ID   TPO_HUMAN               Reviewed;         353 AA.
AC   P40225; A1L3Y0; B7ZLR8; B9EGA8; Q13020; Q15790; Q15791; Q15792;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 203.
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   AltName: Full=Myeloproliferative leukemia virus oncogene ligand;
DE   Flags: Precursor;
GN   Name=THPO; Synonyms=MGDF;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal liver;
RX   PubMed=8202154; DOI=10.1038/369533a0;
RA   de Sauvage F.J., Hass P.E., Spencer S.D., Malloy B.E., Gurney A.L.,
RA   Spencer S.A., Darbonne W.C., Henzel W.J., Wong S.C., Kuang W.-J.,
RA   Oles K.J., Hultgren B., Solberg L.A. Jr., Goeddel D.V., Eaton D.L.;
RT   "Stimulation of megakaryocytopoiesis and thrombopoiesis by the c-Mpl
RT   ligand.";
RL   Nature 369:533-538(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal liver;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=7809166; DOI=10.1073/pnas.91.26.13023;
RA   Foster D.C., Sprecher C.A., Grant F.J., Kramer J.M., Kuijper J.L.,
RA   Holly R.D., Whitmore T.E., Heipel M.D., Bell L.A.N., Ching A.F.,
RA   McGrane V., Hart C., O'Hara P.J., Lok S.;
RT   "Human thrombopoietin: gene structure, cDNA sequence, expression, and
RT   chromosomal localization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:13023-13027(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=7926023; DOI=10.1016/0014-5793(94)01008-0;
RA   Sohma Y., Akahori H., Seki N., Hori T.-A., Ogami K., Kawamura K.,
RA   Miyazaki H.;
RT   "Molecular cloning and chromosomal localization of the human thrombopoietin
RT   gene.";
RL   FEBS Lett. 353:57-61(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX   PubMed=7849319;
RA   Gurney A.L., Kuang W.-J., Xie M.-H., Malloy B.E., Eaton D.L.,
RA   de Sauvage F.J.;
RT   "Genomic structure, chromosomal localization, and conserved alternative
RT   splice forms of thrombopoietin.";
RL   Blood 85:981-988(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=8537317; DOI=10.1093/oxfordjournals.jbchem.a124883;
RA   Kato T., Ogami K., Shimada Y., Iwamatsu A., Sohma Y., Akahori H., Horie K.,
RA   Kokubo A., Kudo Y., Maeda E., Kobayashi K., Ohashi H., Ozawa T., Inoue H.,
RA   Kawamura K., Miyazaki H.;
RT   "Purification and characterization of thrombopoietin.";
RL   J. Biochem. 118:229-236(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=7822271; DOI=10.1074/jbc.270.2.511;
RA   Chang M., McNinch J., Basu R., Shutter J., Hsu R., Perkins C., Mar V.,
RA   Suggs S., Welcher A., Li L., Lu H., Bartley T., Hunt P., Martin F.,
RA   Samal B., Bogenberger J.;
RT   "Cloning and characterization of the human megakaryocyte growth and
RT   development factor (MGDF) gene.";
RL   J. Biol. Chem. 270:511-514(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
RA   Im S.H., Lee W.S., Chung K.H.;
RT   "Cloning and sequencing of human thrombopoietin.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   DISEASE.
RX   PubMed=9425899; DOI=10.1038/ng0198-49;
RA   Wiestner A., Schlemper R.J., van der Maas A.P.C., Skoda R.C.;
RT   "An activating splice donor mutation in the thrombopoietin gene causes
RT   hereditary thrombocythaemia.";
RL   Nat. Genet. 18:49-52(1998).
RN   [11]
RP   DISULFIDE BONDS, AND GLYCOSYLATION AT SER-22; THR-58; THR-131; THR-179;
RP   THR-180; SER-184; ASN-197; ASN-206; THR-213; ASN-234; ASN-255 AND SER-265.
RX   PubMed=8942648; DOI=10.1021/bi961075b;
RA   Hoffman R.C., Andersen H., Walker K., Krakover J.D., Patel S., Stamm M.R.,
RA   Osborn S.G.;
RT   "Peptide, disulfide, and glycosylation mapping of recombinant human
RT   thrombopoietin from ser1 to Arg246.";
RL   Biochemistry 35:14849-14861(1996).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 22-184 IN COMPLEX WITH ANTIBODY,
RP   AND DISULFIDE BONDS.
RX   PubMed=14769915; DOI=10.1073/pnas.0308530100;
RA   Feese M.D., Tamada T., Kato Y., Maeda Y., Hirose M., Matsukura Y.,
RA   Shigematsu H., Muto T., Matsumoto A., Watarai H., Ogami K., Tahara T.,
RA   Kato T., Miyazaki H., Kuroki R.;
RT   "Structure of the receptor-binding domain of human thrombopoietin
RT   determined by complexation with a neutralizing antibody fragment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:1816-1821(2004).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P40225-1; Sequence=Displayed;
CC       Name=2; Synonyms=TPO-2;
CC         IsoId=P40225-2; Sequence=VSP_001450;
CC       Name=3; Synonyms=Truncated;
CC         IsoId=P40225-3; Sequence=VSP_001451;
CC   -!- DOMAIN: Two-domain structure with an erythropoietin-like N-terminal and
CC       a Ser/Pro/Thr-rich C-terminal.
