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Protein

Thrombomodulin

Gene

THBD

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Blood coagulation, Hemostasis

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombomodulin
Short name:
TM
Alternative name(s):
CD_antigen: CD141
Gene namesi
Name:THBD
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 518502ExtracellularSequence analysisAdd
BLAST
Transmembranei519 – 53921HelicalSequence analysisAdd
BLAST
Topological domaini540 – 57839CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 578562ThrombomodulinPRO_0000007770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Disulfide bondi137 ↔ 158By similarity
Disulfide bondi246 ↔ 257By similarity
Disulfide bondi253 ↔ 266By similarity
Disulfide bondi268 ↔ 281By similarity
Disulfide bondi289 ↔ 297By similarity
Disulfide bondi293 ↔ 309By similarity
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Disulfide bondi311 ↔ 324By similarity
Disulfide bondi330 ↔ 341By similarity
Disulfide bondi337 ↔ 350By similarity
Modified residuei343 – 3431(3R)-3-hydroxyasparagineBy similarity
Disulfide bondi352 ↔ 363By similarity
Disulfide bondi370 ↔ 379By similarity
Disulfide bondi375 ↔ 389By similarity
Disulfide bondi391 ↔ 405By similarity
Disulfide bondi409 ↔ 414By similarity
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi418 ↔ 426By similarity
Disulfide bondi428 ↔ 440By similarity
Disulfide bondi446 ↔ 455By similarity
Disulfide bondi451 ↔ 464By similarity
Disulfide bondi466 ↔ 480By similarity
Glycosylationi493 – 4931O-linked (Xyl...) (glycosaminoglycan)By similarity
Glycosylationi495 – 4951O-linked (Xyl...) (glycosaminoglycan)By similarity

Post-translational modificationi

N-glycosylated.By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ5W7P8.

Expressioni

Tissue specificityi

Expressed in lung, liver, spleen, kidney, pancreas and lymph node. Low expression in heart, cerebrum, urinary bladder and uterus.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000007702.

Structurei

3D structure databases

ProteinModelPortaliQ5W7P8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 167137C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini242 – 28241EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini285 – 32541EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini326 – 36439EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini366 – 40641EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini405 – 44137EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini442 – 48140EGF-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

eggNOGiENOG410IF0T. Eukaryota.
ENOG410Y5JS. LUCA.
HOGENOMiHOG000114624.
HOVERGENiHBG000291.
InParanoidiQ5W7P8.
KOiK03907.

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.
IPR001881. EGF-like_Ca-bd_dom.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR015149. Tme5_EGF-like.
[Graphical view]
PfamiPF07645. EGF_CA. 2 hits.
PF00059. Lectin_C. 1 hit.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFiPIRSF001775. CD93/CD141. 1 hit.
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 4 hits.
[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.

Q5W7P8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRVLLLGVL APAGLGLPTP AQPQPRSSQC MEHDCFQLFR GPATFLAASQ
60 70 80 90 100
TCEGLGGHLM TVRSSVAADV ISLLLSGDGG DGPRLWIGLQ LRRGCSDPGQ
110 120 130 140 150
GGPLRGFQWV TGDNRTSYSR WARPHVGPAG PPCAPLCVAV SDAAAPAPGE
160 170 180 190 200
PAWEEQRCAA EADGFLCEFH FAASCRPLLV DARAAAAAGV SVTYSTPFGA
210 220 230 240 250
RGADFQALPA GSSAAVAPFG VQLACAAPRG EAEARWGREA PGAWDCSVEN
260 270 280 290 300
GGCQRACSAS AGAPRCLCPA DTYLQADGRS CATFAEHSCH KLCEHFCIPN
310 320 330 340 350
ASVPGSYLCM CETGYQLAAD QHRCEDVDDC IQVPSLCPQL CVNTRGAFEC
360 370 380 390 400
HCYPGYELVD NECVEPVDPC FGSKCEYQCQ PVSQTDYRCI CAEGFAPVPH
410 420 430 440 450
DPHRCQMFCN QTACPADCDP NSPTSCQCPE GYILDDGFMC TDIDECENGE
460 470 480 490 500
CPEACRNLPG TYECICGPDS PLAGQVATDC GRIISDPDGD SDSGSGEPPV
510 520 530 540 550
TPTPGVTPSP SPVGPVHSGV LIGISIASLS LVVALLALLC HLRKKQGAPR
560 570
AELEYKCGAP AKEVVLQHVR TEQMPQKL
Length:578
Mass (Da):60,745
Last modified:December 7, 2004 - v1
Checksum:i06D255C9BBFCC883
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB193481 mRNA. Translation: BAD66823.1.
RefSeqiNP_001006954.1. NM_001006953.2.
UniGeneiCfa.16238.

Genome annotation databases

GeneIDi474355.
KEGGicfa:474355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB193481 mRNA. Translation: BAD66823.1.
RefSeqiNP_001006954.1. NM_001006953.2.
UniGeneiCfa.16238.

3D structure databases

ProteinModelPortaliQ5W7P8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000007702.

Proteomic databases

PaxDbiQ5W7P8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi474355.
KEGGicfa:474355.

Organism-specific databases

CTDi7056.

Phylogenomic databases

eggNOGiENOG410IF0T. Eukaryota.
ENOG410Y5JS. LUCA.
HOGENOMiHOG000114624.
HOVERGENiHBG000291.
InParanoidiQ5W7P8.
KOiK03907.

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.
IPR001881. EGF-like_Ca-bd_dom.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR015149. Tme5_EGF-like.
[Graphical view]
PfamiPF07645. EGF_CA. 2 hits.
PF00059. Lectin_C. 1 hit.
PF09064. Tme5_EGF_like. 1 hit.
[Graphical view]
PIRSFiPIRSF001775. CD93/CD141. 1 hit.
SMARTiSM00034. CLECT. 1 hit.
SM00181. EGF. 6 hits.
SM00179. EGF_CA. 4 hits.
[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

  1. "Molecular cloning of canine thrombomodulin cDNA and expression in normal tissues."
    Maruyama H., Oguma K., Maeda S., Kano R., Tsujimoto H., Watari T., Tokuriki M., Hasegawa A.
    J. Vet. Med. Sci. 66:1423-1427(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Entry informationi

Entry nameiTRBM_CANLF
AccessioniPrimary (citable) accession number: Q5W7P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 7, 2004
Last modified: June 8, 2016
This is version 88 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

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 one 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.