ID   OMD_HUMAN               Reviewed;         421 AA.
AC   Q99983; Q5TBF4;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 190.
DE   RecName: Full=Osteomodulin;
DE   AltName: Full=Keratan sulfate proteoglycan osteomodulin;
DE            Short=KSPG osteomodulin;
DE   AltName: Full=Osteoadherin;
DE            Short=OSAD;
DE   Flags: Precursor;
GN   Name=OMD; Synonyms=SLRR2C; ORFNames=UNQ190/PRO216;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Osteoblast;
RA   Ohno I., Hashimoto J., Takaoka K., Ochi T., Okubo K., Matsubara K.;
RT   "The cloning of a cDNA for novel genes expressed in human osteoblast.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ohno I., Matsubara K., Okubo K.;
RT   "Human osteomodulin gene: intron-exon junctions and chromosomal
RT   localization.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   SULFATION AT TYR-22; TYR-25; TYR-31; TYR-39; TYR-51; TYR-58; TYR-77;
RP   TYR-416 AND TYR-417, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14551184; DOI=10.1074/jbc.m308689200;
RA   Onnerfjord P., Heathfield T.F., Heinegaard D.;
RT   "Identification of tyrosine sulfation in extracellular leucine-rich repeat
RT   proteins using mass spectrometry.";
RL   J. Biol. Chem. 279:26-33(2004).
CC   -!- FUNCTION: May be implicated in biomineralization processes. Has a
CC       function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
CC       {ECO:0000250|UniProtKB:O77742}.
CC   -!- SUBUNIT: Binds the alpha(V)beta(3)-integrin.
CC       {ECO:0000250|UniProtKB:O77742}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Bone specific.
CC   -!- PTM: Glycosylated; contains keratan sulfate.
CC       {ECO:0000250|UniProtKB:O77742}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; AB000114; BAA19055.1; -; mRNA.
DR   EMBL; AB009589; BAA23982.1; -; Genomic_DNA.
DR   EMBL; AY358872; AAQ89231.1; -; mRNA.
DR   EMBL; AL137848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62821.1; -; Genomic_DNA.
DR   EMBL; BC046356; AAH46356.1; -; mRNA.
DR   CCDS; CCDS6696.1; -.
DR   RefSeq; NP_005005.1; NM_005014.2.
DR   PDB; 5YQ5; X-ray; 2.17 A; A/B/C/D=21-421.
DR   PDBsum; 5YQ5; -.
DR   AlphaFoldDB; Q99983; -.
DR   SMR; Q99983; -.
DR   BioGRID; 111011; 5.
DR   IntAct; Q99983; 5.
DR   STRING; 9606.ENSP00000364700; -.
DR   GlyConnect; 1588; 2 N-Linked glycans (1 site).
DR   GlyCosmos; Q99983; 5 sites, 2 glycans.
DR   GlyGen; Q99983; 5 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q99983; -.
DR   PhosphoSitePlus; Q99983; -.
DR   BioMuta; OMD; -.
DR   DMDM; 20138850; -.
DR   jPOST; Q99983; -.
DR   MassIVE; Q99983; -.
DR   PaxDb; 9606-ENSP00000364700; -.
DR   PeptideAtlas; Q99983; -.
DR   ProteomicsDB; 78561; -.
DR   Antibodypedia; 28259; 219 antibodies from 27 providers.
DR   DNASU; 4958; -.
DR   Ensembl; ENST00000375550.5; ENSP00000364700.4; ENSG00000127083.8.
DR   Ensembl; ENST00000707247.1; ENSP00000516806.1; ENSG00000291355.1.
DR   GeneID; 4958; -.
DR   KEGG; hsa:4958; -.
DR   MANE-Select; ENST00000375550.5; ENSP00000364700.4; NM_005014.3; NP_005005.1.
DR   UCSC; uc004asd.5; human.
DR   AGR; HGNC:8134; -.
DR   CTD; 4958; -.
DR   DisGeNET; 4958; -.
DR   GeneCards; OMD; -.
DR   HGNC; HGNC:8134; OMD.
DR   HPA; ENSG00000127083; Low tissue specificity.
DR   MIM; 618926; gene.
DR   neXtProt; NX_Q99983; -.
DR   OpenTargets; ENSG00000127083; -.
DR   PharmGKB; PA31921; -.
DR   VEuPathDB; HostDB:ENSG00000127083; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000160986; -.
DR   HOGENOM; CLU_000288_186_4_1; -.
DR   InParanoid; Q99983; -.
DR   OMA; YNIFNLS; -.
DR   OrthoDB; 521898at2759; -.
DR   PhylomeDB; Q99983; -.
