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P15306

- TRBM_MOUSE

UniProt

P15306 - TRBM_MOUSE

Protein

Thrombomodulin

Gene

Thbd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va and factor VIIIa, and thereby reduces the amount of thrombin generated.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. carbohydrate binding Source: InterPro
    3. transmembrane signaling receptor activity Source: InterPro

    GO - Biological processi

    1. blood coagulation Source: MGI
    2. female pregnancy Source: MGI
    3. negative regulation of coagulation Source: MGI
    4. response to cAMP Source: Ensembl
    5. response to lipopolysaccharide Source: Ensembl
    6. response to X-ray Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_225233. Cell surface interactions at the vascular wall.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thrombomodulin
    Short name:
    TM
    Alternative name(s):
    Fetomodulin
    CD_antigen: CD141
    Gene namesi
    Name:Thbd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:98736. Thbd.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. extracellular space Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 577561ThrombomodulinPRO_0000007772Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi113 – 1131N-linked (GlcNAc...)1 Publication
    Disulfide bondi135 ↔ 156By similarity
    Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi244 ↔ 255By similarity
    Disulfide bondi251 ↔ 264By similarity
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi266 ↔ 279By similarity
    Disulfide bondi287 ↔ 295By similarity
    Disulfide bondi291 ↔ 307By similarity
    Disulfide bondi309 ↔ 322By similarity
    Disulfide bondi328 ↔ 339By similarity
    Disulfide bondi335 ↔ 348By similarity
    Disulfide bondi350 ↔ 361By similarity
    Disulfide bondi368 ↔ 377By similarity
    Disulfide bondi373 ↔ 387By similarity
    Disulfide bondi389 ↔ 403By similarity
    Disulfide bondi407 ↔ 416By similarity
    Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi412 ↔ 424By similarity
    Disulfide bondi426 ↔ 438By similarity
    Disulfide bondi444 ↔ 454By similarity
    Disulfide bondi449 ↔ 463By similarity
    Disulfide bondi465 ↔ 479By similarity
    Glycosylationi494 – 4941O-linked (Xyl...) (glycosaminoglycan)By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP15306.
    PRIDEiP15306.

    PTM databases

    PhosphoSiteiP15306.

    Expressioni

    Tissue specificityi

    Endothelial cells are unique in synthesizing thrombomodulin.

    Gene expression databases

    ArrayExpressiP15306.
    BgeeiP15306.
    CleanExiMM_THBD.
    GenevestigatoriP15306.

    Interactioni

    Protein-protein interaction databases

    IntActiP15306. 1 interaction.
    MINTiMINT-4138449.

    Structurei

    3D structure databases

    ProteinModelPortaliP15306.
    SMRiP15306. Positions 22-168, 244-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 517501ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini542 – 57736CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei518 – 54124HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 167137C-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini240 – 28041EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 32341EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini324 – 36239EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 40441EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini403 – 43937EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini440 – 48041EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation
    Contains 6 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG147686.
    HOGENOMiHOG000114624.
    HOVERGENiHBG000291.
    InParanoidiP15306.
    KOiK03907.
    OMAiLCGPLCV.
    OrthoDBiEOG70ZZMW.
    PhylomeDBiP15306.
    TreeFamiTF330714.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR016316. CD93/CD141.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR001491. Thrombomodulin.
    IPR015149. Tme5_EGF-like.
    [Graphical view]
    PfamiPF07645. EGF_CA. 1 hit.
    PF00059. Lectin_C. 1 hit.
    PF09064. Tme5_EGF_like. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001775. CD93/CD141. 1 hit.
    PRINTSiPR00907. THRMBOMODULN.
    SMARTiSM00034. CLECT. 1 hit.
    SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    PS01186. EGF_2. 3 hits.
    PS50026. EGF_3. 3 hits.
    PS01187. EGF_CA. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P15306-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGIFFLGVL APASLGLSAL AKLQPTGSQC VEHECFALFQ GPATFLDASQ    50
    ACQRLQGHLM TVRSSVAADV ISLLLSQSSM DLGPWIGLQL PQGCDDPVHL 100
    GPLRGFQWVT GDNHTSYSRW ARPNDQTAPL CGPLCVTVST ATEAAPGEPA 150
    WEEKPCETET QGFLCEFYFT ASCRPLTVNT RDPEAAHISS TYNTPFGVSG 200
    ADFQTLPVGS SAAVEPLGLE LVCRAPPGTS EGHWAWEATG AWNCSVENGG 250
    CEYLCNRSTN EPRCLCPRDM DLQADGRSCA RPVVQSCNEL CEHFCVSNAE 300
    VPGSYSCMCE TGYQLAADGH RCEDVDDCKQ GPNPCPQLCV NTKGGFECFC 350
    YDGYELVDGE CVELLDPCFG SNCEFQCQPV SPTDYRCICA PGFAPKPDEP 400
    HKCEMFCNET SCPADCDPNS PTVCECPEGF ILDEGSVCTD IDECSQGECF 450
    TSECRNFPGS YECICGPDTA LAGQISKDCD PIPVREDTKE EEGSGEPPVS 500
    PTPGSPTGPP SARPVHSGVL IGISIASLSL VVALLALLCH LRKKQGAARA 550
    ELEYKCASSA KEVVLQHVRT DRTLQKF 577
    Length:577
    Mass (Da):61,868
    Last modified:April 1, 1990 - v1
    Checksum:iB20E50B0FE745014
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14432 mRNA. Translation: CAA32597.1.
    BC019154 mRNA. Translation: AAH19154.1.
    CCDSiCCDS16838.1.
    PIRiS08488. A60501.
    RefSeqiNP_033404.1. NM_009378.3.
    UniGeneiMm.24096.

