TRBM_CANLF
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 25-MAY-2022, entry version 109.
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; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; 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 normal
RT tissues.";
RL J. Vet. Med. Sci. 66:1423-1427(2004).
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 -!- TISSUE SPECIFICITY: Expressed in lung, liver, spleen, kidney, pancreas
CC and lymph node. Low expression in heart, cerebrum, urinary bladder and
CC uterus. {ECO:0000269|PubMed:15585960}.
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; AB193481; BAD66823.1; -; mRNA.
DR RefSeq; NP_001006954.1; NM_001006953.2.
DR AlphaFoldDB; Q5W7P8; -.
DR SMR; Q5W7P8; -.
DR STRING; 9615.ENSCAFP00000007702; -.
DR PaxDb; Q5W7P8; -.
DR GeneID; 474355; -.
DR KEGG; cfa:474355; -.
DR CTD; 7056; -.
DR eggNOG; ENOG502R1T7; Eukaryota.
DR InParanoid; Q5W7P8; -.
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; 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; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hemostasis; Hydroxylation; Membrane; Proteoglycan; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..578
FT /note="Thrombomodulin"
FT /id="PRO_0000007770"
FT TOPO_DOM 17..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..167
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 242..282
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 285..325
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 326..364
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 366..406
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 405..441
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 442..481
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 483..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 495
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT DISULFID 137..158
FT /evidence="ECO:0000250"
FT DISULFID 246..257
FT /evidence="ECO:0000250"
FT DISULFID 253..266
FT /evidence="ECO:0000250"
FT DISULFID 268..281
FT /evidence="ECO:0000250"
FT DISULFID 289..297
FT /evidence="ECO:0000250"
FT DISULFID 293..309
FT /evidence="ECO:0000250"
FT DISULFID 311..324
FT /evidence="ECO:0000250"
FT DISULFID 330..341
FT /evidence="ECO:0000250"
FT DISULFID 337..350
FT /evidence="ECO:0000250"
FT DISULFID 352..363
FT /evidence="ECO:0000250"
FT DISULFID 370..379
FT /evidence="ECO:0000250"
FT DISULFID 375..389
FT /evidence="ECO:0000250"
FT DISULFID 391..405
FT /evidence="ECO:0000250"
FT DISULFID 409..414
FT /evidence="ECO:0000250"
FT DISULFID 418..426
FT /evidence="ECO:0000250"
FT DISULFID 428..440
FT /evidence="ECO:0000250"
FT DISULFID 446..455
FT /evidence="ECO:0000250"
FT DISULFID 451..464
FT /evidence="ECO:0000250"
FT DISULFID 466..480
FT /evidence="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
