TPO_CANLF
ID TPO_CANLF Reviewed; 352 AA.
AC P42705;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Thrombopoietin;
DE AltName: Full=C-MPL ligand;
DE Short=ML;
DE AltName: Full=Megakaryocyte colony-stimulating factor;
DE AltName: Full=Megakaryocyte growth and development factor;
DE Short=MGDF;
DE Flags: Precursor;
GN Name=THPO; Synonyms=TPO;
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, AND PROTEIN SEQUENCE OF 24-44.
RC TISSUE=Kidney;
RX PubMed=8020099; DOI=10.1016/0092-8674(94)90450-2;
RA Bartley T.D., Bogenberger J., Hunt P., Li Y.-S., Lu H.S., Martin F.,
RA Chang M.-S., Samal B.B., Nichol J.L., Swift S., Johnson M.J., Hsu R.-Y.,
RA Parker V.P., Suggs S., Skrine J.D., Merewether L.A., Clogson C., Hsu E.,
RA Hokom M.M., Hornkohl A., Choi E., Pangelinan M., Sun Y., Mar V., McNich J.,
RA Simonet L., Jacobsen F., Xie C., Shutter J., Chute H., Basu R.,
RA Selander L., Trollinger D., Sieu L., Padilla D., Trail G., Elliott G.,
RA Izumi R., Covey T., Crouse J., Garcia A., Xu W., del Castillo J., Biron J.,
RA Cole S., Hu M.C.-T., Pacifici R., Ponting I., Saris C., Wen D., Yung Y.P.,
RA Lin H., Bosselman R.A.;
RT "Identification and cloning of a megakaryocyte growth and development
RT factor that is a ligand for the cytokine receptor Mpl.";
RL Cell 77:1117-1124(1994).
CC -!- FUNCTION: Lineage-specific cytokine affecting the proliferation and
CC maturation of megakaryocytes from their committed progenitor cells. It
CC acts at a late stage of megakaryocyte development. It may be the major
CC physiological regulator of circulating platelets.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: Two-domain structure with an erythropoietin-like N-terminal and
CC a Ser/Pro/Thr-rich C-terminal.
CC -!- SIMILARITY: Belongs to the EPO/TPO family. {ECO:0000305}.
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DR AlphaFoldDB; P42705; -.
DR SMR; P42705; -.
DR STRING; 9615.ENSCAFP00000066649; -.
DR InParanoid; P42705; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IBA:GO_Central.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR019767; EPO/TPO_CS.
DR InterPro; IPR001323; EPO_TPO.
DR InterPro; IPR003978; Thrombopoietin.
DR PANTHER; PTHR10560; PTHR10560; 1.
DR Pfam; PF00758; EPO_TPO; 1.
DR PRINTS; PR01485; THROMBOPTN.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00817; EPO_TPO; 1.
PE 1: Evidence at protein level;
KW Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8020099"
FT CHAIN 24..352
FT /note="Thrombopoietin"
FT /id="PRO_0000008410"
FT REGION 233..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..330
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..172
FT /evidence="ECO:0000255"
FT DISULFID 50..106
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 37642 MW; 024F3B41B061FBD8 CRC64;
MELTELLLVV MLLLTARLDP CLPAPPACDP RLLNKMLRDS HVLHSRLSQC PDIYPLSTPV
LLPAVDFSLG EWKTQKEQTK AQDVWGAVAL LLDGVLAARG QLGPSCLSSL LGQLSGQVRL
LLGALQGLLG TQLPPQGRTT THKDPNAIFL SFQQLLRGKV RFLLLVAGPT LCAKQSQPTT
AVPTNTSLFL TLRKLPNRTS GLLETNSSIS ARTTGSGLLK RLQGFRAKIP GLLNQTSRSL
NQTPGHLSRT HGPLNGTHGL LPGLSLTALG APDIPPGTSD MDALPPNLWP RYSPSPIHPP
PGQYTLFSPL PTSPTPQNPL QPPPPDPSAT ANSTSPLLIA AHPHFQNLSQ EE
