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PGS1_RABIT
ID   PGS1_RABIT              Reviewed;         135 AA.
AC   O46377;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Biglycan;
DE   AltName: Full=Bone/cartilage proteoglycan I;
DE   AltName: Full=PG-S1;
DE   Flags: Fragment;
GN   Name=BGN;
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   STRAIN=New Zealand white;
RX   PubMed=9822203; DOI=10.1016/s0945-053x(98)90089-0;
RA   Boykiw R.H., Sciore P., Reno C.R., Marchuk L., Frank C., Hart D.A.;
RT   "Altered levels of extracellular matrix molecules mRNA in healing rabbit
RT   ligaments.";
RL   Matrix Biol. 17:371-378(1998).
CC   -!- FUNCTION: May be involved in collagen fiber assembly. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Forms a ternary complex with MFAP2 and ELN (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Found in several connective tissues, especially in
CC       articular cartilages.
CC   -!- PTM: The two attached glycosaminoglycan chains can be either
CC       chondroitin sulfate or dermatan sulfate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000305}.
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DR   EMBL; AF020290; AAC39515.1; -; mRNA.
DR   AlphaFoldDB; O46377; -.
DR   SMR; O46377; -.
DR   STRING; 9986.ENSOCUP00000026470; -.
DR   PRIDE; O46377; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; O46377; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR028547; Biglycan.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45712:SF11; PTHR45712:SF11; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   PROSITE; PS51450; LRR; 4.
PE   2: Evidence at transcript level;
KW   Extracellular matrix; Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW   Reference proteome; Repeat; Secreted.
FT   CHAIN           <1..>135
FT                   /note="Biglycan"
FT                   /id="PRO_0000180083"
FT   REPEAT          4..24
FT                   /note="LRR 1"
FT   REPEAT          25..46
FT                   /note="LRR 2"
FT   REPEAT          49..72
FT                   /note="LRR 3"
FT   REPEAT          73..95
FT                   /note="LRR 4"
FT   REPEAT          96..117
FT                   /note="LRR 5"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         135
SQ   SEQUENCE   135 AA;  15323 MW;  EFDC6E74D42F5098 CRC64;
     DGLKLNYLRI SEAKLTGIPK DLPETLNELH LDHNKIQAIE LEDLLRYSKL YRLGLGHNQI
     RMIENGSLSF LPTLRELHLD NNKLSRVPAG LPDLKLLQVV YLHSNNITKV GVNDFCPVGF
     GVKRAYYNGI SLFNN
 
 
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