TRBM_MOUSE
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 03-AUG-2022, entry version 192.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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; DOI=10.1016/s0021-9258(19)37661-6;
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 project:
RT 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., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Thrombomodulin is a specific endothelial cell receptor that
CC forms a 1:1 stoichiometric complex with thrombin. This complex is
CC responsible for the conversion of protein C to the activated protein C
CC (protein Ca). Once evolved, protein Ca scissions the activated
CC cofactors of the coagulation mechanism, factor Va and factor VIIIa, and
CC thereby reduces the amount of thrombin generated.
CC -!- SUBUNIT: Interacts with ITGAL, ITGAM and ITGB2.
CC {ECO:0000250|UniProtKB:P07204}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane 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";
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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 AlphaFoldDB; P15306; -.
DR SMR; P15306; -.
DR BioGRID; 204174; 2.
DR IntAct; P15306; 1.
DR MINT; P15306; -.
DR STRING; 10090.ENSMUSP00000096877; -.
DR GlyGen; P15306; 5 sites.
DR iPTMnet; P15306; -.
DR PhosphoSitePlus; P15306; -.
DR PaxDb; P15306; -.
DR PeptideAtlas; P15306; -.
DR PRIDE; P15306; -.
DR ProteomicsDB; 298287; -.
DR Antibodypedia; 792; 1016 antibodies from 44 providers.
DR DNASU; 21824; -.
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 VEuPathDB; HostDB:ENSMUSG00000074743; -.
DR eggNOG; ENOG502R1T7; Eukaryota.
DR GeneTree; ENSGT00940000163276; -.
DR HOGENOM; CLU_027075_2_1_1; -.
DR InParanoid; P15306; -.
DR OMA; HRCQMFC; -.
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 BioGRID-ORCS; 21824; 3 hits in 72 CRISPR screens.
DR PRO; PR:P15306; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P15306; protein.
DR Bgee; ENSMUSG00000074743; Expressed in right lung lobe and 258 other tissues.
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:0009897; C:external side of plasma membrane; IDA: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:1905370; C:serine-type endopeptidase complex; 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; 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; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hemostasis; Membrane; Proteoglycan; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..577
FT /note="Thrombomodulin"
FT /id="PRO_0000007772"
FT TOPO_DOM 17..517
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..167
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 240..280
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 283..323
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 324..362
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 364..404
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 403..439
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 440..480
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 476..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT DISULFID 135..156
FT /evidence="ECO:0000250"
FT DISULFID 244..255
FT /evidence="ECO:0000250"
FT DISULFID 251..264
FT /evidence="ECO:0000250"
FT DISULFID 266..279
FT /evidence="ECO:0000250"
FT DISULFID 287..295
FT /evidence="ECO:0000250"
FT DISULFID 291..307
FT /evidence="ECO:0000250"
FT DISULFID 309..322
FT /evidence="ECO:0000250"
FT DISULFID 328..339
FT /evidence="ECO:0000250"
FT DISULFID 335..348
FT /evidence="ECO:0000250"
FT DISULFID 350..361
FT /evidence="ECO:0000250"
FT DISULFID 368..377
FT /evidence="ECO:0000250"
FT DISULFID 373..387
FT /evidence="ECO:0000250"
FT DISULFID 389..403
FT /evidence="ECO:0000250"
FT DISULFID 407..416
FT /evidence="ECO:0000250"
FT DISULFID 412..424
FT /evidence="ECO:0000250"
FT DISULFID 426..438
FT /evidence="ECO:0000250"
FT DISULFID 444..454
FT /evidence="ECO:0000250"
FT DISULFID 449..463
FT /evidence="ECO:0000250"
FT DISULFID 465..479
FT /evidence="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
