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Database: UniProt
Entry: A0A091PYW9_LEPDC
LinkDB: A0A091PYW9_LEPDC
Original site: A0A091PYW9_LEPDC 
ID   A0A091PYW9_LEPDC        Unreviewed;       475 AA.
AC   A0A091PYW9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 32.
DE   RecName: Full=Thrombomodulin {ECO:0000256|ARBA:ARBA00019822};
DE   Flags: Fragment;
GN   ORFNames=N330_06015 {ECO:0000313|EMBL:KFQ12511.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ12511.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ12511.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ12511.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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.
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}.
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DR   EMBL; KK680740; KFQ12511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PYW9; -.
DR   Proteomes; UP000053001; 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   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
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; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR   PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF09064; Tme5_EGF_like; 1.
DR   PIRSF; PIRSF001775; CD93/CD141; 2.
DR   PRINTS; PR00907; THRMBOMODULN.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 4.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 2.
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:UP000053001};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        423..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..124
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          349..386
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          396..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ12511.1"
FT   NON_TER         475
FT                   /evidence="ECO:0000313|EMBL:KFQ12511.1"
SQ   SEQUENCE   475 AA;  51867 MW;  E2CD15AA80A61F13 CRC64;
     AQCLEHDCFS IFWSAKPFAE ASEVCKGGGG HLMTVRSTVA EDAIALLVQN RSGRLWLGLR
     LPLPCTEPAQ RLRGFQWVTG DGRTDYSNWA PSMGRRCGER CVTGSREPRW EEQRSEARGD
     FLVLPPCSIA TIPAIGLELR CDKDRESGVL RWEHDGPGAW PCLLANGGCE GMCGEEGGQP
     RCSCPDGKLL DPDGRSCSSP CAGAPCQHHC IVNGTSFLCM CESGSADGTS CEDDDDCAVF
     PRLCEQVCVN TEGGFECHCY RGYKMLEGSC RPVSRCYEAP CEQQCEDVPH GYRCGCFPGY
     AVHPQMPTRC LLHCNHSQCP AQCDTNTLSC ECPEGFVLDD ANSGQVCMDI DECNMNYCQH
     NCTNHPGGYE CHCYAGYQLV NENDCVKITE DWEGEYSGDF RPRPQTPIPS RTPPKAAHLH
     PGALVGITMG ALSAALALLA LGYHLAKKSC RPPSTMDYKY SGPHEKEMGL QPITS
//
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