OMD_MOUSE
ID OMD_MOUSE Reviewed; 423 AA.
AC O35103;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Ohno I., Matsubara K., Okubo K.;
RT "The cloning and characterization of a cDNA for the novel bone matrix
RT protein; osteomodulin.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be implicated in biomineralization processes. Has a
CC function in binding of osteoblasts via the alpha(V)beta(3)-integrin (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds the alpha(V)beta(3)-integrin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Bone specific.
CC -!- PTM: Binds keratan sulfate chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; AB007848; BAA22790.1; -; mRNA.
DR CCDS; CCDS26504.1; -.
DR RefSeq; NP_036180.1; NM_012050.2.
DR RefSeq; XP_006516991.1; XM_006516928.2.
DR RefSeq; XP_017171009.1; XM_017315520.1.
DR AlphaFoldDB; O35103; -.
DR SMR; O35103; -.
DR STRING; 10090.ENSMUSP00000065706; -.
DR GlyGen; O35103; 6 sites.
DR PhosphoSitePlus; O35103; -.
DR MaxQB; O35103; -.
DR PaxDb; O35103; -.
DR PRIDE; O35103; -.
DR ProteomicsDB; 294274; -.
DR Antibodypedia; 28259; 206 antibodies from 27 providers.
DR DNASU; 27047; -.
DR Ensembl; ENSMUST00000065494; ENSMUSP00000065706; ENSMUSG00000048368.
DR Ensembl; ENSMUST00000221170; ENSMUSP00000152066; ENSMUSG00000048368.
DR GeneID; 27047; -.
DR KEGG; mmu:27047; -.
DR UCSC; uc007qjp.1; mouse.
DR CTD; 4958; -.
DR MGI; MGI:1350918; Omd.
DR VEuPathDB; HostDB:ENSMUSG00000048368; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160986; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; O35103; -.
DR OMA; YNIFNLS; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O35103; -.
DR TreeFam; TF334562; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR BioGRID-ORCS; 27047; 3 hits in 72 CRISPR screens.
DR PRO; PR:O35103; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O35103; protein.
DR Bgee; ENSMUSG00000048368; Expressed in vault of skull and 121 other tissues.
DR Genevisible; O35103; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
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; IEA:InterPro.
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; 2.
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_0000032755"
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 381..406
FT /note="Disordered"
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; 49745 MW; 41ED7CA6B3A6F3B7 CRC64;
MGFLSPIYVL FFCFGVRVYC QYEAYRWDDD YDQEPNEDYD PEFQFHQNIE YGVPFYNNIL
GCAKECFCPT NFPTSMYCDN RKLKTIPIIP MHIQQLNLQF NDIEAVTANS FINATHLKEI
NLSHNKIKSQ KIDYGVFAKL SNLQQLHLEH NNLEEFPFPL PKSLERLLLG YNEISILPTN
AMDGLVNVTM LDLCYNHLSD SMLKEKTLSK MEKLMQLNLC NNRLESMPLG LPSSLMYLSL
ENNSISSIPD NYFDKLPKLH ALRISHNKLE DIPYDIFNLS NLIELNVGHN KLKQAFYIPR
NLEHLYLQNN EIESINVTMI CPSPDPVHHH HLTYLRVDQN KLKEPISSYI FFCFPRIHSI
YYGEQRSTNG ETIQLKTQVF RSYQEEEEED DHDSQDNTLE GQEVSDEHYN SHYYEMQEWQ
DTI
