TFPI2_HUMAN
ID TFPI2_HUMAN Reviewed; 235 AA.
AC P48307; Q66ME8; Q8NAK6; Q9UC86;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Tissue factor pathway inhibitor 2;
DE Short=TFPI-2;
DE AltName: Full=Placental protein 5;
DE Short=PP5;
DE Flags: Precursor;
GN Name=TFPI2;
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), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=7896752; DOI=10.1093/oxfordjournals.jbchem.a124648;
RA Miyagi Y., Koshikawa N., Yasumitsu H., Miyagi E., Hirahara F., Aoki I.,
RA Misugi K., Umeda M., Miyazaki K.;
RT "cDNA cloning and mRNA expression of a serine proteinase inhibitor secreted
RT by cancer cells: identification as placental protein 5 and tissue factor
RT pathway inhibitor-2.";
RL J. Biochem. 116:939-942(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8159751; DOI=10.1073/pnas.91.8.3353;
RA Sprecher C.A., Kisiel W., Mathewes S., Foster D.C.;
RT "Molecular cloning, expression, and partial characterization of a second
RT human tissue-factor-pathway inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3353-3357(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11342222; DOI=10.1016/s0167-4781(00)00298-0;
RA Kamei S., Kazama Y., Kuijper J.L., Foster D.C., Kisiel W.;
RT "Genomic structure and promoter activity of the human tissue factor pathway
RT inhibitor-2 gene.";
RL Biochim. Biophys. Acta 1517:430-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Xu Y., Li T., Du G.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 23-42, AND FUNCTION.
RC TISSUE=Fibroblast;
RX PubMed=7872799; DOI=10.1006/abbi.1995.1168;
RA Rao C.N., Liu Y.Y., Peavey C.L., Woodley D.T.;
RT "Novel extracellular matrix-associated serine proteinase inhibitors from
RT human skin fibroblasts.";
RL Arch. Biochem. Biophys. 317:311-314(1995).
RN [11]
RP PROTEIN SEQUENCE OF 23-35; 47-53 AND 133-146.
RC TISSUE=Placenta;
RX PubMed=3276312; DOI=10.1016/0006-291x(88)90546-3;
RA Buetzow R., Huhtala M.-L., Bohn H., Virtanen I., Seppaelae M.;
RT "Purification and characterization of placental protein 5.";
RL Biochem. Biophys. Res. Commun. 150:483-490(1988).
RN [12]
RP ERRATUM OF PUBMED:3276312.
RA Buetzow R., Huhtala M.-L., Bohn H., Virtanen I., Seppaelae M.;
RL Biochem. Biophys. Res. Commun. 151:630-631(1988).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-90 IN COMPLEX WITH BOVINE
RP TRYPSIN, AND DISULFIDE BONDS.
RX PubMed=15932872; DOI=10.1074/jbc.m504105200;
RA Schmidt A.E., Chand H.S., Cascio D., Kisiel W., Bajaj S.P.;
RT "Crystal structure of Kunitz domain 1 (KD1) of tissue factor pathway
RT inhibitor-2 in complex with trypsin. Implications for KD1 specificity of
RT inhibition.";
RL J. Biol. Chem. 280:27832-27838(2005).
RN [14]
RP INTERACTION WITH PPP2R3C.
RX PubMed=24333728; DOI=10.1016/j.canlet.2013.12.007;
RA Katayama K., Yamaguchi M., Noguchi K., Sugimoto Y.;
RT "Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-
RT glycoprotein/ABCB1 and down-regulates the expression and function.";
RL Cancer Lett. 345:124-131(2014).
CC -!- FUNCTION: May play a role in the regulation of plasmin-mediated matrix
CC remodeling. Inhibits trypsin, plasmin, factor VIIa/tissue factor and
CC weakly factor Xa. Has no effect on thrombin.
CC {ECO:0000269|PubMed:7872799}.
CC -!- SUBUNIT: Finds in a complex with ABCB1, TFPI2 and PPP2R3C; leading to
CC the dephosphorylation of ABCB1. {ECO:0000269|PubMed:24333728}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48307-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48307-2; Sequence=VSP_056031;
CC -!- TISSUE SPECIFICITY: Umbilical vein endothelial cells, liver, placenta,
CC heart, pancreas, and maternal serum at advanced pregnancy.
CC -!- DOMAIN: This inhibitor contains three inhibitory domains.
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DR EMBL; D29992; BAA06272.1; -; mRNA.
DR EMBL; L27624; AAA20094.1; -; mRNA.
DR EMBL; AF217542; AAK13254.1; -; Genomic_DNA.
DR EMBL; AY691946; AAU04568.1; -; mRNA.
DR EMBL; AK092499; BAC03906.1; -; mRNA.
DR EMBL; AK313260; BAG36070.1; -; mRNA.
DR EMBL; AC002076; AAS02022.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24140.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76809.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76811.1; -; Genomic_DNA.
DR EMBL; BC005330; AAH05330.1; -; mRNA.
DR CCDS; CCDS5632.1; -. [P48307-1]
DR PIR; A54951; A54951.
DR PIR; S71593; S71593.
