ID   OMD_RAT                 Reviewed;         423 AA.
AC   Q9Z1S7;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-NOV-2023, entry version 134.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Calvaria;
RX   PubMed=10607915; DOI=10.1016/s0945-053x(99)00048-7;
RA   Shen Z., Gantcheva S., Sommarin Y., Heinegaard D.;
RT   "Tissue distribution of a novel cell binding protein, osteoadherin, in the
RT   rat.";
RL   Matrix Biol. 18:533-542(1999).
CC   -!- FUNCTION: May be implicated in biomineralization processes. Has a
CC       function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
CC       {ECO:0000250|UniProtKB:O77742}.
CC   -!- SUBUNIT: Binds the alpha(V)beta(3)-integrin.
CC       {ECO:0000250|UniProtKB:O77742}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Osteoblast and odontoblast. Expressed in femoral
CC       bone and calvaria tissues. Detected in femoral head, rib, tendon and
CC       bone marrow. {ECO:0000269|PubMed:10607915}.
CC   -!- DEVELOPMENTAL STAGE: In developing molars, it was first detected in
CC       alveolar bone in 19-day-old embryos. In more mature teeth (newborn and
CC       2-day-old rats), the expression starts in the polarized odontoblasts
CC       and increases in the secretory and mature odontoblasts.
CC       {ECO:0000269|PubMed:10607915}.
CC   -!- PTM: Glycosylated; contains keratan sulfate.
CC       {ECO:0000250|UniProtKB:O77742}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; AF104362; AAD04570.1; -; mRNA.
DR   AlphaFoldDB; Q9Z1S7; -.
DR   SMR; Q9Z1S7; -.
DR   STRING; 10116.ENSRNOP00000020648; -.
DR   GlyCosmos; Q9Z1S7; 6 sites, No reported glycans.
DR   GlyGen; Q9Z1S7; 6 sites.
DR   PhosphoSitePlus; Q9Z1S7; -.
DR   PaxDb; 10116-ENSRNOP00000020648; -.
DR   AGR; RGD:621818; -.
DR   RGD; 621818; Omd.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; Q9Z1S7; -.
DR   PhylomeDB; Q9Z1S7; -.
DR   Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-RNO-2022857; Keratan sulfate degradation.
DR   PRO; PR:Q9Z1S7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030500; P:regulation of bone mineralization; NAS:RGD.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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   PANTHER; PTHR45712; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF3; OSTEOMODULIN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00364; LRR_BAC; 5.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 8.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Leucine-rich repeat; Proteoglycan; Reference proteome; Repeat; Secreted;
KW   Signal; Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..423
FT                   /note="Osteomodulin"
FT                   /id="PRO_0000032756"
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..279
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          383..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..400
FT                   /note="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         413
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         414
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"
SQ   SEQUENCE   423 AA;  49783 MW;  587D679FD9482E9F CRC64;
     MGCLRPIYVL FFCFVVRVYG QYEAYQWDED YEQEPSEDYE PEFQFHQNIE YGAPFYQNIL
     GCAKECFCPT NFPTSMYCDN RKLKTIPDIP MHIQQLNLQF NDIEAVTADS FINATHLKEI
     NLSHNKIKSQ KIDYGVFAKL SNLQQLHLDH NNLEEFPFPL PKSLERLLLG YNEISTLPTH
     AMDGLVNVTM LDLCYNHLSD STLKGKILSK LEKLMQLNLC NNRLESMPPG LPLSLMYLSL
     ENNSISSIPE DYFQKLPKLH ALRISHNKLE DIPYDIFNLS NLIELNVGHN KLKQAFYIPR
     NLEHLYLQNN EIQSINVTMM CPSLDPLHHH HLTYLRVDQN KLKEPISSYI FFCFPRIHSI
     YYGEQRSTNG ETIQLKTQVF RRYQDEEEEE EDDSQDHTLE GQEETEEHFN SHYYEMQAWQ
     NTI
//