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Protein

Osteomodulin

Gene

Omd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

  • cell adhesion Source: UniProtKB-KW
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621818. Omd.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003275621 – 423OsteomodulinAdd BLAST403

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22SulfotyrosineBy similarity1
Modified residuei25SulfotyrosineBy similarity1
Modified residuei31SulfotyrosineBy similarity1
Modified residuei39SulfotyrosineBy similarity1
Modified residuei51SulfotyrosineBy similarity1
Modified residuei77SulfotyrosineBy similarity1
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Glycosylationi121N-linked (GlcNAc...)Sequence analysis1
Glycosylationi187N-linked (GlcNAc...)Sequence analysis1
Glycosylationi242N-linked (GlcNAc...)Sequence analysis1
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Glycosylationi316N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi321 ↔ 353By similarity
Modified residuei413SulfotyrosineBy similarity1
Modified residuei414SulfotyrosineBy similarity1

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067041.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1S7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 91LRRNTAdd BLAST39
Repeati92 – 113LRR 1Add BLAST22
Repeati116 – 129LRR 2Add BLAST14
Repeati142 – 164LRR 3Add BLAST23
Repeati165 – 184LRR 4Add BLAST20
Repeati187 – 207LRR 5Add BLAST21
Repeati213 – 233LRR 6Add BLAST21
Repeati234 – 255LRR 7Add BLAST22
Repeati258 – 279LRR 8Add BLAST22
Repeati281 – 294LRR 9Add BLAST14
Repeati301 – 322LRR 10Add BLAST22
Repeati331 – 353LRR 11Add BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi385 – 407Asp/Glu-rich (acidic)Add BLAST23

Sequence similaritiesi

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

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiQ9Z1S7.
PhylomeDBiQ9Z1S7.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR030705. Osteomodulin.
[Graphical view]
PANTHERiPTHR24373:SF155. PTHR24373:SF155. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF104362 mRNA. Translation: AAD04570.1.
UniGeneiRn.30124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104362 mRNA. Translation: AAD04570.1.
UniGeneiRn.30124.

3D structure databases

ProteinModelPortaliQ9Z1S7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067041.

Proteomic databases

PaxDbiQ9Z1S7.
PRIDEiQ9Z1S7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi621818. Omd.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiQ9Z1S7.
PhylomeDBiQ9Z1S7.

Miscellaneous databases

PROiQ9Z1S7.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
IPR030705. Osteomodulin.
[Graphical view]
PANTHERiPTHR24373:SF155. PTHR24373:SF155. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetiSearch...

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: July 6, 2016
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.