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Protein

Fibromodulin

Gene

Fmod

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-2022857. Keratan sulfate degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibromodulin
Short name:
FM
Alternative name(s):
Collagen-binding 59 kDa protein
Keratan sulfate proteoglycan fibromodulin
Short name:
KSPG fibromodulin
Gene namesi
Name:Fmod
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1328364. Fmod.

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 – 18By similarityAdd BLAST18
ChainiPRO_000003274019 – 376FibromodulinAdd BLAST358

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Pyrrolidone carboxylic acidBy similarity1
Modified residuei20SulfotyrosineBy similarity1
Modified residuei38SulfotyrosineBy similarity1
Modified residuei53SulfotyrosineBy similarity1
Modified residuei55SulfotyrosineBy similarity1
Modified residuei63SulfotyrosineBy similarity1
Modified residuei65SulfotyrosineBy similarity1
Glycosylationi127N-linked (GlcNAc...) (keratan sulfate)By similarity1
Glycosylationi166N-linked (GlcNAc...) (keratan sulfate)By similarity1
Glycosylationi201N-linked (GlcNAc...) (keratan sulfate)By similarity1
Glycosylationi291N-linked (GlcNAc...) (keratan sulfate)By similarity1
Disulfide bondi334 ↔ 367By similarity
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Binds keratan sulfate chains.By similarity
Sulfated on tyrosine residue(s).Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiP50608.
PeptideAtlasiP50608.
PRIDEiP50608.

PTM databases

iPTMnetiP50608.
PhosphoSitePlusiP50608.

Expressioni

Tissue specificityi

Highest levels observed in knee epiphysis, in calvarial and diaphyseal bone, in nasal and costal cartilage, in the eye, and in bladder. In mature knee joint it is mostly present in the proliferating zone of growth plate. It is also observed in ligaments, especially at insertion sites, in the junction between meniscus and joint capsule, in the perimysium of skeletal muscle and in the periosteum.

Developmental stagei

Highest levels between 5 days and 1 month of age. Thereafter, the expression of declined to a level of approx. 35% of maximum, and remained constant throughout the rest of the observation period.

Gene expression databases

BgeeiENSMUSG00000041559.
CleanExiMM_FMOD.
ExpressionAtlasiP50608. baseline and differential.
GenevisibleiP50608. MM.

Interactioni

Subunit structurei

Binds to type I and type II collagen.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035489.

Structurei

3D structure databases

ProteinModelPortaliP50608.
SMRiP50608.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini67 – 105LRRNTAdd BLAST39
Repeati106 – 127LRR 1Add BLAST22
Repeati130 – 151LRR 2Add BLAST22
Repeati156 – 176LRR 3Add BLAST21
Repeati177 – 198LRR 4Add BLAST22
Repeati201 – 222LRR 5Add BLAST22
Repeati224 – 245LRR 6Add BLAST22
Repeati246 – 266LRR 7Add BLAST21
Repeati269 – 289LRR 8Add BLAST21
Repeati294 – 315LRR 9Add BLAST22
Repeati316 – 335LRR 10Add BLAST20
Repeati344 – 367LRR 11Add BLAST24

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi68 – 73Poly-Pro6
Compositional biasi76 – 92Cys-richAdd BLAST17

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.
GeneTreeiENSGT00760000118969.
HOVERGENiHBG108061.
InParanoidiP50608.
KOiK08121.
OMAiDEDPHWW.
OrthoDBiEOG091G0A3V.
PhylomeDBiP50608.
TreeFamiTF334562.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR027215. Fibromodulin.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24373:SF127. PTHR24373:SF127. 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. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50608-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQWASVLLLA GLCSLSQGQY DEDSHWWIQY LRNQQSTYYD PYDPYPYEPS
60 70 80 90 100
EPYPYGVEEG PAYAYGAPPP PEPRDCPQEC DCPPNFPTAM YCDNRNLKYL
110 120 130 140 150
PFVPSRMKYV YFQNNQISAI QEGVFDNATG LLWVALHGNQ ITSDKVGRKV
160 170 180 190 200
FSKLRHLERL YLDHNNLTRM PGPLPRSLRE LHLDHNQISR VPNNALEGLE
210 220 230 240 250
NLTALYLHHN EIQEVGSSMR GLRSLILLDL SYNHLRRVPD GLPSALEQLY
260 270 280 290 300
LEHNNVYTVP DSYFRGSPKL LYVRLSHNSL TNNGLATNTF NSSSLLELDL
310 320 330 340 350
SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVM NFSKLQVLRL
360 370
DGNEIKRSAM PVDAPLCLRL ANLIEI
Length:376
Mass (Da):43,055
Last modified:October 1, 1996 - v1
Checksum:i45A9EDDB0BADA85B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94998 mRNA. Translation: CAA64454.1.
BC064779 mRNA. Translation: AAH64779.1.
CCDSiCCDS15301.1.
RefSeqiNP_067330.1. NM_021355.3.
UniGeneiMm.287146.

Genome annotation databases

EnsembliENSMUST00000048183; ENSMUSP00000035489; ENSMUSG00000041559.
GeneIDi14264.
KEGGimmu:14264.
UCSCiuc007crd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94998 mRNA. Translation: CAA64454.1.
BC064779 mRNA. Translation: AAH64779.1.
CCDSiCCDS15301.1.
RefSeqiNP_067330.1. NM_021355.3.
UniGeneiMm.287146.

3D structure databases

ProteinModelPortaliP50608.
SMRiP50608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035489.

PTM databases

iPTMnetiP50608.
PhosphoSitePlusiP50608.

Proteomic databases

PaxDbiP50608.
PeptideAtlasiP50608.
PRIDEiP50608.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048183; ENSMUSP00000035489; ENSMUSG00000041559.
GeneIDi14264.
KEGGimmu:14264.
UCSCiuc007crd.1. mouse.

Organism-specific databases

CTDi2331.
MGIiMGI:1328364. Fmod.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118969.
HOVERGENiHBG108061.
InParanoidiP50608.
KOiK08121.
OMAiDEDPHWW.
OrthoDBiEOG091G0A3V.
PhylomeDBiP50608.
TreeFamiTF334562.

Enzyme and pathway databases

ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-2022857. Keratan sulfate degradation.

Miscellaneous databases

PROiP50608.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000041559.
CleanExiMM_FMOD.
ExpressionAtlasiP50608. baseline and differential.
GenevisibleiP50608. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR027215. Fibromodulin.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PANTHERiPTHR24373:SF127. PTHR24373:SF127. 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. 9 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFMOD_MOUSE
AccessioniPrimary (citable) accession number: P50608
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 126 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.