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Protein

Thrombomodulin

Gene

Thbd

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

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

GO - Biological processi

  • blood coagulation Source: MGI
  • female pregnancy Source: MGI
  • negative regulation of blood coagulation Source: InterPro
  • negative regulation of coagulation Source: MGI
  • response to cAMP Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • response to X-ray Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_278886. Cell surface interactions at the vascular wall.
REACT_286713. Common Pathway of Fibrin Clot Formation.

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 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:98736. Thbd.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 517501ExtracellularSequence AnalysisAdd
BLAST
Transmembranei518 – 54124HelicalSequence AnalysisAdd
BLAST
Topological domaini542 – 57736CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • extracellular space Source: Ensembl
  • integral component of plasma membrane Source: InterPro
  • plasma membrane Source: MGI
Complete GO annotation...

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

MaxQBiP15306.
PaxDbiP15306.
PRIDEiP15306.

PTM databases

PhosphoSiteiP15306.

Expressioni

Tissue specificityi

Endothelial cells are unique in synthesizing thrombomodulin.

Gene expression databases

BgeeiP15306.
CleanExiMM_THBD.
ExpressionAtlasiP15306. baseline and differential.
GenevisibleiP15306. MM.

Interactioni

Protein-protein interaction databases

IntActiP15306. 1 interaction.
MINTiMINT-4138449.
STRINGi10090.ENSMUSP00000096877.

Structurei

3D structure databases

ProteinModelPortaliP15306.
SMRiP15306. Positions 244-479.
ModBaseiSearch...
MobiDBiSearch...

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. 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.
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.
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

        10         20         30         40         50
MLGIFFLGVL APASLGLSAL AKLQPTGSQC VEHECFALFQ GPATFLDASQ
60 70 80 90 100
ACQRLQGHLM TVRSSVAADV ISLLLSQSSM DLGPWIGLQL PQGCDDPVHL
110 120 130 140 150
GPLRGFQWVT GDNHTSYSRW ARPNDQTAPL CGPLCVTVST ATEAAPGEPA
160 170 180 190 200
WEEKPCETET QGFLCEFYFT ASCRPLTVNT RDPEAAHISS TYNTPFGVSG
210 220 230 240 250
ADFQTLPVGS SAAVEPLGLE LVCRAPPGTS EGHWAWEATG AWNCSVENGG
260 270 280 290 300
CEYLCNRSTN EPRCLCPRDM DLQADGRSCA RPVVQSCNEL CEHFCVSNAE
310 320 330 340 350
VPGSYSCMCE TGYQLAADGH RCEDVDDCKQ GPNPCPQLCV NTKGGFECFC
360 370 380 390 400
YDGYELVDGE CVELLDPCFG SNCEFQCQPV SPTDYRCICA PGFAPKPDEP
410 420 430 440 450
HKCEMFCNET SCPADCDPNS PTVCECPEGF ILDEGSVCTD IDECSQGECF
460 470 480 490 500
TSECRNFPGS YECICGPDTA LAGQISKDCD PIPVREDTKE EEGSGEPPVS
510 520 530 540 550
PTPGSPTGPP SARPVHSGVL IGISIASLSL VVALLALLCH LRKKQGAARA
560 570
ELEYKCASSA KEVVLQHVRT DRTLQKF
Length:577
Mass (Da):61,868
Last modified:April 1, 1990 - v1
Checksum:iB20E50B0FE745014
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X14432 mRNA. Translation: CAA32597.1.
BC019154 mRNA. Translation: AAH19154.1.
CCDSiCCDS16838.1.
PIRiS08488. A60501.
RefSeqiNP_033404.1. NM_009378.3.
UniGeneiMm.24096.

3D structure databases

ProteinModelPortaliP15306.
SMRiP15306. Positions 244-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15306. 1 interaction.
MINTiMINT-4138449.
STRINGi10090.ENSMUSP00000096877.

PTM databases

PhosphoSiteiP15306.

Proteomic databases

MaxQBiP15306.
PaxDbiP15306.
PRIDEiP15306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7056.
MGIiMGI:98736. Thbd.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_278886. Cell surface interactions at the vascular wall.
REACT_286713. Common Pathway of Fibrin Clot Formation.

Miscellaneous databases

NextBioi301248.
PROiP15306.
SOURCEiSearch...

Gene expression databases

BgeeiP15306.
CleanExiMM_THBD.
ExpressionAtlasiP15306. baseline and differential.
GenevisibleiP15306. MM.

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. 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.
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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 148 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

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 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.