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Database: UniProt
Entry: Q5W7P8
LinkDB: Q5W7P8
Original site: Q5W7P8 
ID   TRBM_CANLF              Reviewed;         578 AA.
AC   Q5W7P8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   10-APR-2019, entry version 99.
DE   RecName: Full=Thrombomodulin;
DE            Short=TM;
DE   AltName: CD_antigen=CD141;
DE   Flags: Precursor;
GN   Name=THBD;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15585960; DOI=10.1292/jvms.66.1423;
RA   Maruyama H., Oguma K., Maeda S., Kano R., Tsujimoto H., Watari T.,
RA   Tokuriki M., Hasegawa A.;
RT   "Molecular cloning of canine thrombomodulin cDNA and expression in
RT   normal tissues.";
RL   J. Vet. Med. Sci. 66:1423-1427(2004).
CC   -!- FUNCTION: Thrombomodulin is a specific endothelial cell receptor
CC       that forms a 1:1 stoichiometric complex with thrombin. This
CC       complex is responsible for the conversion of protein C to the
CC       activated protein C (protein Ca). Once evolved, protein Ca
CC       scissions the activated cofactors of the coagulation mechanism,
CC       factor Va and factor VIIIa, and thereby reduces the amount of
CC       thrombin generated (By similarity). {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   -!- TISSUE SPECIFICITY: Expressed in lung, liver, spleen, kidney,
CC       pancreas and lymph node. Low expression in heart, cerebrum,
CC       urinary bladder and uterus. {ECO:0000269|PubMed:15585960}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
DR   EMBL; AB193481; BAD66823.1; -; mRNA.
DR   RefSeq; NP_001006954.1; NM_001006953.2.
DR   UniGene; Cfa.16238; -.
DR   ProteinModelPortal; Q5W7P8; -.
DR   SMR; Q5W7P8; -.
DR   STRING; 9612.ENSCAFP00000007702; -.
DR   PaxDb; Q5W7P8; -.
DR   PRIDE; Q5W7P8; -.
DR   GeneID; 474355; -.
DR   KEGG; cfa:474355; -.
DR   CTD; 7056; -.
DR   eggNOG; ENOG410IF0T; Eukaryota.
DR   eggNOG; ENOG410Y5JS; LUCA.
DR   HOGENOM; HOG000114624; -.
DR   HOVERGEN; HBG000291; -.
DR   InParanoid; Q5W7P8; -.
DR   KO; K03907; -.
DR   OrthoDB; 1174178at2759; -.
DR   Proteomes; UP000002254; 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   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   2: Evidence at transcript level;
KW   Blood coagulation; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Hemostasis; Hydroxylation; Membrane; Proteoglycan;
KW   Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17    578       Thrombomodulin.
FT                                /FTId=PRO_0000007770.
FT   TOPO_DOM     17    518       Extracellular. {ECO:0000255}.
FT   TRANSMEM    519    539       Helical. {ECO:0000255}.
FT   TOPO_DOM    540    578       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       31    167       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      242    282       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      285    325       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      326    364       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      366    406       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      405    441       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      442    481       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MOD_RES     343    343       (3R)-3-hydroxyasparagine. {ECO:0000250}.
FT   CARBOHYD    114    114       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    300    300       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    493    493       O-linked (Xyl...) (glycosaminoglycan)
FT                                serine. {ECO:0000250}.
FT   CARBOHYD    495    495       O-linked (Xyl...) (glycosaminoglycan)
FT                                serine. {ECO:0000250}.
FT   DISULFID    137    158       {ECO:0000250}.
FT   DISULFID    246    257       {ECO:0000250}.
FT   DISULFID    253    266       {ECO:0000250}.
FT   DISULFID    268    281       {ECO:0000250}.
FT   DISULFID    289    297       {ECO:0000250}.
FT   DISULFID    293    309       {ECO:0000250}.
FT   DISULFID    311    324       {ECO:0000250}.
FT   DISULFID    330    341       {ECO:0000250}.
FT   DISULFID    337    350       {ECO:0000250}.
FT   DISULFID    352    363       {ECO:0000250}.
FT   DISULFID    370    379       {ECO:0000250}.
FT   DISULFID    375    389       {ECO:0000250}.
FT   DISULFID    391    405       {ECO:0000250}.
FT   DISULFID    409    414       {ECO:0000250}.
FT   DISULFID    418    426       {ECO:0000250}.
FT   DISULFID    428    440       {ECO:0000250}.
FT   DISULFID    446    455       {ECO:0000250}.
FT   DISULFID    451    464       {ECO:0000250}.
FT   DISULFID    466    480       {ECO:0000250}.
SQ   SEQUENCE   578 AA;  60745 MW;  06D255C9BBFCC883 CRC64;
     MLRVLLLGVL APAGLGLPTP AQPQPRSSQC MEHDCFQLFR GPATFLAASQ TCEGLGGHLM
     TVRSSVAADV ISLLLSGDGG DGPRLWIGLQ LRRGCSDPGQ GGPLRGFQWV TGDNRTSYSR
     WARPHVGPAG PPCAPLCVAV SDAAAPAPGE PAWEEQRCAA EADGFLCEFH FAASCRPLLV
     DARAAAAAGV SVTYSTPFGA RGADFQALPA GSSAAVAPFG VQLACAAPRG EAEARWGREA
     PGAWDCSVEN GGCQRACSAS AGAPRCLCPA DTYLQADGRS CATFAEHSCH KLCEHFCIPN
     ASVPGSYLCM CETGYQLAAD QHRCEDVDDC IQVPSLCPQL CVNTRGAFEC HCYPGYELVD
     NECVEPVDPC FGSKCEYQCQ PVSQTDYRCI CAEGFAPVPH DPHRCQMFCN QTACPADCDP
     NSPTSCQCPE GYILDDGFMC TDIDECENGE CPEACRNLPG TYECICGPDS PLAGQVATDC
     GRIISDPDGD SDSGSGEPPV TPTPGVTPSP SPVGPVHSGV LIGISIASLS LVVALLALLC
     HLRKKQGAPR AELEYKCGAP AKEVVLQHVR TEQMPQKL
//
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