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Q99983 (OMD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Osteomodulin
Alternative name(s):
Keratan sulfate proteoglycan osteomodulin
Short name=KSPG osteomodulin
Osteoadherin
Short name=OSAD
Gene names
Name:OMD
Synonyms:SLRR2C
ORF Names:UNQ190/PRO216
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Bone specific.

Post-translational modification

Binds keratan sulfate chains By similarity.

Sequence similarities

Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily.

Contains 11 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 421401Osteomodulin
PRO_0000032754

Regions

Domain53 – 9139LRRNT
Repeat92 – 11322LRR 1
Repeat116 – 12914LRR 2
Repeat142 – 16423LRR 3
Repeat165 – 18420LRR 4
Repeat187 – 21024LRR 5
Repeat213 – 23321LRR 6
Repeat234 – 25522LRR 7
Repeat258 – 28023LRR 8
Repeat281 – 29414LRR 9
Repeat301 – 32121LRR 10
Repeat331 – 35323LRR 11
Compositional bias62 – 7817Cys-rich
Compositional bias385 – 40925Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue221Sulfotyrosine Probable
Modified residue251Sulfotyrosine Probable
Modified residue311Sulfotyrosine Probable
Modified residue391Sulfotyrosine Ref.7
Modified residue511Sulfotyrosine Probable
Modified residue581Sulfotyrosine Probable
Modified residue771Sulfotyrosine Probable
Modified residue4161Sulfotyrosine Ref.7
Modified residue4171Sulfotyrosine Ref.7
Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Disulfide bond321 ↔ 353 By similarity

Natural variations

Natural variant2001D → G.
Corresponds to variant rs34069871 [ dbSNP | Ensembl ].
VAR_052014
Natural variant2121E → G.
Corresponds to variant rs34413259 [ dbSNP | Ensembl ].
VAR_052015
Natural variant2211S → N.
Corresponds to variant rs34860658 [ dbSNP | Ensembl ].
VAR_052016
Natural variant2821I → T.
Corresponds to variant rs35779901 [ dbSNP | Ensembl ].
VAR_052017
Natural variant3531C → W.
Corresponds to variant rs34059114 [ dbSNP | Ensembl ].
VAR_052018

Sequences

Sequence LengthMass (Da)Tools
Q99983 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: CED47B2BC33BB872

FASTA42149,492
        10         20         30         40         50         60 
MGFLSPIYVI FFFFGVKVHC QYETYQWDED YDQEPDDDYQ TGFPFRQNVD YGVPFHQYTL 

        70         80         90        100        110        120 
GCVSECFCPT NFPSSMYCDN RKLKTIPNIP MHIQQLYLQF NEIEAVTANS FINATHLKEI 

       130        140        150        160        170        180 
NLSHNKIKSQ KIDYGVFAKL PNLLQLHLEH NNLEEFPFPL PKSLERLLLG YNEISKLQTN 

       190        200        210        220        230        240 
AMDGLVNLTM LDLCYNYLHD SLLKDKIFAK MEKLMQLNLC SNRLESMPPG LPSSLMYLSL 

       250        260        270        280        290        300 
ENNSISSIPE KYFDKLPKLH TLRMSHNKLQ DIPYNIFNLP NIVELSVGHN KLKQAFYIPR 

       310        320        330        340        350        360 
NLEHLYLQNN EIEKMNLTVM CPSIDPLHYH HLTYIRVDQN KLKEPISSYI FFCFPHIHTI 

       370        380        390        400        410        420 
YYGEQRSTNG QTIQLKTQVF RRFPDDDDES EDHDDPDNAH ESPEQEGAEG HFDLHYYENQ 


E 

« Hide

References

« Hide 'large scale' references
[1]"The cloning of a cDNA for novel genes expressed in human osteoblast."
Ohno I., Hashimoto J., Takaoka K., Ochi T., Okubo K., Matsubara K.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Osteoblast.
[2]"Human osteomodulin gene: intron-exon junctions and chromosomal localization."
Ohno I., Matsubara K., Okubo K.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry."
Onnerfjord P., Heathfield T.F., Heinegaard D.
J. Biol. Chem. 279:26-33(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-22; TYR-25; TYR-31; TYR-39; TYR-51; TYR-58; TYR-77; TYR-416 AND TYR-417, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB000114 mRNA. Translation: BAA19055.1.
AB009589 Genomic DNA. Translation: BAA23982.1.
AY358872 mRNA. Translation: AAQ89231.1.
AL137848 Genomic DNA. Translation: CAI16696.1.
CH471089 Genomic DNA. Translation: EAW62821.1.
BC046356 mRNA. Translation: AAH46356.1.
RefSeqNP_005005.1. NM_005014.2.
UniGeneHs.94070.

3D structure databases

ProteinModelPortalQ99983.
SMRQ99983. Positions 61-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000364700.

Polymorphism databases

DMDM20138850.

Proteomic databases

PaxDbQ99983.
PRIDEQ99983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375550; ENSP00000364700; ENSG00000127083.
GeneID4958.
KEGGhsa:4958.
UCSCuc004asd.4. human.

Organism-specific databases

CTD4958.
GeneCardsGC09M095176.
HGNCHGNC:8134. OMD.
neXtProtNX_Q99983.
PharmGKBPA31921.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000234447.
HOVERGENHBG108061.
InParanoidQ99983.
KOK08124.
OMAFYIPRNL.
OrthoDBEOG741Z2B.
TreeFamTF334562.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeQ99983.
CleanExHS_OMD.
GenevestigatorQ99983.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiOMD_(gene).
GenomeRNAi4958.
NextBio19096.
PROQ99983.

Entry information

Entry nameOMD_HUMAN
AccessionPrimary (citable) accession number: Q99983
Secondary accession number(s): Q5TBF4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: May 1, 1997
Last modified: March 19, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM