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P50609 (FMOD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Fibromodulin

Short name=FM
Alternative name(s):
Collagen-binding 59 kDa protein
Keratan sulfate proteoglycan fibromodulin
Short name=KSPG fibromodulin
Gene names
Name:Fmod
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis By similarity.

Subunit structure

Binds to type I and type II collagen By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

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 – 1818 By similarity
Chain19 – 376358Fibromodulin
PRO_0000032741

Regions

Domain67 – 10539LRRNT
Repeat106 – 12722LRR 1
Repeat130 – 14314LRR 2
Repeat156 – 17621LRR 3
Repeat177 – 19822LRR 4
Repeat201 – 22222LRR 5
Repeat224 – 24522LRR 6
Repeat246 – 26621LRR 7
Repeat269 – 28921LRR 8
Repeat294 – 31522LRR 9
Repeat316 – 33520LRR 10
Repeat344 – 36724LRR 11
Compositional bias68 – 736Poly-Pro
Compositional bias76 – 9217Cys-rich

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid By similarity
Modified residue201Sulfotyrosine By similarity
Modified residue381Sulfotyrosine By similarity
Modified residue531Sulfotyrosine By similarity
Modified residue551Sulfotyrosine By similarity
Modified residue631Sulfotyrosine By similarity
Modified residue651Sulfotyrosine By similarity
Glycosylation1271N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation1661N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation2011N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation2911N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation3411N-linked (GlcNAc...) Potential
Disulfide bond334 ↔ 367 By similarity

Sequences

Sequence LengthMass (Da)Tools
P50609 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9C3298675CE3714A

FASTA37643,219
        10         20         30         40         50         60 
MQWASILLLR GLCSLSQGQY EEDSHWWLQY LRNQQSTYYD PYDTYPYETS DPYPYEVEEG 

        70         80         90        100        110        120 
PAYAYGAPPP PEPRDCPQEC DCPPNFPTAM YCDNRNLKYL PFVPSRMKYV YFQNNQIAAI 

       130        140        150        160        170        180 
QEGVFDNATG LLWIALHGNQ ITSDKIGRKV FSKLRHLERL YLDHNNLTRM PGPLPRSLRE 

       190        200        210        220        230        240 
LHLDHNQISR VPNNALEGLE NLTALYLHHN EIQEVGSSMR GLRSLILLDL SYNHLRRVPD 

       250        260        270        280        290        300 
GLPSALEQLY LEHNNVYTVP DSYFRGSPKL LYVRLSHNSL TNNGLATNTF NSSSLLELDL 

       310        320        330        340        350        360 
SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVM NFSKLQVLRL DGNEIKRSAM 

       370 
PVDAPLCLRL ASLIEI 

« Hide

References

[1]Krull N.
Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82152 mRNA. Translation: CAA57648.1.
RefSeqNP_542429.1. NM_080698.1.
UniGeneRn.8778.

3D structure databases

ProteinModelPortalP50609.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000004382.

Proteomic databases

PaxDbP50609.
PRIDEP50609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64507.
KEGGrno:64507.
UCSCRGD:619769. rat.

Organism-specific databases

CTD2331.
RGD619769. Fmod.

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000234447.
HOVERGENHBG108061.
InParanoidP50609.
KOK08121.
PhylomeDBP50609.

Gene expression databases

GenevestigatorP50609.

Family and domain databases

InterProIPR027215. Fibromodulin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PANTHERPTHR24371:SF11. PTHR24371:SF11. 1 hit.
PfamPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio613278.
PROP50609.

Entry information

Entry nameFMOD_RAT
AccessionPrimary (citable) accession number: P50609
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families