    Genome annotation databases

    EnsembliENSMUST00000099270; ENSMUSP00000096877; ENSMUSG00000074743.
    GeneIDi21824.
    KEGGimmu:21824.
    UCSCiuc008mtd.2. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Thrombomodulin

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14432 mRNA. Translation: CAA32597.1 .
    BC019154 mRNA. Translation: AAH19154.1 .
    CCDSi CCDS16838.1.
    PIRi S08488. A60501.
    RefSeqi NP_033404.1. NM_009378.3.
    UniGenei Mm.24096.

    3D structure databases

    ProteinModelPortali P15306.
    SMRi P15306. Positions 22-168, 244-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P15306. 1 interaction.
    MINTi MINT-4138449.

    PTM databases

    PhosphoSitei P15306.

    Proteomic databases

    PaxDbi P15306.
    PRIDEi P15306.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000099270 ; ENSMUSP00000096877 ; ENSMUSG00000074743 .
    GeneIDi 21824.
    KEGGi mmu:21824.
    UCSCi uc008mtd.2. mouse.

    Organism-specific databases

    CTDi 7056.
    MGIi MGI:98736. Thbd.

    Phylogenomic databases

    eggNOGi NOG147686.
    HOGENOMi HOG000114624.
    HOVERGENi HBG000291.
    InParanoidi P15306.
    KOi K03907.
    OMAi LCGPLCV.
    OrthoDBi EOG70ZZMW.
    PhylomeDBi P15306.
    TreeFami TF330714.

    Enzyme and pathway databases

    Reactomei REACT_225233. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    NextBioi 301248.
    PROi P15306.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15306.
    Bgeei P15306.
    CleanExi MM_THBD.
    Genevestigatori P15306.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR016316. CD93/CD141.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR001491. Thrombomodulin.
    IPR015149. Tme5_EGF-like.
    [Graphical view ]
    Pfami PF07645. EGF_CA. 1 hit.
    PF00059. Lectin_C. 1 hit.
    PF09064. Tme5_EGF_like. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001775. CD93/CD141. 1 hit.
    PRINTSi PR00907. THRMBOMODULN.
    SMARTi SM00034. CLECT. 1 hit.
    SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    PS01186. EGF_2. 3 hits.
    PS50026. EGF_3. 3 hits.
    PS01187. EGF_CA. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a cDNA for mouse thrombomodulin and comparison of the predicted mouse and human amino acid sequences."
      Dittman W.A., Majerus P.W.
      Nucleic Acids Res. 17:802-802(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The structure and function of mouse thrombomodulin. Phorbol myristate acetate stimulates degradation and synthesis of thrombomodulin without affecting mRNA levels in hemangioma cells."
      Dittman W.A., Kumada T., Sadler J.E., Majerus P.W.
      J. Biol. Chem. 263:15815-15822(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary gland.
    4. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113.
      Tissue: Myoblast.

    Entry informationi

    Entry nameiTRBM_MOUSE
    AccessioniPrimary (citable) accession number: P15306
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 140 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

    External Data

    Dasty 3