Q99983 (OMD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein Proteoglycan Sulfation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW keratan sulfate biosynthetic process Traceable author statement. Source: Reactome keratan sulfate catabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome lysosomal lumen Traceable author statement. Source: Reactome proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 421	401	Osteomodulin		PRO_0000032754
Regions
	Domain	53 – 91	39	LRRNT
	Repeat	92 – 113	22	LRR 1
	Repeat	116 – 129	14	LRR 2
	Repeat	142 – 164	23	LRR 3
	Repeat	165 – 184	20	LRR 4
	Repeat	187 – 210	24	LRR 5
	Repeat	213 – 233	21	LRR 6
	Repeat	234 – 255	22	LRR 7
	Repeat	258 – 280	23	LRR 8
	Repeat	281 – 294	14	LRR 9
	Repeat	301 – 321	21	LRR 10
	Repeat	331 – 353	23	LRR 11
	Compositional bias	62 – 78	17	Cys-rich
	Compositional bias	385 – 409	25	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	22	1	Sulfotyrosine Probable
	Modified residue	25	1	Sulfotyrosine Probable
	Modified residue	31	1	Sulfotyrosine Probable
	Modified residue	39	1	Sulfotyrosine Ref.7
	Modified residue	51	1	Sulfotyrosine Probable
	Modified residue	58	1	Sulfotyrosine Probable
	Modified residue	77	1	Sulfotyrosine Probable
	Modified residue	416	1	Sulfotyrosine Ref.7
	Modified residue	417	1	Sulfotyrosine Ref.7
	Glycosylation	113	1	N-linked (GlcNAc...) Potential
	Glycosylation	121	1	N-linked (GlcNAc...) Potential
	Glycosylation	187	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
	Disulfide bond	321 ↔ 353		By similarity
Natural variations
	Natural variant	200	1	D → G. Corresponds to variant rs34069871 [ dbSNP | Ensembl ].		VAR_052014
	Natural variant	212	1	E → G. Corresponds to variant rs34413259 [ dbSNP | Ensembl ].		VAR_052015
	Natural variant	221	1	S → N. Corresponds to variant rs34860658 [ dbSNP | Ensembl ].		VAR_052016
	Natural variant	282	1	I → T. Corresponds to variant rs35779901 [ dbSNP | Ensembl ].		VAR_052017
	Natural variant	353	1	C → W. Corresponds to variant rs34059114 [ dbSNP | Ensembl ].		VAR_052018

Sequences

	Sequence		Length	Mass (Da)
	Q99983 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: CED47B2BC33BB872	FASTA	421	49,492
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
IPI	IPI00020990.
RefSeq	NP_005005.1. NM_005014.2.
UniGene	Hs.94070.
3D structure databases
ProteinModelPortal	Q99983.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000364700.
Polymorphism databases
DMDM	20138850.
Proteomic databases
PaxDb	Q99983.
PRIDE	Q99983.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375550; ENSP00000364700; ENSG00000127083.
GeneID	4958.
KEGG	hsa:4958.
UCSC	uc004asd.4. human.
Organism-specific databases
CTD	4958.
GeneCards	GC09M095176.
HGNC	HGNC:8134. OMD.
neXtProt	NX_Q99983.
PharmGKB	PA31921.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4886.
HOGENOM	HOG000234447.
HOVERGEN	HBG108061.
InParanoid	Q99983.
KO	K08124.
OMA	FYIPRNL.
OrthoDB	EOG415GDJ.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
Bgee	Q99983.
CleanEx	HS_OMD.
Genevestigator	Q99983.
GermOnline	ENSG00000127083. Homo sapiens.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR003591. Leu-rich_rpt_typical-subtyp. IPR000372. LRR-contain_N. [Graphical view]
Pfam	PF01462. LRRNT. 1 hit. [Graphical view]
SMART	SM00369. LRR_TYP. 1 hit. SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 8 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	4958.
NextBio	19096.

Entry information

Entry name

OMD_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.