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P15306 (TRBM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thrombomodulin

Short name=TM
Alternative name(s):
Fetomodulin
CD_antigen=CD141
Gene names
Name:Thbd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Endothelial cells are unique in synthesizing thrombomodulin.

Sequence similarities

Contains 1 C-type lectin domain.

Contains 6 EGF-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 577561Thrombomodulin
PRO_0000007772

Regions

Topological domain17 – 517501Extracellular Potential
Transmembrane518 – 54124Helical; Potential
Topological domain542 – 57736Cytoplasmic Potential
Domain31 – 167137C-type lectin
Domain240 – 28041EGF-like 1
Domain283 – 32341EGF-like 2
Domain324 – 36239EGF-like 3; calcium-binding Potential
Domain364 – 40441EGF-like 4
Domain403 – 43937EGF-like 5
Domain440 – 48041EGF-like 6; calcium-binding Potential

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Ref.4
Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Potential
Glycosylation4941O-linked (Xyl...) (glycosaminoglycan) By similarity
Disulfide bond135 ↔ 156 By similarity
Disulfide bond244 ↔ 255 By similarity
Disulfide bond251 ↔ 264 By similarity
Disulfide bond266 ↔ 279 By similarity
Disulfide bond287 ↔ 295 By similarity
Disulfide bond291 ↔ 307 By similarity
Disulfide bond309 ↔ 322 By similarity
Disulfide bond328 ↔ 339 By similarity
Disulfide bond335 ↔ 348 By similarity
Disulfide bond350 ↔ 361 By similarity
Disulfide bond368 ↔ 377 By similarity
Disulfide bond373 ↔ 387 By similarity
Disulfide bond389 ↔ 403 By similarity
Disulfide bond407 ↔ 416 By similarity
Disulfide bond412 ↔ 424 By similarity
Disulfide bond426 ↔ 438 By similarity
Disulfide bond444 ↔ 454 By similarity
Disulfide bond449 ↔ 463 By similarity
Disulfide bond465 ↔ 479 By similarity

Sequences

Sequence LengthMass (Da)Tools
P15306 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: B20E50B0FE745014

FASTA57761,868
        10         20         30         40         50         60 
MLGIFFLGVL APASLGLSAL AKLQPTGSQC VEHECFALFQ GPATFLDASQ ACQRLQGHLM 

        70         80         90        100        110        120 
TVRSSVAADV ISLLLSQSSM DLGPWIGLQL PQGCDDPVHL GPLRGFQWVT GDNHTSYSRW 

       130        140        150        160        170        180 
ARPNDQTAPL CGPLCVTVST ATEAAPGEPA WEEKPCETET QGFLCEFYFT ASCRPLTVNT 

       190        200        210        220        230        240 
RDPEAAHISS TYNTPFGVSG ADFQTLPVGS SAAVEPLGLE LVCRAPPGTS EGHWAWEATG 

       250        260        270        280        290        300 
AWNCSVENGG CEYLCNRSTN EPRCLCPRDM DLQADGRSCA RPVVQSCNEL CEHFCVSNAE 

       310        320        330        340        350        360 
VPGSYSCMCE TGYQLAADGH RCEDVDDCKQ GPNPCPQLCV NTKGGFECFC YDGYELVDGE 

       370        380        390        400        410        420 
CVELLDPCFG SNCEFQCQPV SPTDYRCICA PGFAPKPDEP HKCEMFCNET SCPADCDPNS 

       430        440        450        460        470        480 
PTVCECPEGF ILDEGSVCTD IDECSQGECF TSECRNFPGS YECICGPDTA LAGQISKDCD 

       490        500        510        520        530        540 
PIPVREDTKE EEGSGEPPVS PTPGSPTGPP SARPVHSGVL IGISIASLSL VVALLALLCH 

       550        560        570 
LRKKQGAARA ELEYKCASSA KEVVLQHVRT DRTLQKF 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14432 mRNA. Translation: CAA32597.1.
BC019154 mRNA. Translation: AAH19154.1.
CCDSCCDS16838.1.
PIRA60501. S08488.
RefSeqNP_033404.1. NM_009378.3.
UniGeneMm.24096.

3D structure databases

ProteinModelPortalP15306.
SMRP15306. Positions 22-168, 244-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15306. 1 interaction.
MINTMINT-4138449.

PTM databases

PhosphoSiteP15306.

Proteomic databases

PaxDbP15306.
PRIDEP15306.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099270; ENSMUSP00000096877; ENSMUSG00000074743.
GeneID21824.
KEGGmmu:21824.
UCSCuc008mtd.2. mouse.

Organism-specific databases

CTD7056.
MGIMGI:98736. Thbd.

Phylogenomic databases

eggNOGNOG147686.
HOGENOMHOG000114624.
HOVERGENHBG000291.
InParanoidP15306.
KOK03907.
OMALCGPLCV.
OrthoDBEOG70ZZMW.
PhylomeDBP15306.
TreeFamTF330714.

Gene expression databases

ArrayExpressP15306.
BgeeP15306.
CleanExMM_THBD.
GenevestigatorP15306.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. 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]
PfamPF07645. EGF_CA. 1 hit.
PF00059. Lectin_C. 1 hit.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFPIRSF001775. CD93/CD141. 1 hit.
PRINTSPR00907. THRMBOMODULN.
SMARTSM00034. CLECT. 1 hit.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

NextBio301248.
PROP15306.
SOURCESearch...

Entry information

Entry nameTRBM_MOUSE
AccessionPrimary (citable) accession number: P15306
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot