OMD_RAT
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 03-AUG-2022, entry version 129.
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 -!- SUBUNIT: Binds the alpha(V)beta(3)-integrin.
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: Binds keratan sulfate chains.
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 GlyGen; Q9Z1S7; 6 sites.
DR PhosphoSitePlus; Q9Z1S7; -.
DR PaxDb; Q9Z1S7; -.
DR PRIDE; Q9Z1S7; -.
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:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
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; -; 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 InterPro; IPR030705; Osteomodulin.
DR PANTHER; PTHR45712:SF3; PTHR45712:SF3; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 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
