PGCA_PIG
ID PGCA_PIG Reviewed; 537 AA.
AC Q29011; O18833; Q7M2W7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Aggrecan core protein;
DE AltName: Full=Cartilage-specific proteoglycan core protein;
DE Short=CSPCP;
DE Contains:
DE RecName: Full=Aggrecan core protein 2;
DE Flags: Fragments;
GN Name=ACAN; Synonyms=AGC1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE OF 1-370, AND GLYCOSYLATION AT ASN-110; ASN-223; ASN-317;
RP THR-355 AND THR-360.
RC TISSUE=Cartilage;
RX PubMed=1417734; DOI=10.1042/bj2860761;
RA Barry F.P., Gaw J.U., Young C.N., Neame P.J.;
RT "Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Amino
RT acid sequence, analysis of N-linked oligosaccharides and location of the
RT keratan sulphate.";
RL Biochem. J. 286:761-769(1992).
RN [2]
RP ERRATUM OF PUBMED:1417734, AND SEQUENCE REVISION.
RA Barry F.P., Gaw J.U., Young C.N., Neame P.J.;
RL Biochem. J. 291:951-951(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 324-453.
RC TISSUE=Chondrocyte;
RX PubMed=9550267; DOI=10.1016/s0945-053x(98)90021-x;
RA Flannery C.R., Little C.B., Caterson B.;
RT "Molecular cloning and sequence analysis of the aggrecan interglobular
RT domain from porcine, equine, bovine and ovine cartilage: comparison of
RT proteinase-susceptible regions and sites of keratan sulfate substitution.";
RL Matrix Biol. 16:507-511(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 454-537.
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 [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1326552; DOI=10.1016/s0021-9258(18)41799-1;
RA Fosang A.J., Neame P.J., Last K., Hardingham T.E., Murphy G.,
RA Hamilton J.A.;
RT "The interglobular domain of cartilage aggrecan is cleaved by PUMP,
RT gelatinases, and cathepsin B.";
RL J. Biol. Chem. 267:19470-19474(1992).
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; AF019757; AAC48799.1; -; mRNA.
DR EMBL; S74664; AAC60528.2; -; mRNA.
DR PIR; S29139; S29139.
DR PIR; S78009; S78009.
DR STRING; 9823.ENSSSCP00000002003; -.
DR iPTMnet; Q29011; -.
DR PaxDb; Q29011; -.
DR PeptideAtlas; Q29011; -.
DR PRIDE; Q29011; -.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR InParanoid; Q29011; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 2.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
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 Pfam; PF07686; V-set; 1.
DR Pfam; PF00193; Xlink; 2.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
DR PROSITE; PS01241; LINK_1; 2.
DR PROSITE; PS50963; LINK_2; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Immunoglobulin domain; Proteoglycan; Reference proteome;
KW Repeat; Secreted.
FT CHAIN 1..>537
FT /note="Aggrecan core protein"
FT /id="PRO_0000046691"
FT CHAIN 4..>537
FT /note="Aggrecan core protein 2"
FT /id="PRO_0000262868"
FT DOMAIN 28..124
FT /note="Ig-like V-type"
FT DOMAIN 137..232
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 238..334
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REGION 32..124
FT /note="G1-A"
FT REGION 136..231
FT /note="G1-B"
FT REGION 237..333
FT /note="G1-B'"
FT REGION 392..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION <454..520
FT /note="KS"
FT REGION 523..>537
FT /note="CS-1"
FT COMPBIAS 446..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1417734"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1417734"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1417734"
FT CARBOHYD 355
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000269|PubMed:1417734"
FT CARBOHYD 360
FT /note="O-linked (Xyl...) (keratan sulfate) threonine"
FT /evidence="ECO:0000269|PubMed:1417734"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..117
FT /evidence="ECO:0000250"
FT DISULFID 159..230
FT /evidence="ECO:0000250"
FT DISULFID 183..204
FT /evidence="ECO:0000250"
FT DISULFID 257..332
FT /evidence="ECO:0000250"
FT DISULFID 281..302
FT /evidence="ECO:0000250"
FT NON_CONS 453..454
FT /evidence="ECO:0000305"
FT NON_TER 537
SQ SEQUENCE 537 AA; 58583 MW; F86A1CC9B6558BCD CRC64;
AISVEVSEPD NSLSVSIPQP SPLRVLLGGS LTIPCYFIDP MHPVXTAPXT APLAPRIKWS
RVSKEKEVVL LVATEGQVRV NSAYQDRVTL PNYPAIPSDA TLEIQNLRSN DSGIYRCEVM
HGIEDSEATL EVVVKGIVFH YRAISXRYTL DFDRAQRACL QNSAIIATPE QLQAAYEDGF
HQCDAGWLAD QTVRYPIHTP REGCYGDKDE FPGVITYGIR DTNETYDVYC FAEEMEGEVF
YATSPEKFTF QEAANECRRL GARLATTGQL YLAWRGGMDM CSAGWLADRS VRYPISKARP
NCGGNLLGVR TVYLHANQTG YPDPSSRYDA ICYTGEDFVD IPENFFGVGG EEDITIQTVT
WPDVELPLPR NITEGEARGT VILTVKPVFE FSPTAPEPEE PFTFAPGTGA TAFPEAENRT
GEATRPWAFP EESTPGLGAP TAFTSEDLVV QVTSAATEEG TEGPSATEAP STSEEPFPSE
KPFPSEEPFP SEEPFPSEKP SASEEPFPSE QPSTLSAPVP SRTELPGSGE VSGAPEV
