TPP2_HUMAN
ID TPP2_HUMAN Reviewed; 1249 AA.
AC P29144; Q5VZU8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Tripeptidyl-peptidase 2;
DE Short=TPP-2;
DE EC=3.4.14.10 {ECO:0000269|PubMed:25525876, ECO:0000269|PubMed:30533531};
DE AltName: Full=Tripeptidyl aminopeptidase;
DE AltName: Full=Tripeptidyl-peptidase II;
DE Short=TPP-II;
GN Name=TPP2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-55, AND PROTEIN SEQUENCE OF 6-26.
RX PubMed=1840501;
RA Tomkinson B.;
RT "Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl
RT peptidase II.";
RL Biomed. Biochim. Acta 50:727-729(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-1249.
RC TISSUE=Lymphocyte;
RX PubMed=1670990; DOI=10.1021/bi00215a025;
RA Tomkinson B., Jonsson A.-K.;
RT "Characterization of cDNA for human tripeptidyl peptidase II: the N-
RT terminal part of the enzyme is similar to subtilisin.";
RL Biochemistry 30:168-174(1991).
RN [6]
RP PROTEIN SEQUENCE OF 2-18 AND 1036-1046, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Quadroni M.;
RL Submitted (JUL-2005) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 13-26; 1099-1118 AND 440-450.
RX PubMed=1691635; DOI=10.1042/bj2670149;
RA Tomkinson B., Zetterqvist O.;
RT "Immunological cross-reactivity between human tripeptidyl peptidase II and
RT fibronectin.";
RL Biochem. J. 267:149-154(1990).
RN [8]
RP PROTEIN SEQUENCE OF 441-450.
RX PubMed=3313395; DOI=10.1073/pnas.84.21.7508;
RA Tomkinson B., Wernstedt C., Hellman U., Zetterqvist O.;
RT "Active site of tripeptidyl peptidase II from human erythrocytes is of the
RT subtilisin type.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7508-7512(1987).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19747897; DOI=10.1016/j.bbrc.2009.09.021;
RA Preta G., de Klark R., Glas R.;
RT "A role for nuclear translocation of tripeptidyl-peptidase II in reactive
RT oxygen species-dependent DNA damage responses.";
RL Biochem. Biophys. Res. Commun. 389:575-579(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, 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 [13]
RP INVOLVEMENT IN IMD78, VARIANTS IMD78 ASP-500 AND 781-TYR--PHE-1249 DEL,
RP CHARACTERIZATION OF VARIANTS IMD78 ASP-500 AND 781-TYR--PHE-1249 DEL,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25525876; DOI=10.1016/j.cell.2014.12.001;
RA Lu W., Zhang Y., McDonald D.O., Jing H., Carroll B., Robertson N.,
RA Zhang Q., Griffin H., Sanderson S., Lakey J.H., Morgan N.V., Reynard L.N.,
RA Zheng L., Murdock H.M., Turvey S.E., Hackett S.J., Prestidge T., Hall J.M.,
RA Cant A.J., Matthews H.F., Koref M.F., Simon A.K., Korolchuk V.I.,
RA Lenardo M.J., Hambleton S., Su H.C.;
RT "Dual proteolytic pathways govern glycolysis and immune competence.";
RL Cell 159:1578-1590(2014).
RN [14]
RP VARIANTS GLY-28 AND ILE-676, CHARACTERIZATION OF VARIANT GLY-28, FUNCTION,
RP AND CATALYTIC ACTIVITY.
RX PubMed=30533531; DOI=10.1212/nxg.0000000000000285;
RA Reinthaler E.M., Graf E., Zrzavy T., Wieland T., Hotzy C., Kopecky C.,
RA Pferschy S., Schmied C., Leutmezer F., Keilani M., Lill C.M., Hoffjan S.,
RA Epplen J.T., Zettl U.K., Hecker M., Deutschlaender A., Meuth S.G.,
RA Ahram M., Mustafa B., El-Khateeb M., Vilarino-Gueell C., Sadovnick A.D.,
RA Zimprich F., Tomkinson B., Strom T., Kristoferitsch W., Lassmann H.,
RA Zimprich A.;
RT "TPP2 mutation associated with sterile brain inflammation mimicking MS.";
RL Neurol. Genet. 4:e285-e285(2018).
