TRBM_SAISC
ID TRBM_SAISC Reviewed; 575 AA.
AC Q71U07;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Thrombomodulin;
DE Short=TM;
DE AltName: CD_antigen=CD141;
DE Flags: Precursor;
GN Name=THBD; Synonyms=TMSC;
OS Saimiri sciureus (Common squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=9521;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Parzy D., Fusai T., Torrentino M., Pouvelle B., Gysin J.;
RT "Saimiri sciureus thrombomodulin gene.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ITGAL, ITGAM and ITGB2.
CC {ECO:0000250|UniProtKB:P07204}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
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DR EMBL; AF169484; AAD49735.1; -; Genomic_DNA.
DR AlphaFoldDB; Q71U07; -.
DR BMRB; Q71U07; -.
DR SMR; Q71U07; -.
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 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; IPR026823; cEGF.
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; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
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; 2.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 2.
PE 3: Inferred from homology;
KW Blood coagulation; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hemostasis; Hydroxylation; Membrane; Proteoglycan; Receptor; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..575
FT /note="Thrombomodulin"
FT /id="PRO_0000007773"
FT TOPO_DOM 19..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..169
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 241..281
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 284..324
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 325..363
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 365..405
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 404..440
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 441..481
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 484..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 342
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 492
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT DISULFID 137..158
FT /evidence="ECO:0000250"
FT DISULFID 245..256
FT /evidence="ECO:0000250"
FT DISULFID 252..265
FT /evidence="ECO:0000250"
FT DISULFID 267..280
FT /evidence="ECO:0000250"
FT DISULFID 288..296
FT /evidence="ECO:0000250"
FT DISULFID 292..308
FT /evidence="ECO:0000250"
FT DISULFID 310..323
FT /evidence="ECO:0000250"
FT DISULFID 329..340
FT /evidence="ECO:0000250"
FT DISULFID 336..349
FT /evidence="ECO:0000250"
FT DISULFID 351..362
FT /evidence="ECO:0000250"
FT DISULFID 369..378
FT /evidence="ECO:0000250"
FT DISULFID 374..388
FT /evidence="ECO:0000250"
FT DISULFID 390..404
FT /evidence="ECO:0000250"
FT DISULFID 408..413
FT /evidence="ECO:0000250"
FT DISULFID 417..425
FT /evidence="ECO:0000250"
FT DISULFID 427..439
FT /evidence="ECO:0000250"
FT DISULFID 445..455
FT /evidence="ECO:0000250"
FT DISULFID 451..464
FT /evidence="ECO:0000250"
FT DISULFID 466..480
FT /evidence="ECO:0000250"
SQ SEQUENCE 575 AA; 60329 MW; 9AF03CD151227D52 CRC64;
MLGVLVLGAL ALAGLGFPAP AEPQPGGSQC VEHDCFALYP GPATFLNASQ ICDGLRGHLM
TVRSSVAADV ISLLLNGDGG VGRRRLWIGL QLPPGCGDPK RLGPLRGFQW VTGDNNTSYS
RWARLDLNGA PLCGPLCVAV SAAEATVPSE PIWEEQQCEV KADGFLCEFH FPATCRPLAV
EPGAAAAAVS ITYGTPFAAR GADFQALPVG SSAAVAPLGL QLMCTAPPGA VQGHWAREAP
GAWDCSVENG GCEHACNAIP GAPRCQCPAG AALQADGRSC TASATQSCND LCEHFCVPNP
DQPGSYSCMC ETGYRLAADQ HRCEDVDDCI LEPSPCPQRC VNTQGGFECH CYPNYDLVDG
ECVEPVDPCF RANCEYQCQP LNQTSYLCVC AEGFAPIPHE PHRCQMFCNQ TACPADCDPN
TQASCECPEG YILDDGFICT DIDECENGGF CSGVCHNLPG TFECICGPDS ALARHIGTDC
DSGKVDGGDS GSGEPPPSPT PGSTLTPPAV GLVHSGLLIG ISIASLCLVV ALLALLCHLR
KKQGAARAKM EYKCAAPSKE VVLQHVRTER TPQRL
