PPWD1_HUMAN
ID PPWD1_HUMAN Reviewed; 646 AA.
AC Q96BP3; B4DWR9; Q15002; Q7KZ89;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Peptidylprolyl isomerase domain and WD repeat-containing protein 1 {ECO:0000305};
DE EC=5.2.1.8 {ECO:0000269|PubMed:20676357};
DE AltName: Full=Spliceosome-associated cyclophilin {ECO:0000305|PubMed:11991638};
GN Name=PPWD1 {ECO:0000312|HGNC:HGNC:28954};
GN Synonyms=KIAA0073 {ECO:0000312|EMBL:BAA07555.1};
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 MRNA] (ISOFORM 2).
RC TISSUE=Esophagus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone;
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 [LARGE SCALE MRNA] OF 2-646 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 473-646, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18397323; DOI=10.1111/j.1742-4658.2008.06381.x;
RA Davis T.L., Walker J.R., Ouyang H., MacKenzie F., Butler-Cole C.,
RA Newman E.M., Eisenmesser E.Z., Dhe-Paganon S.;
RT "The crystal structure of human WD40 repeat-containing peptidylprolyl
RT isomerase (PPWD1).";
RL FEBS J. 275:2283-2295(2008).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding (PubMed:20676357). May be involved in pre-mRNA splicing
CC (PubMed:11991638). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:20676357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000305|PubMed:20676357}.
CC -!- SUBUNIT: Identified in the spliceosome C complex.
CC {ECO:0000269|PubMed:11991638}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18397323}.
CC Note=Associated with spliceosomal complexes.
CC {ECO:0000269|PubMed:11991638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96BP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BP3-2; Sequence=VSP_055266;
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC subfamily. {ECO:0000305}.
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; AK301654; BAG63131.1; -; mRNA.
DR EMBL; AC008560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015385; AAH15385.1; -; mRNA.
DR EMBL; D38552; BAA07555.1; -; mRNA.
DR CCDS; CCDS3985.1; -. [Q96BP3-1]
DR CCDS; CCDS64162.1; -. [Q96BP3-2]
DR RefSeq; NP_001265855.1; NM_001278926.1.
DR RefSeq; NP_001265856.1; NM_001278927.1.
DR RefSeq; NP_001265858.1; NM_001278929.1. [Q96BP3-2]
DR RefSeq; NP_056157.1; NM_015342.3. [Q96BP3-1]
DR PDB; 2A2N; X-ray; 1.65 A; A/B/C=473-646.
DR PDB; 5YZG; EM; 4.10 A; 2=1-646.
DR PDB; 7A5P; EM; 5.00 A; z=1-646.
DR PDBsum; 2A2N; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 7A5P; -.
DR AlphaFoldDB; Q96BP3; -.
DR SMR; Q96BP3; -.
DR BioGRID; 116971; 46.
DR CORUM; Q96BP3; -.
DR IntAct; Q96BP3; 11.
DR MINT; Q96BP3; -.
DR STRING; 9606.ENSP00000261308; -.
DR GlyGen; Q96BP3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96BP3; -.
DR MetOSite; Q96BP3; -.
DR PhosphoSitePlus; Q96BP3; -.
DR BioMuta; PPWD1; -.
DR DMDM; 74760739; -.
DR EPD; Q96BP3; -.
DR jPOST; Q96BP3; -.
DR MassIVE; Q96BP3; -.
DR MaxQB; Q96BP3; -.
DR PaxDb; Q96BP3; -.
DR PeptideAtlas; Q96BP3; -.
DR PRIDE; Q96BP3; -.
DR ProteomicsDB; 5373; -.
DR ProteomicsDB; 76096; -. [Q96BP3-1]
DR Antibodypedia; 11576; 215 antibodies from 22 providers.
DR DNASU; 23398; -.
DR Ensembl; ENST00000261308.10; ENSP00000261308.4; ENSG00000113593.12. [Q96BP3-1]
DR Ensembl; ENST00000538977.5; ENSP00000444496.1; ENSG00000113593.12. [Q96BP3-2]
DR GeneID; 23398; -.
DR KEGG; hsa:23398; -.
DR MANE-Select; ENST00000261308.10; ENSP00000261308.4; NM_015342.4; NP_056157.1.