CC -!- FUNCTION: Cytosolic tripeptidyl-peptidase that releases N-terminal
CC tripeptides from polypeptides and is a component of the proteolytic
CC cascade acting downstream of the 26S proteasome in the ubiquitin-
CC proteasome pathway (PubMed:25525876, PubMed:30533531). It plays an
CC important role in intracellular amino acid homeostasis
CC (PubMed:25525876). Stimulates adipogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q64514, ECO:0000269|PubMed:25525876,
CC ECO:0000269|PubMed:30533531}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000269|PubMed:25525876,
CC ECO:0000269|PubMed:30533531};
CC -!- INTERACTION:
CC P29144; Q08426: EHHADH; NbExp=5; IntAct=EBI-1044672, EBI-2339219;
CC P29144; P06746: POLB; NbExp=8; IntAct=EBI-1044672, EBI-713836;
CC P29144; Q96I34: PPP1R16A; NbExp=4; IntAct=EBI-1044672, EBI-710402;
CC P29144; P29144: TPP2; NbExp=2; IntAct=EBI-1044672, EBI-1044672;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19747897}. Nucleus
CC {ECO:0000269|PubMed:19747897}. Note=Translocates to the nucleus in
CC response to gamma-irradiation.
CC -!- DISEASE: Immunodeficiency 78 with autoimmunity and developmental delay
CC (IMD78) [MIM:619220]: An autosomal recessive disorder characterized by
CC immune dysregulation, increased susceptibility to bacterial, viral and
CC fungal infections, recurrent sinopulmonary or skin infections, and
CC autoimmune abnormalities including hemolytic anemia and autoimmune
CC cytopenias. Patients also have global developmental delay with speech
CC delay and variable intellectual disability. Disease onset is in infancy
CC or early childhood. {ECO:0000269|PubMed:25525876}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The limitation of proteolytic products to tripeptides is
CC achieved by tailoring the size of the substrate-binding cleft: the two
CC negatively charged residues Glu-305 and Glu-331 that are blocking
CC position P4 limit the number of residues that can be accommodated in
CC the binding cleft and thus create a molecular ruler. At the same time,
CC they orient substrates so that the tripeptides are removed exclusively
CC from the N-terminus (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AL158063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09059.1; -; Genomic_DNA.
DR EMBL; BC039905; AAH39905.1; -; mRNA.
DR EMBL; M73047; AAA36760.1; -; mRNA.
DR EMBL; M55169; AAA63263.1; -; mRNA.
DR CCDS; CCDS9502.1; -.
DR PIR; S54376; S54376.
DR RefSeq; NP_001317517.1; NM_001330588.1.
DR RefSeq; NP_003282.2; NM_003291.3.
DR AlphaFoldDB; P29144; -.
DR SMR; P29144; -.
DR BioGRID; 113027; 91.
DR DIP; DIP-50761N; -.
DR IntAct; P29144; 34.
DR MINT; P29144; -.
DR STRING; 9606.ENSP00000365233; -.
DR BindingDB; P29144; -.
DR ChEMBL; CHEMBL6156; -.
DR GuidetoPHARMACOLOGY; 2423; -.
DR MEROPS; S08.A56; -.
DR GlyGen; P29144; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P29144; -.
DR MetOSite; P29144; -.
DR PhosphoSitePlus; P29144; -.
DR SwissPalm; P29144; -.
DR BioMuta; TPP2; -.
DR DMDM; 34223721; -.
DR EPD; P29144; -.
DR jPOST; P29144; -.
DR MassIVE; P29144; -.
DR MaxQB; P29144; -.
DR PaxDb; P29144; -.
DR PeptideAtlas; P29144; -.
DR PRIDE; P29144; -.
DR ProteomicsDB; 54528; -.
DR Antibodypedia; 11138; 138 antibodies from 26 providers.
DR DNASU; 7174; -.
DR Ensembl; ENST00000376065.8; ENSP00000365233.4; ENSG00000134900.12.
DR GeneID; 7174; -.
DR KEGG; hsa:7174; -.
DR UCSC; uc001vpi.5; human.
DR CTD; 7174; -.
DR DisGeNET; 7174; -.
DR GeneCards; TPP2; -.
DR HGNC; HGNC:12016; TPP2.
DR HPA; ENSG00000134900; Low tissue specificity.
DR MalaCards; TPP2; -.
DR MIM; 190470; gene.
DR MIM; 619220; phenotype.
DR neXtProt; NX_P29144; -.
DR OpenTargets; ENSG00000134900; -.
DR Orphanet; 444463; Autoimmune hemolytic anemia-autoimmune thrombocytopenia-primary immunodeficiency syndrome.
DR PharmGKB; PA36695; -.
DR VEuPathDB; HostDB:ENSG00000134900; -.
DR eggNOG; KOG1114; Eukaryota.
DR GeneTree; ENSGT00390000014623; -.
DR HOGENOM; CLU_003084_1_0_1; -.
DR InParanoid; P29144; -.
DR OrthoDB; 156304at2759; -.
