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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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 376358FibromodulinPRO_0000032740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acidBy similarity
Modified residuei20 – 201SulfotyrosineBy similarity
Modified residuei38 – 381SulfotyrosineBy similarity
Modified residuei53 – 531SulfotyrosineBy similarity
Modified residuei55 – 551SulfotyrosineBy similarity
Modified residuei63 – 631SulfotyrosineBy similarity
Modified residuei65 – 651SulfotyrosineBy similarity
Glycosylationi127 – 1271N-linked (GlcNAc...) (keratan sulfate)By similarity
Glycosylationi166 – 1661N-linked (GlcNAc...) (keratan sulfate)By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...) (keratan sulfate)By similarity
Glycosylationi291 – 2911N-linked (GlcNAc...) (keratan sulfate)By similarity
Disulfide bondi334 ↔ 367By similarity
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence analysis

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.
PhosphoSiteiP50608.

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. Positions 76-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 10539LRRNTAdd
BLAST
Repeati106 – 12722LRR 1Add
BLAST
Repeati130 – 15122LRR 2Add
BLAST
Repeati156 – 17621LRR 3Add
BLAST
Repeati177 – 19822LRR 4Add
BLAST
Repeati201 – 22222LRR 5Add
BLAST
Repeati224 – 24522LRR 6Add
BLAST
Repeati246 – 26621LRR 7Add
BLAST
Repeati269 – 28921LRR 8Add
BLAST
Repeati294 – 31522LRR 9Add
BLAST
Repeati316 – 33520LRR 10Add
BLAST
Repeati344 – 36724LRR 11Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 736Poly-Pro
Compositional biasi76 – 9217Cys-richAdd
BLAST

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.
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. Positions 76-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000035489.

PTM databases

iPTMnetiP50608.
PhosphoSiteiP50608.

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.
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: September 7, 2016
This is version 124 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.