OSTF1_HUMAN
ID OSTF1_HUMAN Reviewed; 214 AA.
AC Q92882; Q5W126; Q96IJ4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Osteoclast-stimulating factor 1;
GN Name=OSTF1;
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], TISSUE SPECIFICITY, INTERACTION WITH SRC, AND
RP FUNCTION.
RC TISSUE=Bone marrow;
RX PubMed=10092216;
RX DOI=10.1002/(sici)1097-4652(199812)177:4<636::aid-jcp14>3.0.co;2-h;
RA Reddy S.V., Devlin R., Menaa C., Nishimura R., Choi S.J., Dallas M.,
RA Yoneda T., Roodman G.D.;
RT "Isolation and characterization of a cDNA clone encoding a novel peptide
RT (OSF) that enhances osteoclast formation and bone resorption.";
RL J. Cell. Physiol. 177:636-645(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-159.
RC TISSUE=Kidney;
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 [5]
RP INTERACTION WITH SMN1.
RA Roodman G.D.;
RL Unpublished observations (NOV-2000).
RN [6]
RP INTERACTION WITH SMN1.
RX PubMed=11551898; DOI=10.1074/jbc.m100233200;
RA Kurihara N., Menaa C., Maeda H., Haile D.J., Reddy S.V.;
RT "Osteoclast-stimulating factor interacts with the spinal muscular atrophy
RT gene product to stimulate osteoclast formation.";
RL J. Biol. Chem. 276:41035-41039(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP STRUCTURE BY NMR OF 15-69.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of human osteoclast-stimulating
RT factor 1 (OSTF1).";
RL Submitted (APR-2005) to the PDB data bank.
CC -!- FUNCTION: Induces bone resorption, acting probably through a signaling
CC cascade which results in the secretion of factor(s) enhancing
CC osteoclast formation and activity. {ECO:0000269|PubMed:10092216}.
CC -!- SUBUNIT: Interacts with SRC and SMN1. Interacts with FASLG.
CC {ECO:0000269|PubMed:10092216, ECO:0000269|PubMed:11551898,
CC ECO:0000269|PubMed:19807924, ECO:0000269|Ref.5}.
CC -!- INTERACTION:
CC Q92882; Q13444: ADAM15; NbExp=2; IntAct=EBI-1051152, EBI-77818;
CC Q92882; O43281: EFS; NbExp=3; IntAct=EBI-1051152, EBI-718488;
CC Q92882; P42858: HTT; NbExp=5; IntAct=EBI-1051152, EBI-466029;
CC Q92882; Q04864: REL; NbExp=3; IntAct=EBI-1051152, EBI-307352;
CC Q92882; O00560: SDCBP; NbExp=3; IntAct=EBI-1051152, EBI-727004;
CC Q92882; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-1051152, EBI-2130429;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in osteoclasts (at
CC protein level). {ECO:0000269|PubMed:10092216}.
CC -!- DOMAIN: The SH3 domain mediates interaction with SMN1.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U63717; AAB06396.1; -; mRNA.
DR EMBL; AK222596; BAD96316.1; -; mRNA.
DR EMBL; AL133548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007459; AAH07459.1; -; mRNA.
DR CCDS; CCDS6651.1; -.
DR RefSeq; NP_036515.4; NM_012383.4.
DR PDB; 1X2K; NMR; -; A=15-69.
DR PDB; 1ZLM; X-ray; 1.07 A; A=12-69.
DR PDB; 3EHQ; X-ray; 2.57 A; A/B=1-214.
DR PDB; 3EHR; X-ray; 1.95 A; A/B=1-214.
DR PDBsum; 1X2K; -.
DR PDBsum; 1ZLM; -.
DR PDBsum; 3EHQ; -.
DR PDBsum; 3EHR; -.
DR AlphaFoldDB; Q92882; -.
DR SMR; Q92882; -.
DR BioGRID; 117747; 83.
DR CORUM; Q92882; -.
