EPYC_BOVIN
ID EPYC_BOVIN Reviewed; 321 AA.
AC P79119;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Epiphycan;
DE AltName: Full=Dermatan sulfate proteoglycan 3;
DE AltName: Full=Proteoglycan-Lb;
DE Short=PG-Lb;
DE AltName: Full=Small chondroitin/dermatan sulfate proteoglycan;
DE Flags: Precursor;
GN Name=EPYC; Synonyms=DSPG3, PGLB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT
RP THR-60; SER-64; SER-95 AND ASN-282, TISSUE SPECIFICITY, AND DISULFIDE BOND.
RC TISSUE=Fetal epiphyseal cartilage;
RX PubMed=9228042; DOI=10.1074/jbc.272.30.18709;
RA Johnson H.J., Rosenberg L., Choi H.U., Garza S., Hoeoek M., Neame P.J.;
RT "Characterization of epiphycan, a small proteoglycan with a leucine-rich
RT repeat core protein.";
RL J. Biol. Chem. 272:18709-18717(1997).
CC -!- FUNCTION: May have a role in bone formation and also in establishing
CC the ordered structure of cartilage through matrix organization.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the zone of flattened
CC chondrocytes of the developing limb cartilage.
CC {ECO:0000269|PubMed:9228042}.
CC -!- DEVELOPMENTAL STAGE: Embryo.
CC -!- PTM: A long and a short form present in approximately equimolar amounts
CC may arise by proteolysis or cleavage by exopeptidases.
CC -!- PTM: The O-linked polysaccharides on Thr-60 and Ser-95 are probably the
CC mucin type linked to GalNAc. There is one glycosaminoglycan chain,
CC known to be dermatan sulfate, and it is probably the O-glycosylation at
CC Ser-64. {ECO:0000269|PubMed:9228042}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class III subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77127; AAB68397.1; -; mRNA.
DR RefSeq; NP_776732.1; NM_174307.2.
DR RefSeq; XP_010803061.1; XM_010804759.2.
DR AlphaFoldDB; P79119; -.
DR SMR; P79119; -.
DR IntAct; P79119; 1.
DR STRING; 9913.ENSBTAP00000010504; -.
DR iPTMnet; P79119; -.
DR PaxDb; P79119; -.
DR PRIDE; P79119; -.
DR Ensembl; ENSBTAT00000010504; ENSBTAP00000010504; ENSBTAG00000007990.
DR GeneID; 281747; -.
DR KEGG; bta:281747; -.
DR CTD; 1833; -.
DR VEuPathDB; HostDB:ENSBTAG00000007990; -.
DR VGNC; VGNC:28558; EPYC.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157574; -.
DR HOGENOM; CLU_067583_0_0_1; -.
DR InParanoid; P79119; -.
DR OMA; CLLCTCM; -.
DR OrthoDB; 1109019at2759; -.
DR TreeFam; TF351924; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000007990; Expressed in cardiac atrium and 30 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0061975; P:articular cartilage development; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR027217; Epiphycan.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR043547; Mimecan/Epiphycan.
DR PANTHER; PTHR46269; PTHR46269; 1.
DR PANTHER; PTHR46269:SF3; PTHR46269:SF3; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Leucine-rich repeat; Proteoglycan; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..321
FT /note="Epiphycan"
FT /id="PRO_0000032767"
FT DOMAIN 105..142
FT /note="LRRNT"
FT REPEAT 143..164
FT /note="LRR 1"
FT REPEAT 167..188
FT /note="LRR 2"
FT REPEAT 191..212
FT /note="LRR 3"
FT REPEAT 237..257
FT /note="LRR 4"
FT REPEAT 258..279
FT /note="LRR 5"
FT REPEAT 289..309
FT /note="LRR 6"
FT REGION 64..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 301
FT /note="Not glycosylated"
FT CARBOHYD 60
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:9228042"
FT CARBOHYD 64
FT /note="O-linked (Xyl...) (dermatan sulfate) serine"
FT /evidence="ECO:0000305|PubMed:9228042"
FT CARBOHYD 95
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:9228042"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:9228042"
FT DISULFID 117..129
FT /evidence="ECO:0000250"
FT DISULFID 278..311
FT /evidence="ECO:0000269|PubMed:9228042"
SQ 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
