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O77742

- OMD_BOVIN

UniProt

O77742 - OMD_BOVIN

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Protein

Osteomodulin

Gene

OMD

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 277Sequence AnalysisPRO_0000032752
Chaini28 – 422395OsteomodulinPRO_0000032753Add
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 residuei412 – 4121SulfotyrosineBy similarity
Modified residuei413 – 4131SulfotyrosineBy similarity

Post-translational modificationi

The N-terminus is blocked.
Some of the oligosaccharides are extended to keratan sulfate chains.
Sulfated on tyrosine residue(s).Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan, Sulfation

Proteomic databases

PRIDEiO77742.

Expressioni

Tissue specificityi

Bone specific.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015704.

Structurei

3D structure databases

ProteinModelPortaliO77742.
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 – 28023LRR 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 – 40622Asp/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.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiO77742.
KOiK08124.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
[Graphical view]
PfamiPF13855. 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.

O77742-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGFSSLVCVL FFFLGVKVYC QYESYQWDED YDQEPDDVYQ TEFQFQQNIN
60 70 80 90 100
YEAPFHQHTL GCASECFCPP NFPSSMYCDN RKLKTIPNIP AHIQQVYLQF
110 120 130 140 150
NEIEAVTADS FINATHLKEI NLSHNKIKSQ KIDHGVFATL PNLLQLHLQH
160 170 180 190 200
NNLEDFPFPL PKSLERIFLG YNEISRLQTN AVNGLVNLTM LDLCFNKIDD
210 220 230 240 250
SVLQEKVLAK MEKLMQLNLC NNRLESMPPG LPSSLMYLSL ENNSISSIPE
260 270 280 290 300
NYFNKLPKLH ALRISHNKLQ DIPYNIFNLS NLIELNVGHN KLKQAFYIPR
310 320 330 340 350
NLEHLYLENN EIENVNVTVM CPSVDPLHYH HLTHIRIDQN KLKAPISSYI
360 370 380 390 400
FLCFPHIHTI YYGEQQSTNG QTIQLKTQVF RRFQDDGDSE DHDDHHEGPE
410 420
EEGTEENIDA HYYGSQEWQE TI
Length:422
Mass (Da):49,116
Last modified:November 1, 1998 - v1
Checksum:i3C349C3D6B59F5AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911L → R AA sequence (PubMed:9566981)Curated
Sequence conflicti194 – 1941C → Y AA sequence (PubMed:9566981)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U67279 mRNA. Translation: AAC39259.1.
RefSeqiNP_776372.1. NM_173947.2.
UniGeneiBt.114.

Genome annotation databases

GeneIDi280885.
KEGGibta:280885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U67279 mRNA. Translation: AAC39259.1 .
RefSeqi NP_776372.1. NM_173947.2.
UniGenei Bt.114.

3D structure databases

ProteinModelPortali O77742.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000015704.

Proteomic databases

PRIDEi O77742.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 280885.
KEGGi bta:280885.

Organism-specific databases

CTDi 4958.

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000234447.
HOVERGENi HBG108061.
InParanoidi O77742.
KOi K08124.

Miscellaneous databases

NextBioi 20805020.

Family and domain databases

InterProi IPR001611. Leu-rich_rpt.
IPR000372. LRR-contain_N.
[Graphical view ]
Pfami 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. "Osteoadherin, a cell binding keratan sulfate proteoglycan in bone, belongs to the family of leucine-rich repeat proteins of the extracellular matrix."
    Sommarin Y., Wendel M., Shen Z., Hellman U., Heinegaard D.
    J. Biol. Chem. 273:16723-16729(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-35; 119-126; 132-139; 191-198; 201-207; 264-268; 294-300 AND 377-381.
    Tissue: Osteoblast.
  2. "Bone matrix proteins: isolation and characterization of a novel cell-binding keratan sulfate proteoglycan (osteoadherin) from bovine bone."
    Wendel M., Sommarin Y., Heinegaard D.
    J. Cell Biol. 141:839-847(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 119-126 AND 191-198, CHARACTERIZATION.
    Tissue: Bone.

Entry informationi

Entry nameiOMD_BOVIN
AccessioniPrimary (citable) accession number: O77742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 94 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3