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O35103

- OMD_MOUSE

UniProt

O35103 - OMD_MOUSE

Protein

Osteomodulin

Gene

Omd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin By similarity.By similarity

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_198578. Keratan sulfate biosynthesis.
    REACT_198960. Keratan sulfate degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Osteomodulin
    Alternative name(s):
    Keratan sulfate proteoglycan osteomodulin
    Short name:
    KSPG osteomodulin
    Osteoadherin
    Short name:
    OSAD
    Gene namesi
    Name:Omd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1350918. Omd.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 423403OsteomodulinPRO_0000032755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei22 – 221SulfotyrosineBy similarity
    Modified residuei25 – 251SulfotyrosineBy similarity
    Modified residuei31 – 311SulfotyrosineBy similarity
    Modified residuei39 – 391SulfotyrosineBy similarity
    Modified residuei51 – 511SulfotyrosineBy similarity
    Modified residuei77 – 771SulfotyrosineBy similarity
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi321 ↔ 353By similarity
    Modified residuei413 – 4131SulfotyrosineBy similarity
    Modified residuei414 – 4141SulfotyrosineBy similarity

    Post-translational modificationi

    Binds keratan sulfate chains.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan, Sulfation

    Proteomic databases

    PRIDEiO35103.

    Expressioni

    Tissue specificityi

    Bone specific.

    Gene expression databases

    BgeeiO35103.
    CleanExiMM_OMD.
    GenevestigatoriO35103.

    Interactioni

    Subunit structurei

    Binds the alpha(V)beta(3)-integrin.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO35103.
    SMRiO35103. Positions 61-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 9139LRRNTAdd
    BLAST
    Repeati92 – 11322LRR 1Add
    BLAST
    Repeati116 – 12914LRR 2Add
    BLAST
    Repeati142 – 16423LRR 3Add
    BLAST
    Repeati165 – 18420LRR 4Add
    BLAST
    Repeati187 – 20721LRR 5Add
    BLAST
    Repeati213 – 23321LRR 6Add
    BLAST
    Repeati234 – 25522LRR 7Add
    BLAST
    Repeati258 – 27922LRR 8Add
    BLAST
    Repeati281 – 29414LRR 9Add
    BLAST
    Repeati301 – 32222LRR 10Add
    BLAST
    Repeati331 – 35323LRR 11Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi62 – 7817Cys-richAdd
    BLAST
    Compositional biasi385 – 40723Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Contains 11 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4886.
    GeneTreeiENSGT00600000084286.
    HOGENOMiHOG000234447.
    HOVERGENiHBG108061.
    InParanoidiO35103.
    KOiK08124.
    OMAiFYIPRNL.
    OrthoDBiEOG741Z2B.
    PhylomeDBiO35103.
    TreeFamiTF334562.

    Family and domain databases

    InterProiIPR001611. Leu-rich_rpt.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 2 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    SMARTiSM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O35103-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFLSPIYVL FFCFGVRVYC QYEAYRWDDD YDQEPNEDYD PEFQFHQNIE    50
    YGVPFYNNIL GCAKECFCPT NFPTSMYCDN RKLKTIPIIP MHIQQLNLQF 100
    NDIEAVTANS FINATHLKEI NLSHNKIKSQ KIDYGVFAKL SNLQQLHLEH 150
    NNLEEFPFPL PKSLERLLLG YNEISILPTN AMDGLVNVTM LDLCYNHLSD 200
    SMLKEKTLSK MEKLMQLNLC NNRLESMPLG LPSSLMYLSL ENNSISSIPD 250
    NYFDKLPKLH ALRISHNKLE DIPYDIFNLS NLIELNVGHN KLKQAFYIPR 300
    NLEHLYLQNN EIESINVTMI CPSPDPVHHH HLTYLRVDQN KLKEPISSYI 350
    FFCFPRIHSI YYGEQRSTNG ETIQLKTQVF RSYQEEEEED DHDSQDNTLE 400
    GQEVSDEHYN SHYYEMQEWQ DTI 423
    Length:423
    Mass (Da):49,745
    Last modified:January 1, 1998 - v1
    Checksum:i41ED7CA6B3A6F3B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007848 mRNA. Translation: BAA22790.1.
    CCDSiCCDS26504.1.
    RefSeqiNP_036180.1. NM_012050.2.
    XP_006516991.1. XM_006516928.1.
    UniGeneiMm.390589.

    Genome annotation databases

    EnsembliENSMUST00000065494; ENSMUSP00000065706; ENSMUSG00000048368.
    GeneIDi27047.
    KEGGimmu:27047.
    UCSCiuc007qjp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007848 mRNA. Translation: BAA22790.1 .
    CCDSi CCDS26504.1.
    RefSeqi NP_036180.1. NM_012050.2.
    XP_006516991.1. XM_006516928.1.
    UniGenei Mm.390589.

    3D structure databases

    ProteinModelPortali O35103.
    SMRi O35103. Positions 61-352.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O35103.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000065494 ; ENSMUSP00000065706 ; ENSMUSG00000048368 .
    GeneIDi 27047.
    KEGGi mmu:27047.
    UCSCi uc007qjp.1. mouse.

    Organism-specific databases

    CTDi 4958.
    MGIi MGI:1350918. Omd.

    Phylogenomic databases

    eggNOGi COG4886.
    GeneTreei ENSGT00600000084286.
    HOGENOMi HOG000234447.
    HOVERGENi HBG108061.
    InParanoidi O35103.
    KOi K08124.
    OMAi FYIPRNL.
    OrthoDBi EOG741Z2B.
    PhylomeDBi O35103.
    TreeFami TF334562.

    Enzyme and pathway databases

    Reactomei REACT_198578. Keratan sulfate biosynthesis.
    REACT_198960. Keratan sulfate degradation.

    Miscellaneous databases

    NextBioi 304973.
    PROi O35103.
    SOURCEi Search...

    Gene expression databases

    Bgeei O35103.
    CleanExi MM_OMD.
    Genevestigatori O35103.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF00560. LRR_1. 1 hit.
    PF13855. LRR_8. 2 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    SMARTi SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cloning and characterization of a cDNA for the novel bone matrix protein; osteomodulin."
      Ohno I., Matsubara K., Okubo K.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.

    Entry informationi

    Entry nameiOMD_MOUSE
    AccessioniPrimary (citable) accession number: O35103
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 11, 2002
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3