DR   TreeFam; TF334562; -.
DR   PathwayCommons; Q99983; -.
DR   Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-HSA-2022857; Keratan sulfate degradation.
DR   Reactome; R-HSA-3656225; Defective CHST6 causes MCDC1.
DR   Reactome; R-HSA-3656243; Defective ST3GAL3 causes MCT12 and EIEE15.
DR   Reactome; R-HSA-3656244; Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
DR   SignaLink; Q99983; -.
DR   SIGNOR; Q99983; -.
DR   BioGRID-ORCS; 4958; 15 hits in 1112 CRISPR screens.
DR   ChiTaRS; OMD; human.
DR   GeneWiki; OMD_(gene); -.
DR   GenomeRNAi; 4958; -.
DR   Pharos; Q99983; Tbio.
DR   PRO; PR:Q99983; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q99983; Protein.
DR   Bgee; ENSG00000127083; Expressed in periodontal ligament and 146 other cell types or tissues.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   PANTHER; PTHR45712; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF3; OSTEOMODULIN; 1.
DR   Pfam; PF13855; LRR_8; 2.
DR   SMART; SM00364; LRR_BAC; 5.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 8.
DR   Genevisible; Q99983; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Leucine-rich repeat; Proteoglycan; Reference proteome;
KW   Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..421
FT                   /note="Osteomodulin"
FT                   /id="PRO_0000032754"
FT   DOMAIN          53..91
FT                   /note="LRRNT"
FT   REPEAT          92..113
FT                   /note="LRR 1"
FT   REPEAT          116..129
FT                   /note="LRR 2"
FT   REPEAT          142..164
FT                   /note="LRR 3"
FT   REPEAT          165..184
FT                   /note="LRR 4"
FT   REPEAT          187..210
FT                   /note="LRR 5"
FT   REPEAT          213..233
FT                   /note="LRR 6"
FT   REPEAT          234..255
FT                   /note="LRR 7"
FT   REPEAT          258..280
FT                   /note="LRR 8"
FT   REPEAT          281..294
FT                   /note="LRR 9"
FT   REPEAT          301..321
FT                   /note="LRR 10"
FT   REPEAT          331..353
FT                   /note="LRR 11"
FT   REGION          382..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         22
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         25
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         31
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         39
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   MOD_RES         51
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         58
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         77
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:14551184"
FT   MOD_RES         416
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   MOD_RES         417
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14551184"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        321..353
FT                   /evidence="ECO:0000250"
FT   VARIANT         200
FT                   /note="D -> G (in dbSNP:rs34069871)"
FT                   /id="VAR_052014"
FT   VARIANT         212
FT                   /note="E -> G (in dbSNP:rs34413259)"
FT                   /id="VAR_052015"
FT   VARIANT         221
FT                   /note="S -> N (in dbSNP:rs34860658)"
FT                   /id="VAR_052016"
FT   VARIANT         282
FT                   /note="I -> T (in dbSNP:rs35779901)"
FT                   /id="VAR_052017"
FT   VARIANT         353
FT                   /note="C -> W (in dbSNP:rs34059114)"
FT                   /id="VAR_052018"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   TURN            134..139
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   TURN            179..184
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   TURN            204..210
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   TURN            274..277
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          304..306
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   HELIX           317..320
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          334..336
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   HELIX           350..353
FT                   /evidence="ECO:0007829|PDB:5YQ5"
FT   STRAND          359..361
FT                   /evidence="ECO:0007829|PDB:5YQ5"
SQ   SEQUENCE   421 AA;  49492 MW;  CED47B2BC33BB872 CRC64;
     MGFLSPIYVI FFFFGVKVHC QYETYQWDED YDQEPDDDYQ TGFPFRQNVD YGVPFHQYTL
     GCVSECFCPT NFPSSMYCDN RKLKTIPNIP MHIQQLYLQF NEIEAVTANS FINATHLKEI
     NLSHNKIKSQ KIDYGVFAKL PNLLQLHLEH NNLEEFPFPL PKSLERLLLG YNEISKLQTN
     AMDGLVNLTM LDLCYNYLHD SLLKDKIFAK MEKLMQLNLC SNRLESMPPG LPSSLMYLSL
     ENNSISSIPE KYFDKLPKLH TLRMSHNKLQ DIPYNIFNLP NIVELSVGHN KLKQAFYIPR
     NLEHLYLQNN EIEKMNLTVM CPSIDPLHYH HLTYIRVDQN KLKEPISSYI FFCFPHIHTI
     YYGEQRSTNG QTIQLKTQVF RRFPDDDDES EDHDDPDNAH ESPEQEGAEG HFDLHYYENQ
     E
//