DR PhylomeDB; P29144; -.
DR TreeFam; TF105647; -.
DR BRENDA; 3.4.14.10; 2681.
DR PathwayCommons; P29144; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P29144; -.
DR BioGRID-ORCS; 7174; 231 hits in 1077 CRISPR screens.
DR ChiTaRS; TPP2; human.
DR GeneWiki; Tripeptidyl_peptidase_II; -.
DR GenomeRNAi; 7174; -.
DR Pharos; P29144; Tchem.
DR PRO; PR:P29144; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P29144; protein.
DR Bgee; ENSG00000134900; Expressed in left testis and 200 other tissues.
DR ExpressionAtlas; P29144; baseline and differential.
DR Genevisible; P29144; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004177; F:aminopeptidase activity; IMP:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0080144; P:amino acid homeostasis; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 3.40.50.200; -; 2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR022229; Peptidase_S8A_TPPII.
DR InterPro; IPR034051; TPP_II_domain.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminopeptidase; Cytoplasm; Direct protein sequencing;
KW Disease variant; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Serine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..1249
FT /note="Tripeptidyl-peptidase 2"
FT /id="PRO_0000076422"
FT DOMAIN 9..508
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 998..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 449
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64514"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 28
FT /note="C -> G (found in a patient diagnosed with multiple
FT sclerosis; unknown pathological significance; decreased
FT protein abundance; not changed aminopeptidase activity)"
FT /evidence="ECO:0000269|PubMed:30533531"
FT /id="VAR_085640"
FT VARIANT 500
FT /note="G -> D (in IMD78; decreased protein abundance;
FT decreased aminopeptidase activity)"
FT /evidence="ECO:0000269|PubMed:25525876"
FT /id="VAR_085641"
FT VARIANT 676
FT /note="T -> I (found in a patient diagnosed with multiple
FT sclerosis; unknown pathological significance;
FT dbSNP:rs760347832)"
FT /evidence="ECO:0000269|PubMed:30533531"
FT /id="VAR_085642"
FT VARIANT 781..1249
FT /note="Missing (in IMD78; loss of expression)"
FT /evidence="ECO:0000269|PubMed:25525876"
FT /id="VAR_085643"
FT CONFLICT 252
FT /note="G -> R (in Ref. 5; AAA36760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1249 AA; 138350 MW; A26A6249DBF7F3DD CRC64;
MATAATEEPF PFHGLLPKKE TGAASFLCRY PEYDGRGVLI AVLDTGVDPG APGMQVTTDG
KPKIVDIIDT TGSGDVNTAT EVEPKDGEIV GLSGRVLKIP ASWTNPSGKY HIGIKNGYDF
YPKALKERIQ KERKEKIWDP VHRVALAEAC RKQEEFDVAN NGSSQANKLI KEELQSQVEL
LNSFEKKYSD PGPVYDCLVW HDGEVWRACI DSNEDGDLSK STVLRNYKEA QEYGSFGTAE
MLNYSVNIYD DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR
LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW KHNIIYVSSA
GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE KLPANQYTWS SRGPSADGAL
GVSISAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LILSGLKANN IDYTVHSVRR
ALENTAVKAD NIEVFAQGHG IIQVDKAYDY LVQNTSFANK LGFTVTVGNN RGIYLRDPVQ
VAAPSDHGVG IEPVFPENTE NSEKISLQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD
PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT DVHFKPGQIR
RHFIEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA YRSHEFYKFC SLPEKGTLTE
AFPVLGGKAI EFCIARWWAS LSDVNIDYTI SFHGIVCTAP QLNIHASEGI NRFDVQSSLK
YEDLAPCITL KNWVQTLRPV SAKTKPLGSR DVLPNNRQLY EMVLTYNFHQ PKSGEVTPSC
PLLCELLYES EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL
ERLKDLPFIV SHRLSNTLSL DIHENHSFAL LGKKKSSNLT LPPKYNQPFF VTSLPDDKIP
KGAGPGCYLA GSLTLSKTEL GKKADVIPVH YYLIPPPTKT KNGSKDKEKD SEKEKDLKEE
FTEALRDLKI QWMTKLDSSD IYNELKETYP NYLPLYVARL HQLDAEKERM KRLNEIVDAA
NAVISHIDQT ALAVYIAMKT DPRPDAATIK NDMDKQKSTL VDALCRKGCA LADHLLHTQA
QDGAISTDAE GKEEEGESPL DSLAETFWET TKWTDLFDNK VLTFAYKHAL VNKMYGRGLK
FATKLVEEKP TKENWKNCIQ LMKLLGWTHC ASFTENWLPI MYPPDYCVF