DR UCSC; uc003jtv.6; human. [Q96BP3-1]
DR CTD; 23398; -.
DR DisGeNET; 23398; -.
DR GeneCards; PPWD1; -.
DR HGNC; HGNC:28954; PPWD1.
DR HPA; ENSG00000113593; Low tissue specificity.
DR MIM; 618274; gene.
DR neXtProt; NX_Q96BP3; -.
DR OpenTargets; ENSG00000113593; -.
DR PharmGKB; PA142671149; -.
DR VEuPathDB; HostDB:ENSG00000113593; -.
DR eggNOG; KOG0882; Eukaryota.
DR GeneTree; ENSGT00940000158733; -.
DR HOGENOM; CLU_012062_31_2_1; -.
DR InParanoid; Q96BP3; -.
DR OMA; GGMVEYW; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q96BP3; -.
DR TreeFam; TF105686; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; Q96BP3; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q96BP3; -.
DR BioGRID-ORCS; 23398; 745 hits in 1087 CRISPR screens.
DR ChiTaRS; PPWD1; human.
DR EvolutionaryTrace; Q96BP3; -.
DR GenomeRNAi; 23398; -.
DR Pharos; Q96BP3; Tbio.
DR PRO; PR:Q96BP3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96BP3; protein.
DR Bgee; ENSG00000113593; Expressed in calcaneal tendon and 191 other tissues.
DR ExpressionAtlas; Q96BP3; baseline and differential.
DR Genevisible; Q96BP3; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50891; SSF50891; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isomerase;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW Rotamase; Spliceosome; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..646
FT /note="Peptidylprolyl isomerase domain and WD repeat-
FT containing protein 1"
FT /id="PRO_0000240306"
FT REPEAT 80..118
FT /note="WD 1"
FT REPEAT 124..162
FT /note="WD 2"
FT REPEAT 168..208
FT /note="WD 3"
FT REPEAT 213..252
FT /note="WD 4"
FT REPEAT 271..309
FT /note="WD 5"
FT REPEAT 345..386
FT /note="WD 6"
FT REPEAT 401..453
FT /note="WD 7"
FT DOMAIN 490..645
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..156
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055266"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:2A2N"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:2A2N"
FT HELIX 513..524
FT /evidence="ECO:0007829|PDB:2A2N"
FT TURN 525..530
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:2A2N"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 592..597
FT /evidence="ECO:0007829|PDB:2A2N"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:2A2N"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:2A2N"
FT HELIX 616..623
FT /evidence="ECO:0007829|PDB:2A2N"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:2A2N"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:2A2N"
SQ SEQUENCE 646 AA; 73575 MW; 4DEFA1C78F914430 CRC64;
MAAESGSDFQ QRRRRRRDPE EPEKTELSER ELAVAVAVSQ ENDEENEERW VGPLPVEATL
AKKRKVLEFE RVYLDNLPSA SMYERSYMHR DVITHVVCTK TDFIITASHD GHVKFWKKIE
EGIEFVKHFR SHLGVIESIA VSSEGALFCS VGDDKAMKVF DVVNFDMINM LKLGYFPGQC
EWIYCPGDAI SSVAASEKST GKIFIYDGRG DNQPLHIFDK LHTSPLTQIR LNPVYKAVVS
SDKSGMIEYW TGPPHEYKFP KNVNWEYKTD TDLYEFAKCK AYPTSVCFSP DGKKIATIGS
DRKVRIFRFV TGKLMRVFDE SLSMFTELQQ MRQQLPDMEF GRRMAVEREL EKVDAVRLIN
IVFDETGHFV LYGTMLGIKV INVETNRCVR ILGKQENIRV MQLALFQGIA KKHRAATTIE
MKASENPVLQ NIQADPTIVC TSFKKNRFYM FTKREPEDTK SADSDRDVFN EKPSKEEVMA
ATQAEGPKRV SDSAIIHTSM GDIHTKLFPV ECPKTVENFC VHSRNGYYNG HTFHRIIKGF
MIQTGDPTGT GMGGESIWGG EFEDEFHSTL RHDRPYTLSM ANAGSNTNGS QFFITVVPTP
WLDNKHTVFG RVTKGMEVVQ RISNVKVNPK TDKPYEDVSI INITVK
