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Epiphycan (Dermatan sulfate proteoglycan 3) (Proteoglycan-Lb) (PG-Lb) (Small chondroitin/dermatan sulfate proteoglycan)

 EPYC_BOVIN              Reviewed;         321 AA.
P79119;
08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
28-MAR-2018, entry version 119.
RecName: Full=Epiphycan;
AltName: Full=Dermatan sulfate proteoglycan 3;
AltName: Full=Proteoglycan-Lb;
Short=PG-Lb;
AltName: Full=Small chondroitin/dermatan sulfate proteoglycan;
Flags: Precursor;
Name=EPYC; Synonyms=DSPG3, PGLB;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT
THR-60; SER-64; SER-95 AND ASN-282, TISSUE SPECIFICITY, AND DISULFIDE
BOND.
TISSUE=Fetal epiphyseal cartilage;
PubMed=9228042; DOI=10.1074/jbc.272.30.18709;
Johnson H.J., Rosenberg L., Choi H.U., Garza S., Hoeoek M.,
Neame P.J.;
"Characterization of epiphycan, a small proteoglycan with a leucine-
rich repeat core protein.";
J. Biol. Chem. 272:18709-18717(1997).
-!- FUNCTION: May have a role in bone formation and also in
establishing the ordered structure of cartilage through matrix
organization.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- TISSUE SPECIFICITY: Preferentially expressed in the zone of
flattened chondrocytes of the developing limb cartilage.
{ECO:0000269|PubMed:9228042}.
-!- DEVELOPMENTAL STAGE: Embryo.
-!- PTM: A long and a short form present in approximately equimolar
amounts may arise by proteolysis or cleavage by exopeptidases.
-!- PTM: The O-linked polysaccharides on Thr-60 and Ser-95 are
probably the mucin type linked to GalNAc. There is one
glycosaminoglycan chain, known to be dermatan sulfate, and it is
probably the O-glycosylation at Ser-64.
{ECO:0000269|PubMed:9228042}.
-!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
family. SLRP class III subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U77127; AAB68397.1; -; mRNA.
RefSeq; NP_776732.1; NM_174307.2.
RefSeq; XP_010803061.1; XM_010804759.2.
UniGene; Bt.65453; -.
ProteinModelPortal; P79119; -.
IntAct; P79119; 1.
STRING; 9913.ENSBTAP00000010504; -.
iPTMnet; P79119; -.
PaxDb; P79119; -.
PRIDE; P79119; -.
Ensembl; ENSBTAT00000010504; ENSBTAP00000010504; ENSBTAG00000007990.
GeneID; 281747; -.
KEGG; bta:281747; -.
CTD; 1833; -.
VGNC; VGNC:28558; EPYC.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00730000110781; -.
HOGENOM; HOG000273909; -.
HOVERGEN; HBG006850; -.
InParanoid; P79119; -.
KO; K08127; -.
OMA; CDDHELD; -.
OrthoDB; EOG091G0C68; -.
TreeFam; TF351924; -.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000007990; -.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR027217; Epiphycan.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
PANTHER; PTHR24373:SF123; PTHR24373:SF123; 1.
Pfam; PF13855; LRR_8; 1.
SMART; SM00369; LRR_TYP; 4.
SMART; SM00013; LRRNT; 1.
PROSITE; PS51450; LRR; 4.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Extracellular matrix; Glycoprotein; Leucine-rich repeat; Proteoglycan;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 19
CHAIN 20 321 Epiphycan.
/FTId=PRO_0000032767.
DOMAIN 105 142 LRRNT.
REPEAT 143 164 LRR 1.
REPEAT 167 188 LRR 2.
REPEAT 191 212 LRR 3.
REPEAT 237 257 LRR 4.
REPEAT 258 279 LRR 5.
REPEAT 289 309 LRR 6.
COMPBIAS 77 86 Poly-Glu.
SITE 301 301 Not glycosylated.
CARBOHYD 60 60 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:9228042}.
CARBOHYD 64 64 O-linked (Xyl...) (dermatan sulfate)
serine. {ECO:0000305|PubMed:9228042}.
CARBOHYD 95 95 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:9228042}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:9228042}.
DISULFID 117 129 {ECO:0000250}.
DISULFID 278 311 {ECO:0000269|PubMed:9228042}.
SEQUENCE 321 AA; 36688 MW; 5D558F31C0B1FD89 CRC64;
MKALARLIVG LLILDAAVTA PTLESINYNS ETYDATLEDL DHLYNYENIP MGRAEIEIAT
VMPSGNRELL TPPPQPEEAE EEEEEESTPR LIDGSSPQEP EFTGVLGPQT NEDFPTCLLC
TCISTTVYCD DHELDAIPPL PKNTAYFYSR FNRIKKINKN DFASLNDLRR IDLTSNLISE
IDEDAFRKLP QLRELVLRDN KIRQLPELPT TLRFIDISNN RLGRKGIKQE AFKDMYDLHH
LYLTDNNLDH IPLPLPENLR ALHLQNNNIM EMHEDTFCNV KNLTYIRKAL EDIRLDGNPI
NLSKTPQAYM CLPRLPIGSL V


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