TRBM_BOVIN
ID TRBM_BOVIN Reviewed; 356 AA.
AC P06579;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Thrombomodulin;
DE Short=TM;
DE AltName: Full=Fetomodulin;
DE AltName: CD_antigen=CD141;
DE Flags: Fragment;
GN Name=THBD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3024152; DOI=10.1073/pnas.83.23.8834;
RA Jackman R.W., Beeler D.L., Vandewater L., Rosenberg R.D.;
RT "Characterization of a thrombomodulin cDNA reveals structural similarity to
RT the low density lipoprotein receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8834-8838(1986).
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.
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DR EMBL; M14657; AAA30785.1; -; mRNA.
DR PIR; A25918; A25918.
DR AlphaFoldDB; P06579; -.
DR SMR; P06579; -.
DR STRING; 9913.ENSBTAP00000052487; -.
DR PaxDb; P06579; -.
DR eggNOG; ENOG502R1T7; Eukaryota.
DR InParanoid; P06579; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
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; IEA:UniProtKB-KW.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IEA:InterPro.
DR InterPro; IPR016316; CD141.
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; PF09064; Tme5_EGF_like; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
PE 2: Evidence at transcript level;
KW Blood coagulation; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hemostasis; Membrane; Proteoglycan; Receptor; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..356
FT /note="Thrombomodulin"
FT /id="PRO_0000055636"
FT TOPO_DOM 1..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..57
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 60..98
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 99..137
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 139..179
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 178..214
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 215..254
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 255..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 271
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT DISULFID 21..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 28..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 43..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 64..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 68..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 84..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 103..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 110..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 125..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 143..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 148..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 164..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 182..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 187..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 201..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 219..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 224..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 239..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT NON_TER 1
SQ SEQUENCE 356 AA; 37795 MW; 29B41F097ABE1093 CRC64;
RGARGETEGR WSREAPGAWA CGVERGGCQH ECKGSAGASN CLCPADAALQ ADGRSCGLPA
EHPCHQLCEH FCHLHGLGNY TCICEAGYQL AADQHRCEDV DDCAQLPSPC PQRCVNTEGG
FQCHCDTGYE LVDGECVDPV DPCFDNNCEY QCQPVGRSEH KCICAEGFAP VPGAPHKCQM
FCNQTSCPAD CDPHYPTICR CPEGYIIDEG STCTDINECD TNICPGQCHN LPGTYECICG
PDSALSGQIG IDCDPTQVNE ERGTPEDYGG SGEPPVSPTP GATARPSPAP AGPLHSGVLV
GISIASLSLV VALLALLCHL RKKQGASRGE LEYKCGVPAK ELMLQQVKTE RTPQKL
