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P15306

- TRBM_MOUSE

UniProt

P15306 - TRBM_MOUSE

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Protein
Thrombomodulin
Gene
Thbd
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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

GO - Biological processi

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

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 517501Extracellular Reviewed prediction
Add
BLAST
Transmembranei518 – 54124Helical; Reviewed prediction
Add
BLAST
Topological domaini542 – 57736Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Chaini17 – 577561Thrombomodulin
PRO_0000007772Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 167137C-type lectin
Add
BLAST
Domaini240 – 28041EGF-like 1
Add
BLAST
Domaini283 – 32341EGF-like 2
Add
BLAST
Domaini324 – 36239EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini364 – 40441EGF-like 4
Add
BLAST
Domaini403 – 43937EGF-like 5
Add
BLAST
Domaini440 – 48041EGF-like 6; calcium-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 6 EGF-like domains.

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...

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

« 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: September 3, 2014
This is version 139 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