OMD_BOVIN
ID OMD_BOVIN Reviewed; 422 AA.
AC O77742;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Osteomodulin;
DE AltName: Full=Keratan sulfate proteoglycan osteomodulin;
DE Short=KSPG osteomodulin;
DE AltName: Full=Osteoadherin;
DE Short=OSAD;
DE Flags: Precursor;
GN Name=OMD;
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], AND PROTEIN SEQUENCE OF 28-35; 119-126;
RP 132-139; 191-198; 201-207; 264-268; 294-300 AND 377-381.
RC TISSUE=Osteoblast;
RX PubMed=9642227; DOI=10.1074/jbc.273.27.16723;
RA Sommarin Y., Wendel M., Shen Z., Hellman U., Heinegaard D.;
RT "Osteoadherin, a cell binding keratan sulfate proteoglycan in bone, belongs
RT to the family of leucine-rich repeat proteins of the extracellular
RT matrix.";
RL J. Biol. Chem. 273:16723-16729(1998).
RN [2]
RP PROTEIN SEQUENCE OF 119-126 AND 191-198, AND CHARACTERIZATION.
RC TISSUE=Bone;
RX PubMed=9566981; DOI=10.1083/jcb.141.3.839;
RA Wendel M., Sommarin Y., Heinegaard D.;
RT "Bone matrix proteins: isolation and characterization of a novel cell-
RT binding keratan sulfate proteoglycan (osteoadherin) from bovine bone.";
RL J. Cell Biol. 141:839-847(1998).
CC -!- FUNCTION: May be implicated in biomineralization processes. Has a
CC function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
CC -!- SUBUNIT: Binds the alpha(V)beta(3)-integrin.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Bone specific.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Some of the oligosaccharides are extended to keratan sulfate
CC chains.
CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; U67279; AAC39259.1; -; mRNA.
DR RefSeq; NP_776372.1; NM_173947.2.
DR AlphaFoldDB; O77742; -.
DR SMR; O77742; -.
DR STRING; 9913.ENSBTAP00000015704; -.
DR PaxDb; O77742; -.
DR PRIDE; O77742; -.
DR GeneID; 280885; -.
DR KEGG; bta:280885; -.
DR CTD; 4958; -.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; O77742; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 2.
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; IPR030705; Osteomodulin.
DR PANTHER; PTHR45712:SF3; PTHR45712:SF3; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..27
FT /evidence="ECO:0000255"
FT /id="PRO_0000032752"
FT CHAIN 28..422
FT /note="Osteomodulin"
FT /id="PRO_0000032753"
FT DOMAIN 53..91
FT /note="LRRNT"
FT REPEAT 92..113
FT /note="LRR 1"
FT REPEAT 116..129
FT /note="LRR 2"
FT REPEAT 142..164
FT /note="LRR 3"
FT REPEAT 165..184
FT /note="LRR 4"
FT REPEAT 187..207
FT /note="LRR 5"
FT REPEAT 213..233
FT /note="LRR 6"
FT REPEAT 234..255
FT /note="LRR 7"
FT REPEAT 258..280
FT /note="LRR 8"
FT REPEAT 281..294
FT /note="LRR 9"
FT REPEAT 301..322
FT /note="LRR 10"
FT REPEAT 331..353
FT /note="LRR 11"
FT REGION 385..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 31
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 77
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 412
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 413
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 321..353
FT /evidence="ECO:0000250"
FT CONFLICT 191
FT /note="L -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="C -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 49116 MW; 3C349C3D6B59F5AD CRC64;
MGFSSLVCVL FFFLGVKVYC QYESYQWDED YDQEPDDVYQ TEFQFQQNIN YEAPFHQHTL
GCASECFCPP NFPSSMYCDN RKLKTIPNIP AHIQQVYLQF NEIEAVTADS FINATHLKEI
NLSHNKIKSQ KIDHGVFATL PNLLQLHLQH NNLEDFPFPL PKSLERIFLG YNEISRLQTN
AVNGLVNLTM LDLCFNKIDD SVLQEKVLAK MEKLMQLNLC NNRLESMPPG LPSSLMYLSL
ENNSISSIPE NYFNKLPKLH ALRISHNKLQ DIPYNIFNLS NLIELNVGHN KLKQAFYIPR
NLEHLYLENN EIENVNVTVM CPSVDPLHYH HLTHIRIDQN KLKAPISSYI FLCFPHIHTI
YYGEQQSTNG QTIQLKTQVF RRFQDDGDSE DHDDHHEGPE EEGTEENIDA HYYGSQEWQE
TI