DR RefSeq; NP_001257932.1; NM_001271003.1. [P48307-2]
DR RefSeq; NP_006519.1; NM_006528.3. [P48307-1]
DR PDB; 1ZR0; X-ray; 1.80 A; B/D=28-90.
DR PDBsum; 1ZR0; -.
DR AlphaFoldDB; P48307; -.
DR SMR; P48307; -.
DR BioGRID; 113693; 42.
DR CORUM; P48307; -.
DR IntAct; P48307; 2.
DR MINT; P48307; -.
DR STRING; 9606.ENSP00000222543; -.
DR MEROPS; I02.013; -.
DR MEROPS; I02.014; -.
DR MEROPS; I02.951; -.
DR GlyGen; P48307; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P48307; -.
DR PhosphoSitePlus; P48307; -.
DR BioMuta; TFPI2; -.
DR DMDM; 1351226; -.
DR jPOST; P48307; -.
DR MassIVE; P48307; -.
DR MaxQB; P48307; -.
DR PaxDb; P48307; -.
DR PeptideAtlas; P48307; -.
DR PRIDE; P48307; -.
DR ProteomicsDB; 55875; -. [P48307-1]
DR Antibodypedia; 4115; 537 antibodies from 34 providers.
DR DNASU; 7980; -.
DR Ensembl; ENST00000222543.11; ENSP00000222543.5; ENSG00000105825.14. [P48307-1]
DR GeneID; 7980; -.
DR KEGG; hsa:7980; -.
DR MANE-Select; ENST00000222543.11; ENSP00000222543.5; NM_006528.4; NP_006519.1.
DR UCSC; uc003umy.2; human. [P48307-1]
DR CTD; 7980; -.
DR DisGeNET; 7980; -.
DR GeneCards; TFPI2; -.
DR HGNC; HGNC:11761; TFPI2.
DR HPA; ENSG00000105825; Tissue enriched (placenta).
DR MIM; 600033; gene.
DR neXtProt; NX_P48307; -.
DR OpenTargets; ENSG00000105825; -.
DR PharmGKB; PA36476; -.
DR VEuPathDB; HostDB:ENSG00000105825; -.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000159917; -.
DR HOGENOM; CLU_058441_1_0_1; -.
DR InParanoid; P48307; -.
DR OrthoDB; 1009074at2759; -.
DR PhylomeDB; P48307; -.
DR TreeFam; TF315349; -.
DR PathwayCommons; P48307; -.
DR SignaLink; P48307; -.
DR BioGRID-ORCS; 7980; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; TFPI2; human.
DR EvolutionaryTrace; P48307; -.
DR GeneWiki; TFPI2; -.
DR GenomeRNAi; 7980; -.
DR Pharos; P48307; Tbio.
DR PRO; PR:P48307; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P48307; protein.
DR Bgee; ENSG00000105825; Expressed in stromal cell of endometrium and 126 other tissues.
DR ExpressionAtlas; P48307; baseline and differential.
DR Genevisible; P48307; HS.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR CDD; cd00109; KU; 2.
DR Gene3D; 4.10.410.10; -; 3.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR008296; TFPI-like.
DR InterPro; IPR029860; TFPI2.
DR PANTHER; PTHR10083:SF352; PTHR10083:SF352; 1.
DR Pfam; PF00014; Kunitz_BPTI; 3.
DR PIRSF; PIRSF001620; TFPI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 3.
DR SUPFAM; SSF57362; SSF57362; 3.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
KW Protease inhibitor; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3276312,
FT ECO:0000269|PubMed:7872799"
FT CHAIN 23..235
FT /note="Tissue factor pathway inhibitor 2"
FT /id="PRO_0000016876"
FT DOMAIN 36..86
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 96..149
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 158..208
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 46..47
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 107..108
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 168..169
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:15932872"
FT DISULFID 45..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:15932872"
FT DISULFID 61..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000269|PubMed:15932872"
FT DISULFID 96..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 106..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 122..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 158..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 167..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 183..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT VAR_SEQ 30..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056031"
FT VARIANT 102
FT /note="V -> A (in dbSNP:rs1804202)"
FT /id="VAR_012005"
FT VARIANT 231
FT /note="R -> Q (in dbSNP:rs12669450)"
FT /id="VAR_050064"
FT CONFLICT 23
FT /note="D -> A (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="D -> G (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="C -> I (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="Y -> R (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1ZR0"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1ZR0"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:1ZR0"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1ZR0"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1ZR0"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:1ZR0"
SQ SEQUENCE 235 AA; 26934 MW; 975ABA5C53F7C65F CRC64;
MDPARPLGLS ILLLFLTEAA LGDAAQEPTG NNAEICLLPL DYGPCRALLL RYYYDRYTQS
CRQFLYGGCE GNANNFYTWE ACDDACWRIE KVPKVCRLQV SVDDQCEGST EKYFFNLSSM
TCEKFFSGGC HRNRIENRFP DEATCMGFCA PKKIPSFCYS PKDEGLCSAN VTRYYFNPRY
RTCDAFTYTG CGGNDNNFVS REDCKRACAK ALKKKKKMPK LRFASRIRKI RKKQF
