PGCA_RABIT
ID PGCA_RABIT Reviewed; 394 AA.
AC Q28670;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Aggrecan core protein;
DE AltName: Full=Cartilage-specific proteoglycan core protein;
DE Short=CSPCP;
DE Flags: Fragment;
GN Name=ACAN; Synonyms=AGC1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cartilage;
RX PubMed=7575690; DOI=10.1002/art.1780381007;
RA Bayne E.K., Macnaul K.L., Donatelli S.A., Christen A., Griffin P.R.,
RA Hoerrner L.A., Calaycay J.R., Ayala J.M., Chapman K., Hagmann W.,
RA Weidner J.R., McDonnel J., Moore V.L., Mumford R.A., Lark M.W.,
RA Hutchinson N.I.;
RT "Use of an antibody against the matrix metalloproteinase-generated aggrecan
RT neoepitope FVDIPEN-COOH to assess the effects of stromelysin in a rabbit
RT model of cartilage degradation.";
RL Arthritis Rheum. 38:1400-1409(1995).
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 -!- 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; L38480; AAA91890.1; -; mRNA.
DR STRING; 9986.ENSOCUP00000024918; -.
DR eggNOG; ENOG502QUX8; Eukaryota.
DR InParanoid; Q28670; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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; 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; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Proteoglycan;
KW Reference proteome; Repeat.
FT CHAIN <1..>394
FT /note="Aggrecan core protein"
FT /id="PRO_0000046692"
FT DOMAIN <1..83
FT /note="Ig-like V-type"
FT DOMAIN 89..184
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 190..286
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REGION <1..76
FT /note="G1-A"
FT /evidence="ECO:0000250"
FT REGION 88..183
FT /note="G1-B"
FT /evidence="ECO:0000250"
FT REGION 189..285
FT /note="G1-B'"
FT /evidence="ECO:0000250"
FT REGION 343..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..182
FT /evidence="ECO:0000250"
FT DISULFID 135..156
FT /evidence="ECO:0000250"
FT DISULFID 209..284
FT /evidence="ECO:0000250"
FT DISULFID 233..254
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 394
SQ SEQUENCE 394 AA; 43306 MW; 51F9A9B655BE82AD CRC64;
STAPLTPRIK WSRISKDKEV VLLVANEGRV RINSAYQDKV SLPNYPAIPS DATLEIQSLR
SNDSGIYRCE VMHGLEDSEA TLEVVVKGVV FHYRAISTRY TLDFDRAQRA CLQNSAIIAT
PEQLQAAYED GFHQCDAGWL ADQTVRYPIH TPREGCYGDK DEFPGVRTYG IRDTNETYDV
YCFAEEMEGE VFYATSPEKF TFQEAASECR RLGARLATTG QLYLAWQAGM DMCSAGWLAD
RSVRYPISKA RPNCGGNLLG VRTVYVHANQ TGYPDPSSRY DAICYTGEXF MDIPENFFGV
GGEEDITVQT VTWPDVELPV PRNITEGEAR GSVVLTAKPV LDVSPTAPQP EETFAPGLGA
TAFPGVENGT EEATRPRGFA DEAALGPSSA TAFT
