Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P50609

- FMOD_RAT

UniProt

P50609 - FMOD_RAT

Protein

Fibromodulin

Gene

Fmod

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    GO - Biological processi

    1. odontogenesis Source: RGD
    2. wound healing Source: RGD

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi619769. Fmod.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: RGD
    2. extracellular region Source: RGD
    3. intracellular Source: RGD
    4. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 376358FibromodulinPRO_0000032741Add
    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

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP50609.
    PRIDEiP50609.

    Expressioni

    Gene expression databases

    GenevestigatoriP50609.

    Interactioni

    Subunit structurei

    Binds to type I and type II collagen.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000004382.

    Structurei

    3D structure databases

    ProteinModelPortaliP50609.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini67 – 10539LRRNTAdd
    BLAST
    Repeati106 – 12722LRR 1Add
    BLAST
    Repeati130 – 14314LRR 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

    eggNOGiCOG4886.
    HOGENOMiHOG000234447.
    HOVERGENiHBG108061.
    InParanoidiP50609.
    KOiK08121.
    PhylomeDBiP50609.

    Family and domain databases

    InterProiIPR027215. Fibromodulin.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PANTHERiPTHR24371:SF11. PTHR24371:SF11. 1 hit.
    PfamiPF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 9 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P50609-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQWASILLLR GLCSLSQGQY EEDSHWWLQY LRNQQSTYYD PYDTYPYETS    50
    DPYPYEVEEG PAYAYGAPPP PEPRDCPQEC DCPPNFPTAM YCDNRNLKYL 100
    PFVPSRMKYV YFQNNQIAAI QEGVFDNATG LLWIALHGNQ ITSDKIGRKV 150
    FSKLRHLERL YLDHNNLTRM PGPLPRSLRE LHLDHNQISR VPNNALEGLE 200
    NLTALYLHHN EIQEVGSSMR GLRSLILLDL SYNHLRRVPD GLPSALEQLY 250
    LEHNNVYTVP DSYFRGSPKL LYVRLSHNSL TNNGLATNTF NSSSLLELDL 300
    SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVM NFSKLQVLRL 350
    DGNEIKRSAM PVDAPLCLRL ASLIEI 376
    Length:376
    Mass (Da):43,219
    Last modified:October 1, 1996 - v1
    Checksum:i9C3298675CE3714A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82152 mRNA. Translation: CAA57648.1.
    RefSeqiNP_542429.1. NM_080698.1.
    UniGeneiRn.8778.

    Genome annotation databases

    GeneIDi64507.
    KEGGirno:64507.
    UCSCiRGD:619769. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82152 mRNA. Translation: CAA57648.1 .
    RefSeqi NP_542429.1. NM_080698.1.
    UniGenei Rn.8778.

    3D structure databases

    ProteinModelPortali P50609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000004382.

    Proteomic databases

    PaxDbi P50609.
    PRIDEi P50609.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64507.
    KEGGi rno:64507.
    UCSCi RGD:619769. rat.

    Organism-specific databases

    CTDi 2331.
    RGDi 619769. Fmod.

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000234447.
    HOVERGENi HBG108061.
    InParanoidi P50609.
    KOi K08121.
    PhylomeDBi P50609.

    Miscellaneous databases

    NextBioi 613278.
    PROi P50609.

    Gene expression databases

    Genevestigatori P50609.

    Family and domain databases

    InterProi IPR027215. Fibromodulin.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    PANTHERi PTHR24371:SF11. PTHR24371:SF11. 1 hit.
    Pfami PF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiFMOD_RAT
    AccessioniPrimary (citable) accession number: P50609
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 91 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3