VLLGSSLTIP CYFIDPMHPV
TTAPSTAPLA PRIKWSRITK EKEVVLLVAT EGQVRINSAY QDKVSLPNYP AIPSDATLEI
QNLRSNDSGI YRCEVMHGIE DSEATLEVVV KGIVFHYRAI STRYTLDFDR AQRACLQNSA
IIATPEQLQA AYEDGFHQCD AGWLADQTVR YPIHTPREGC YGDKDEFPGV RTYGIRDTNE
TYDVYCFAEE MEGEVLYATS PEKFTFQEAA NECRRLGARL ATTGQLYLAW QGGMDMCSAG
WLADRSVRYP ISKARPNCGG NLLGVRTVYL HANQTGYPDP SSRYDAICYT GEDFVDIPEN
FFGVGGEEDI TIQTVTWPDV ELPLPRNITE GEARGNVILT VKPIFDLSPT APEPEEPFTF
VPEPEKPFTF ATDVGVTAFP EAENRTGEAT RPWGVPEEST PGPAFTAFTS EDHVVQVTAV
PGAAEVPGQP RLPGGVVFHY RPGSARYSLT FEEAQQACLR TGAVIASPEQ LQAAYEAGYE
QCDAGWLQDQ TVRYPIVSPR TPCVGDKDSS PGVRTYGVRP PSETYDVYCY VDKLEGEVFF
ITRLEQFTFQ EALAFCESHN ATLASTGQLY AAWRQGLDKC YAGWLSDGSL RYPIVTPRPS
CGGDKPGVRT VYLYPNQTGL PDPLSRHHVF CFRGVSGVPS PGEEEGGTPT PSVVEDWIPT
QVGPVVPSVP MGEETTAILD FTIEPENQTE WEPAYSPAGT SPLPGIPPTW PPTSTATEES
TEGPSGTEVP SVSEEPSPSE EPFPWEELST LSPPGPSGTE LPGSGEASGV PEVSGDFTGS
GEVSGHPDSS GQLSGESASG LPSEDLDSSG LTSAVGSGLA SGDEDRITLS SIPKVEGEGL
ETSASGVEDL SGLPSGREGL ETSTSGVGDL SGLPSGEGLE VSASGVEDLS GLPSGEGPET
STSGVGDLSR LPSGEGPEVS ASGVGDLSGL PSGREGLETS TSGVEDLSGL PSGEGPEAST
SGVGDLSRLP SGEGPEVSAS GVEDLSGLPS GEGLEASASG VGDLSGLPSG EGPEASASGV
GDLSRLPSGE GPEVSASGVE DLSGLSSGES PEASASGVGD LSGLPSGREG LETSASGVGD
LSGLPSGEGQ EASASGVEDL SRLPSGEGPE ASASGVGELS GLPSGREGLE TSASGVGDLS
GLPSGEGPEA FASGVEDLSI LPSGEGPEAS ASGVGDLSGL PSGREGLETS TSGVGDLSGL
PSGREGLETS TSGVGDLSGL PSGEGPEASA SGIGDISGLP SGREGLETSS SGVEDHPETS
ASGVEDLSGL PSGVEGHPET SASGVEDLSD LSSGGEGLET SASGAEDLSG FPSGKEDLIG
SASGALDFGR IPSGTLGSGQ APEASSLPSG FSGEYSGVDF GSGPISGLPD FSGLPSGFPT
ISLVDTTLVE VITTTSASEL EGRGTIGISG AGETSGLPVS ELDISGAVSG LPSGAELSGQ
ASGSPDMSGE TSGFFGVSGQ PSGFPDISGG TSGLFEVSGQ PSGFSGETSG VTELSGLYSG
QPDVSGEASG VPSGSGQPFG MTDLSGETSG VPDISGQPSG LPEFSGTTSG IPDLVSSTMS
GSGESSGITF VDTSLVEVTP TTFKEKKRLG SVELSGLPSG EVDLSGASGT MDISGQSSGA
TDSSGLTSHL PKFSGLPSGA AEVSGESSGA EVGSSLPSGT YEGSGNFHPA FPTVFLVDRT
LVESVTQAPT AQEAGEGPSG ILELSGAHSG APDVSGDHSG SLDLSGMQSG LVEPSGEPSS
TPYFSGDFSG TMDVTGEPST AMSASGEASG LLEVTLITSE FVEGVTEPTV SQELAQRPPV
THTPQLFESS GEASASGEIS GATPAFPGSG LEASSVPESS SETSDFPERA VGVSAAPEAS
GGASGAPDVS EATSTFPEAD VEGASGLGVS GGTSAFPEAP REGSATPEVQ EEPTTSYDVG
REALGWPSAT PTASGDRIEV SGDLSGHTSG LDVVISTSVP ESEWIQQTQR PAEAHLEIEA
SSPLHSGEET QTAETATSPT DDASIPTSPS GTDESAPAIP DIDECLSSPC LNGATCVDAI
DSFTCLCLPS YRGDLCEIDQ ELCEEGWTKF QGHCYRYFPD RESWVDAESR CRAQQSHLSS
IVTPEEQEFV NNNAQDYQWI GLNDRTIEGD FRWSDGHSLQ FENWRPNQPD NFFVSGEDCV
VMIWHEKGEW NDVPCNYYLP FTCKKGTVAC GDPPVVEHAR TFGQKKDRYE INSLVRYQCT
EGFVQRHVPT IRCQPSGHWE KPRITCTDPS TYKRRLQKRS SRAPRRSRPS TAH
