ID A0A2I0M9A6_COLLI Unreviewed; 204 AA.
AC A0A2I0M9A6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Thrombomodulin {ECO:0000256|ARBA:ARBA00019822};
GN Name=THBD {ECO:0000313|EMBL:PKK26262.1};
GN ORFNames=A306_00008221 {ECO:0000313|EMBL:PKK26262.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK26262.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK26262.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK26262.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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 {ECO:0000256|ARBA:ARBA00024920}.
CC -!- SUBUNIT: Interacts with ITGAL, ITGAM and ITGB2.
CC {ECO:0000256|ARBA:ARBA00011341}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK26262.1}.
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DR EMBL; AKCR02000027; PKK26262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0M9A6; -.
DR STRING; 8932.A0A2I0M9A6; -.
DR InParanoid; A0A2I0M9A6; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.10.25.10; Laminin; 2.
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; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF09064; Tme5_EGF_like; 1.
DR PRINTS; PR00907; THRMBOMODULN.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 143..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..105
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 115..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 21760 MW; 92000815FCF9D5E8 CRC64;
MLGGHCRPVS HCYKTPCEQK CEEVPDGYRC GCCNRSQCPA QCDPHSLSCE CPEGFVLDDV
ESKKICVDIN ECDMNYCQHD CVNHPGSYEC HCHAGYQLLN QNDCGKILEE DGDGGYSGDL
GPEAQTPIPS RTPPKAEHLH PGALVGIAMG ALSAALVLLA LGYHLAKKCC GSPSSMDYKC
GGPHKKEMGL QPVTSGCAAS GQKL
//