CC   -!- DISEASE: Thrombocythemia 1 (THCYT1) [MIM:187950]: A myeloproliferative
CC       disorder characterized by excessive platelet production, resulting in
CC       increased numbers of circulating platelets. It can be associated with
CC       spontaneous hemorrhages and thrombotic episodes. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the EPO/TPO family. {ECO:0000305}.
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DR   EMBL; L33410; AAA59857.1; -; mRNA.
DR   EMBL; U11025; AAA50553.1; -; mRNA.
DR   EMBL; L36051; AAC37568.1; -; Genomic_DNA.
DR   EMBL; L36052; AAC37566.1; -; mRNA.
DR   EMBL; D32046; BAA06807.1; -; Genomic_DNA.
DR   EMBL; S76771; AAB33390.1; -; Genomic_DNA.
DR   EMBL; D32047; BAA21930.1; -; mRNA.
DR   EMBL; U59493; AAB03392.1; -; mRNA.
DR   EMBL; U59494; AAB03393.1; -; mRNA.
DR   EMBL; U59495; AAB03394.1; -; mRNA.
DR   EMBL; U17071; AAA74083.1; -; Genomic_DNA.
DR   EMBL; BC130322; AAI30323.1; -; mRNA.
DR   EMBL; BC136338; AAI36339.1; -; mRNA.
DR   EMBL; BC143982; AAI43983.1; -; mRNA.
DR   CCDS; CCDS3265.1; -. [P40225-1]
DR   CCDS; CCDS54693.1; -. [P40225-2]
DR   PIR; G02729; G02729.
DR   PIR; I59281; I80105.
DR   RefSeq; NP_000451.1; NM_000460.3. [P40225-1]
DR   RefSeq; NP_001171068.1; NM_001177597.2. [P40225-2]
DR   RefSeq; NP_001171069.1; NM_001177598.2.
DR   RefSeq; NP_001276926.1; NM_001289997.1.
DR   RefSeq; NP_001276927.1; NM_001289998.1. [P40225-1]
DR   RefSeq; NP_001276932.1; NM_001290003.1.
DR   RefSeq; NP_001276951.1; NM_001290022.1. [P40225-2]
DR   RefSeq; NP_001276955.1; NM_001290026.1.
DR   RefSeq; NP_001276956.1; NM_001290027.1.
DR   RefSeq; NP_001276957.1; NM_001290028.1. [P40225-1]
DR   PDB; 1V7M; X-ray; 2.51 A; V/X=22-184.
DR   PDB; 1V7N; X-ray; 3.30 A; V/X/Y/Z=22-184.
DR   PDB; 8G04; EM; 3.40 A; A=22-184.
DR   PDBsum; 1V7M; -.
DR   PDBsum; 1V7N; -.
DR   PDBsum; 8G04; -.
DR   AlphaFoldDB; P40225; -.
DR   EMDB; EMD-29644; -.
DR   SMR; P40225; -.
DR   BioGRID; 112922; 6.
DR   DIP; DIP-5729N; -.
DR   ELM; P40225; -.
DR   IntAct; P40225; 3.
DR   STRING; 9606.ENSP00000494504; -.
DR   ChEMBL; CHEMBL1293256; -.
DR   GlyConnect; 592; 12 N-Linked glycans, 4 O-Linked glycans.
DR   GlyCosmos; P40225; 14 sites, 32 glycans.
DR   GlyGen; P40225; 15 sites, 25 N-linked glycans (2 sites), 7 O-linked glycans (1 site).
DR   iPTMnet; P40225; -.
DR   PhosphoSitePlus; P40225; -.
DR   BioMuta; THPO; -.
DR   DMDM; 730982; -.
DR   MassIVE; P40225; -.
DR   PaxDb; 9606-ENSP00000204615; -.
DR   PeptideAtlas; P40225; -.
DR   ProteomicsDB; 55350; -. [P40225-1]
DR   ProteomicsDB; 55351; -. [P40225-2]
DR   ProteomicsDB; 55352; -. [P40225-3]
DR   ABCD; P40225; 1 sequenced antibody.
DR   Antibodypedia; 19145; 682 antibodies from 36 providers.
DR   DNASU; 7066; -.
DR   Ensembl; ENST00000445696.6; ENSP00000410763.2; ENSG00000090534.20. [P40225-2]
DR   Ensembl; ENST00000647395.1; ENSP00000494504.1; ENSG00000090534.20. [P40225-1]
DR   GeneID; 7066; -.
DR   KEGG; hsa:7066; -.
DR   MANE-Select; ENST00000647395.1; ENSP00000494504.1; NM_000460.4; NP_000451.1.
DR   UCSC; uc003fol.2; human. [P40225-1]
DR   AGR; HGNC:11795; -.
DR   CTD; 7066; -.
DR   DisGeNET; 7066; -.
DR   GeneCards; THPO; -.