DR IntAct; Q92882; 24.
DR MINT; Q92882; -.
DR STRING; 9606.ENSP00000340836; -.
DR GlyGen; Q92882; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92882; -.
DR PhosphoSitePlus; Q92882; -.
DR BioMuta; OSTF1; -.
DR DMDM; 108885279; -.
DR EPD; Q92882; -.
DR jPOST; Q92882; -.
DR MassIVE; Q92882; -.
DR MaxQB; Q92882; -.
DR PaxDb; Q92882; -.
DR PeptideAtlas; Q92882; -.
DR PRIDE; Q92882; -.
DR ProteomicsDB; 75569; -.
DR ABCD; Q92882; 2 sequenced antibodies.
DR Antibodypedia; 27176; 223 antibodies from 27 providers.
DR DNASU; 26578; -.
DR Ensembl; ENST00000346234.7; ENSP00000340836.6; ENSG00000134996.12.
DR GeneID; 26578; -.
DR KEGG; hsa:26578; -.
DR MANE-Select; ENST00000346234.7; ENSP00000340836.6; NM_012383.5; NP_036515.4.
DR UCSC; uc004ajv.5; human.
DR CTD; 26578; -.
DR DisGeNET; 26578; -.
DR GeneCards; OSTF1; -.
DR HGNC; HGNC:8510; OSTF1.
DR HPA; ENSG00000134996; Low tissue specificity.
DR MIM; 610180; gene.
DR neXtProt; NX_Q92882; -.
DR OpenTargets; ENSG00000134996; -.
DR PharmGKB; PA32839; -.
DR VEuPathDB; HostDB:ENSG00000134996; -.
DR eggNOG; ENOG502QTZB; Eukaryota.
DR GeneTree; ENSGT00920000149159; -.
DR HOGENOM; CLU_092255_0_0_1; -.
DR InParanoid; Q92882; -.
DR OMA; NMSWLRE; -.
DR OrthoDB; 1453481at2759; -.
DR PhylomeDB; Q92882; -.
DR TreeFam; TF314534; -.
DR PathwayCommons; Q92882; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q92882; -.
DR BioGRID-ORCS; 26578; 20 hits in 1072 CRISPR screens.
DR ChiTaRS; OSTF1; human.
DR EvolutionaryTrace; Q92882; -.
DR GeneWiki; OSTF1; -.
DR GenomeRNAi; 26578; -.
DR Pharos; Q92882; Tbio.
DR PRO; PR:Q92882; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q92882; protein.
DR Bgee; ENSG00000134996; Expressed in monocyte and 187 other tissues.
DR Genevisible; Q92882; HS.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ANK repeat; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..214
FT /note="Osteoclast-stimulating factor 1"
FT /id="PRO_0000067035"
FT DOMAIN 12..71
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 72..101
FT /note="ANK 1"
FT REPEAT 105..135
FT /note="ANK 2"
FT REPEAT 139..168
FT /note="ANK 3"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 48
FT /note="N -> S (in dbSNP:rs2295862)"
FT /id="VAR_048309"
FT VARIANT 159
FT /note="L -> F (in dbSNP:rs17850197)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026573"
FT CONFLICT 11
FT /note="P -> PGEG (in Ref. 4; AAH07459)"
FT /evidence="ECO:0000305"
FT CONFLICT 144..145
FT /note="LH -> FD (in Ref. 1; AAB06396)"
FT /evidence="ECO:0000305"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1ZLM"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1ZLM"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1ZLM"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1ZLM"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1ZLM"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1ZLM"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3EHR"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:3EHR"
SQ SEQUENCE 214 AA; 23787 MW; 6C37F3D2B68578C3 CRC64;
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTNWW KGTSKGRTGL
IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHKD
IVEMLFTQPN IELNQQNKLG DTALHAAAWK GYADIVQLLL AKGARTDLRN IEKKLAFDMA
TNAACASLLK KKQGTDAVRT LSNAEDYLDD EDSD
