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Q9Z1S7

- OMD_RAT

UniProt

Q9Z1S7 - OMD_RAT

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Protein

Osteomodulin

Gene

Omd

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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
  2. regulation of bone mineralization Source: RGD
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621818. Omd.

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
Chaini21 – 423403OsteomodulinPRO_0000032756Add
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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan, Sulfation

Proteomic databases

PaxDbiQ9Z1S7.
PRIDEiQ9Z1S7.

Expressioni

Tissue specificityi

Osteoblast and odontoblast. Expressed in femoral bone and calvaria tissues. Detected in femoral head, rib, tendon and bone marrow.1 Publication

Developmental stagei

In developing molars, it was first detected in alveolar bone in 19-day-old embryos. In more mature teeth (newborn and 2-day-old rats), the expression starts in the polarized odontoblasts and increases in the secretory and mature odontoblasts.1 Publication

Gene expression databases

GenevestigatoriQ9Z1S7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020648.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1S7.
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 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.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiQ9Z1S7.
KOiK08124.
PhylomeDBiQ9Z1S7.

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.

Q9Z1S7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGCLRPIYVL FFCFVVRVYG QYEAYQWDED YEQEPSEDYE PEFQFHQNIE
60 70 80 90 100
YGAPFYQNIL GCAKECFCPT NFPTSMYCDN RKLKTIPDIP MHIQQLNLQF
110 120 130 140 150
NDIEAVTADS FINATHLKEI NLSHNKIKSQ KIDYGVFAKL SNLQQLHLDH
160 170 180 190 200
NNLEEFPFPL PKSLERLLLG YNEISTLPTH AMDGLVNVTM LDLCYNHLSD
210 220 230 240 250
STLKGKILSK LEKLMQLNLC NNRLESMPPG LPLSLMYLSL ENNSISSIPE
260 270 280 290 300
DYFQKLPKLH ALRISHNKLE DIPYDIFNLS NLIELNVGHN KLKQAFYIPR
310 320 330 340 350
NLEHLYLQNN EIQSINVTMM CPSLDPLHHH HLTYLRVDQN KLKEPISSYI
360 370 380 390 400
FFCFPRIHSI YYGEQRSTNG ETIQLKTQVF RRYQDEEEEE EDDSQDHTLE
410 420
GQEETEEHFN SHYYEMQAWQ NTI
Length:423
Mass (Da):49,783
Last modified:May 1, 1999 - v1
Checksum:i587D679FD9482E9F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104362 mRNA. Translation: AAD04570.1.
RefSeqiNP_114005.1. NM_031817.1.
UniGeneiRn.30124.

Genome annotation databases

GeneIDi83717.
KEGGirno:83717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104362 mRNA. Translation: AAD04570.1 .
RefSeqi NP_114005.1. NM_031817.1.
UniGenei Rn.30124.

3D structure databases

ProteinModelPortali Q9Z1S7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000020648.

Proteomic databases

PaxDbi Q9Z1S7.
PRIDEi Q9Z1S7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 83717.
KEGGi rno:83717.

Organism-specific databases

CTDi 4958.
RGDi 621818. Omd.

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000234447.
HOVERGENi HBG108061.
InParanoidi Q9Z1S7.
KOi K08124.
PhylomeDBi Q9Z1S7.

Miscellaneous databases

NextBioi 616285.
PROi Q9Z1S7.

Gene expression databases

Genevestigatori Q9Z1S7.

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. "Tissue distribution of a novel cell binding protein, osteoadherin, in the rat."
    Shen Z., Gantcheva S., Sommarin Y., Heinegaard D.
    Matrix Biol. 18:533-542(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Calvaria.

Entry informationi

Entry nameiOMD_RAT
AccessioniPrimary (citable) accession number: Q9Z1S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 96 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3