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Aggrecan core protein (Cartilage-specific proteoglycan core protein) (CSPCP) (Fragment)

 PGCA_RABIT              Reviewed;         394 AA.
Q28670;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 96.
RecName: Full=Aggrecan core protein;
AltName: Full=Cartilage-specific proteoglycan core protein;
Short=CSPCP;
Flags: Fragment;
Name=ACAN; Synonyms=AGC1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cartilage;
PubMed=7575690; DOI=10.1002/art.1780381007;
Bayne E.K., Macnaul K.L., Donatelli S.A., Christen A., Griffin P.R.,
Hoerrner L.A., Calaycay J.R., Ayala J.M., Chapman K., Hagmann W.,
Weidner J.R., McDonnel J., Moore V.L., Mumford R.A., Lark M.W.,
Hutchinson N.I.;
"Use of an antibody against the matrix metalloproteinase-generated
aggrecan neoepitope FVDIPEN-COOH to assess the effects of stromelysin
in a rabbit model of cartilage degradation.";
Arthritis Rheum. 38:1400-1409(1995).
-!- FUNCTION: This proteoglycan is a major component of extracellular
matrix of cartilagenous tissues. A major function of this protein
is to resist compression in cartilage. It binds avidly to
hyaluronic acid via an N-terminal globular region. May play a
regulatory role in the matrix assembly of the cartilage.
-!- SUBUNIT: Interacts with FBLN1 and COMP. {ECO:0000250}.
-!- DOMAIN: Two globular domains, G1 and G2, comprise the N-terminus
of the proteoglycan, while another globular region, G3, makes up
the C-terminus. G1 contains Link domains and thus consists of
three disulfide-bonded loop structures designated as the A, B, B'
motifs. G2 is similar to G1. The keratan sulfate (KS) and the
chondroitin sulfate (CS) attachment domains lie between G2 and G3.
-!- PTM: Contains mostly chondroitin sulfate, but also keratan sulfate
chains, N-linked and O-linked oligosaccharides. {ECO:0000250}.
-!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
{ECO:0000305}.
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EMBL; L38480; AAA91890.1; -; mRNA.
UniGene; Ocu.2050; -.
ProteinModelPortal; Q28670; -.
STRING; 9986.ENSOCUP00000024918; -.
eggNOG; ENOG410IJP2; Eukaryota.
eggNOG; ENOG410XRES; LUCA.
HOGENOM; HOG000168421; -.
HOVERGEN; HBG008175; -.
InParanoid; Q28670; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.100.10; -; 2.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR000538; Link_dom.
Pfam; PF07686; V-set; 1.
Pfam; PF00193; Xlink; 2.
PRINTS; PR01265; LINKMODULE.
SMART; SM00445; LINK; 2.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF56436; SSF56436; 2.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
PROSITE; PS01241; LINK_1; 2.
PROSITE; PS50963; LINK_2; 2.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Proteoglycan; Reference proteome; Repeat.
CHAIN <1 >394 Aggrecan core protein.
/FTId=PRO_0000046692.
DOMAIN <1 83 Ig-like V-type.
DOMAIN 89 184 Link 1. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 190 286 Link 2. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REGION <1 76 G1-A. {ECO:0000250}.
REGION 88 183 G1-B. {ECO:0000250}.
REGION 189 285 G1-B'. {ECO:0000250}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 111 182 {ECO:0000250}.
DISULFID 135 156 {ECO:0000250}.
DISULFID 209 284 {ECO:0000250}.
DISULFID 233 254 {ECO:0000250}.
NON_TER 1 1
NON_TER 394 394
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


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