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Database: UniProt
Entry: P15306
LinkDB: P15306
Original site: P15306 
ID   TRBM_MOUSE              Reviewed;         577 AA.
AC   P15306;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   13-FEB-2019, entry version 175.
DE   RecName: Full=Thrombomodulin;
DE            Short=TM;
DE   AltName: Full=Fetomodulin;
DE   AltName: CD_antigen=CD141;
DE   Flags: Precursor;
GN   Name=Thbd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2536925; DOI=10.1093/nar/17.2.802;
RA   Dittman W.A., Majerus P.W.;
RT   "Sequence of a cDNA for mouse thrombomodulin and comparison of the
RT   predicted mouse and human amino acid sequences.";
RL   Nucleic Acids Res. 17:802-802(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2844823;
RA   Dittman W.A., Kumada T., Sadler J.E., Majerus P.W.;
RT   "The structure and function of mouse thrombomodulin. Phorbol myristate
RT   acetate stimulates degradation and synthesis of thrombomodulin without
RT   affecting mRNA levels in hemangioma cells.";
RL   J. Biol. Chem. 263:15815-15822(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Thrombomodulin is a specific endothelial cell receptor
CC       that forms a 1:1 stoichiometric complex with thrombin. This
CC       complex is responsible for the conversion of protein C to the
CC       activated protein C (protein Ca). Once evolved, protein Ca
CC       scissions the activated cofactors of the coagulation mechanism,
CC       factor Va and factor VIIIa, and thereby reduces the amount of
CC       thrombin generated.
CC   -!- SUBUNIT: Interacts with ITGAL, ITGAM and ITGB2.
CC       {ECO:0000250|UniProtKB:P07204}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Endothelial cells are unique in synthesizing
CC       thrombomodulin.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Thrombomodulin;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_154";
DR   EMBL; X14432; CAA32597.1; -; mRNA.
DR   EMBL; BC019154; AAH19154.1; -; mRNA.
DR   CCDS; CCDS16838.1; -.
DR   PIR; S08488; A60501.
DR   RefSeq; NP_033404.1; NM_009378.3.
DR   UniGene; Mm.24096; -.
DR   ProteinModelPortal; P15306; -.
DR   SMR; P15306; -.
DR   IntAct; P15306; 2.
DR   MINT; P15306; -.
DR   STRING; 10090.ENSMUSP00000096877; -.
DR   iPTMnet; P15306; -.
DR   PhosphoSitePlus; P15306; -.
DR   PaxDb; P15306; -.
DR   PeptideAtlas; P15306; -.
DR   PRIDE; P15306; -.
DR   Ensembl; ENSMUST00000099270; ENSMUSP00000096877; ENSMUSG00000074743.
DR   GeneID; 21824; -.
DR   KEGG; mmu:21824; -.
DR   UCSC; uc008mtd.2; mouse.
DR   CTD; 7056; -.
DR   MGI; MGI:98736; Thbd.
DR   eggNOG; ENOG410IF0T; Eukaryota.
DR   eggNOG; ENOG410Y5JS; LUCA.
DR   GeneTree; ENSGT00940000163276; -.
DR   HOGENOM; HOG000114624; -.
DR   HOVERGEN; HBG000291; -.
DR   InParanoid; P15306; -.
DR   KO; K03907; -.
DR   OMA; LCGPLCV; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; P15306; -.
DR   TreeFam; TF330714; -.
DR   Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR   PRO; PR:P15306; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000074743; Expressed in 275 organ(s), highest expression level in lung.
DR   ExpressionAtlas; P15306; baseline and differential.
DR   Genevisible; P15306; MM.
DR   GO; GO:0016327; C:apicolateral plasma membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005774; C:vacuolar membrane; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; TAS:MGI.
DR   GO; GO:0007565; P:female pregnancy; IMP:MGI.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; IEA:InterPro.
DR   GO; GO:0050819; P:negative regulation of coagulation; TAS:MGI.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016316; CD141.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR015149; Tme5_EGF-like.
DR   PANTHER; PTHR24036:SF5; PTHR24036:SF5; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF09064; Tme5_EGF_like; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   1: Evidence at protein level;
KW   Blood coagulation; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hemostasis; Membrane; Proteoglycan; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17    577       Thrombomodulin.
FT                                /FTId=PRO_0000007772.
FT   TOPO_DOM     17    517       Extracellular. {ECO:0000255}.
FT   TRANSMEM    518    541       Helical. {ECO:0000255}.
FT   TOPO_DOM    542    577       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       31    167       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      240    280       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      283    323       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      324    362       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      364    404       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      403    439       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      440    480       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CARBOHYD    113    113       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    243    243       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    408    408       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    494    494       O-linked (Xyl...) (glycosaminoglycan)
FT                                serine. {ECO:0000250}.
FT   DISULFID    135    156       {ECO:0000250}.
FT   DISULFID    244    255       {ECO:0000250}.
FT   DISULFID    251    264       {ECO:0000250}.
FT   DISULFID    266    279       {ECO:0000250}.
FT   DISULFID    287    295       {ECO:0000250}.
FT   DISULFID    291    307       {ECO:0000250}.
FT   DISULFID    309    322       {ECO:0000250}.
FT   DISULFID    328    339       {ECO:0000250}.
FT   DISULFID    335    348       {ECO:0000250}.
FT   DISULFID    350    361       {ECO:0000250}.
FT   DISULFID    368    377       {ECO:0000250}.
FT   DISULFID    373    387       {ECO:0000250}.
FT   DISULFID    389    403       {ECO:0000250}.
FT   DISULFID    407    416       {ECO:0000250}.
FT   DISULFID    412    424       {ECO:0000250}.
FT   DISULFID    426    438       {ECO:0000250}.
FT   DISULFID    444    454       {ECO:0000250}.
FT   DISULFID    449    463       {ECO:0000250}.
FT   DISULFID    465    479       {ECO:0000250}.
SQ   SEQUENCE   577 AA;  61868 MW;  B20E50B0FE745014 CRC64;
     MLGIFFLGVL APASLGLSAL AKLQPTGSQC VEHECFALFQ GPATFLDASQ ACQRLQGHLM
     TVRSSVAADV ISLLLSQSSM DLGPWIGLQL PQGCDDPVHL GPLRGFQWVT GDNHTSYSRW
     ARPNDQTAPL CGPLCVTVST ATEAAPGEPA WEEKPCETET QGFLCEFYFT ASCRPLTVNT
     RDPEAAHISS TYNTPFGVSG ADFQTLPVGS SAAVEPLGLE LVCRAPPGTS EGHWAWEATG
     AWNCSVENGG CEYLCNRSTN EPRCLCPRDM DLQADGRSCA RPVVQSCNEL CEHFCVSNAE
     VPGSYSCMCE TGYQLAADGH RCEDVDDCKQ GPNPCPQLCV NTKGGFECFC YDGYELVDGE
     CVELLDPCFG SNCEFQCQPV SPTDYRCICA PGFAPKPDEP HKCEMFCNET SCPADCDPNS
     PTVCECPEGF ILDEGSVCTD IDECSQGECF TSECRNFPGS YECICGPDTA LAGQISKDCD
     PIPVREDTKE EEGSGEPPVS PTPGSPTGPP SARPVHSGVL IGISIASLSL VVALLALLCH
     LRKKQGAARA ELEYKCASSA KEVVLQHVRT DRTLQKF
//
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