DR   HGNC; HGNC:11795; THPO.
DR   HPA; ENSG00000090534; Tissue enriched (liver).
DR   MalaCards; THPO; -.
DR   MIM; 187950; phenotype.
DR   MIM; 600044; gene.
DR   neXtProt; NX_P40225; -.
DR   OpenTargets; ENSG00000090534; -.
DR   Orphanet; 3319; Congenital amegakaryocytic thrombocytopenia.
DR   Orphanet; 71493; Familial thrombocytosis.
DR   Orphanet; 397692; Hereditary isolated aplastic anemia.
DR   Orphanet; 329319; Thrombocythemia with distal limb defects.
DR   PharmGKB; PA36506; -.
DR   VEuPathDB; HostDB:ENSG00000090534; -.
DR   eggNOG; ENOG502S9T0; Eukaryota.
DR   GeneTree; ENSGT00390000006294; -.
DR   HOGENOM; CLU_039844_0_0_1; -.
DR   InParanoid; P40225; -.
DR   OMA; PILCARQ; -.
DR   OrthoDB; 5347971at2759; -.
DR   PhylomeDB; P40225; -.
DR   TreeFam; TF338084; -.
DR   PathwayCommons; P40225; -.
DR   Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR   SignaLink; P40225; -.
DR   SIGNOR; P40225; -.
DR   BioGRID-ORCS; 7066; 7 hits in 1139 CRISPR screens.
DR   ChiTaRS; THPO; human.
DR   EvolutionaryTrace; P40225; -.
DR   GeneWiki; Thrombopoietin; -.
DR   GenomeRNAi; 7066; -.
DR   Pharos; P40225; Tbio.
DR   PRO; PR:P40225; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P40225; Protein.
DR   Bgee; ENSG00000090534; Expressed in right lobe of liver and 93 other cell types or tissues.
DR   ExpressionAtlas; P40225; baseline and differential.
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:0008083; F:growth factor activity; TAS:UniProtKB.
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:0035855; P:megakaryocyte development; IDA:ARUK-UCL.
DR   GO; GO:0030219; P:megakaryocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:ARUK-UCL.
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; IDA:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:ARUK-UCL.
DR   GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:ARUK-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0097696; P:receptor signaling pathway via STAT; IDA:ARUK-UCL.
DR   GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; IDA:ARUK-UCL.
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; THROMBOPOIETIN; 1.
DR   PANTHER; PTHR10560:SF0; THROMBOPOIETIN; 1.
DR   Pfam; PF00758; EPO_TPO; 1.
DR   PRINTS; PR01485; THROMBOPTN.
DR   SUPFAM; SSF47266; 4-helical cytokines; 1.
DR   PROSITE; PS00817; EPO_TPO; 1.
DR   Genevisible; P40225; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytokine; Disulfide bond; Glycoprotein;
KW   Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT   CHAIN           22..353
FT                   /note="Thrombopoietin"
FT                   /id="PRO_0000008411"
FT   REGION          257..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..334
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        22
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        58
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        131
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        179
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        180
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        184
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        213
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        265
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:8942648"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..172
FT   DISULFID        50..106
FT   VAR_SEQ         133..136
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_001450"
FT   VAR_SEQ         160..198
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001451"
FT   VARIANT         14
FT                   /note="L -> P (in dbSNP:rs1042346)"
FT                   /id="VAR_011795"
FT   VARIANT         116
FT                   /note="G -> E (in dbSNP:rs1126665)"
FT                   /id="VAR_011796"
FT   CONFLICT        46
FT                   /note="R -> K (in Ref. 8; AAB03392/AAB03393/AAB03394)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="M -> MSQ (in Ref. 7; AAA74083)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="Q -> E (in Ref. 2; AAA50553)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="T -> P (in Ref. 7; AAA74083)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="G -> E (in Ref. 8; AAB03393/AAB03394)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="S -> C (in Ref. 8; AAB03393/AAB03394)"
FT                   /evidence="ECO:0000305"
FT   HELIX           32..45
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           77..98
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           113..129
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           148..157
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   TURN            158..160
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:1V7M"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:1V7N"
SQ   SEQUENCE   353 AA;  37823 MW;  F0AB5449B72E5526 CRC64;
     MELTELLLVV MLLLTARLTL SSPAPPACDL RVLSKLLRDS HVLHSRLSQC PEVHPLPTPV
     LLPAVDFSLG EWKTQMEETK AQDILGAVTL LLEGVMAARG QLGPTCLSSL LGQLSGQVRL
     LLGALQSLLG TQLPPQGRTT AHKDPNAIFL SFQHLLRGKV RFLMLVGGST LCVRRAPPTT
     AVPSRTSLVL TLNELPNRTS GLLETNFTAS ARTTGSGLLK WQQGFRAKIP GLLNQTSRSL
     DQIPGYLNRI HELLNGTRGL FPGPSRRTLG APDISSGTSD TGSLPPNLQP GYSPSPTHPP
     TGQYTLFPLP PTLPTPVVQL HPLLPDPSAP TPTPTSPLLN TSYTHSQNLS QEG
//