PDCL3_HUMAN
ID PDCL3_HUMAN Reviewed; 239 AA.
AC Q9H2J4; B2RA00; Q53S68;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosducin-like protein 3;
DE AltName: Full=HTPHLP;
DE AltName: Full=PhPL3;
DE AltName: Full=Viral IAP-associated factor 1 {ECO:0000303|PubMed:15371430};
DE Short=VIAF-1 {ECO:0000303|PubMed:15371430};
GN Name=PDCL3; Synonyms=PhLP2A, VIAF1;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PHOSPHORYLATION.
RC TISSUE=B-cell;
RX PubMed=15371430; DOI=10.1074/jbc.m409623200;
RA Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E., Rumble J.M.,
RA Balliu B., Duckett C.S.;
RT "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that
RT modulates caspase activation.";
RL J. Biol. Chem. 279:51091-51099(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP FUNCTION, AND INTERACTION WITH CCT COMPLEX.
RX PubMed=17429077; DOI=10.1091/mbc.e07-01-0069;
RA Stirling P.C., Srayko M., Takhar K.S., Pozniakovsky A., Hyman A.A.,
RA Leroux M.R.;
RT "Functional interaction between phosducin-like protein 2 and cytosolic
RT chaperonin is essential for cytoskeletal protein function and cell cycle
RT progression.";
RL Mol. Biol. Cell 18:2336-2345(2007).
RN [8]
RP INTERACTION WITH XIAP.
RX PubMed=19012568; DOI=10.1111/j.1747-0285.2008.00719.x;
RA Bisson W.H., Zhang Z., Welsh K., Huang J.W., Ryan J., Reed J.C.,
RA Pellecchia M.;
RT "Binding properties of the C-terminal domain of VIAF.";
RL Chem. Biol. Drug Des. 72:331-336(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
RP IDENTIFICATION BY 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-234 AND SER-236, 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 [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-234 AND SER-236, 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 [13]
RP FUNCTION, AND INTERACTION WITH KDR/VEGFR2.
RX PubMed=23792958; DOI=10.1074/jbc.m113.473173;
RA Srinivasan S., Meyer R.D., Lugo R., Rahimi N.;
RT "Identification of PDCL3 as a novel chaperone protein involved in the
RT generation of functional VEGF receptor 2.";
RL J. Biol. Chem. 288:23171-23181(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH KDR,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACETYLATION AT MET-1, AND
RP MUTAGENESIS OF MET-1.
RX PubMed=26059764; DOI=10.1007/s10456-015-9468-3;
RA Srinivasan S., Chitalia V., Meyer R.D., Hartsough E., Mehta M., Harrold I.,
RA Anderson N., Feng H., Smith L.E., Jiang Y., Costello C.E., Rahimi N.;
RT "Hypoxia-induced expression of phosducin-like 3 regulates expression of
RT VEGFR-2 and promotes angiogenesis.";
RL Angiogenesis 18:449-462(2015).
CC -!- FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor
CC KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination
CC and degradation (PubMed:23792958, PubMed:26059764). Inhibits the
CC folding activity of the chaperonin-containing T-complex (CCT) which
CC leads to inhibition of cytoskeletal actin folding (PubMed:17429077).
CC Acts as a chaperone during heat shock alongside HSP90 and HSP40/70
CC chaperone complexes (By similarity). Modulates the activation of
CC caspases during apoptosis (PubMed:15371430).
CC {ECO:0000250|UniProtKB:Q4KLJ8, ECO:0000269|PubMed:15371430,
CC ECO:0000269|PubMed:17429077, ECO:0000269|PubMed:23792958,
CC ECO:0000269|PubMed:26059764}.
CC -!- SUBUNIT: Interacts (via thioredoxin fold region) with KDR/VEGFR2 (via
CC juxtamembrane domain) (PubMed:23792958, PubMed:26059764). Forms ternary
CC complexes with the chaperonin CCT complex and actin substrate, leading
CC to inhibition of actin folding (PubMed:17429077). Interacts with XIAP
CC (via BIR 3 and RING domain) (PubMed:19012568). Interacts with HSP90AA1
CC and HSP90AB1 (By similarity). {ECO:0000250|UniProtKB:Q4KLJ8,
CC ECO:0000269|PubMed:17429077, ECO:0000269|PubMed:19012568,
CC ECO:0000269|PubMed:23792958, ECO:0000269|PubMed:26059764}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15371430,
CC ECO:0000269|PubMed:26059764}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:26059764}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:26059764}.
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells (at protein level)
CC (PubMed:26059764). Expressed in all tissues examined including spleen,
CC thymus, prostate, testis, ovary, small intestine and colon
CC (PubMed:15371430). {ECO:0000269|PubMed:15371430,
CC ECO:0000269|PubMed:26059764}.
CC -!- PTM: N-terminal methionine acetylation destabilizes the protein.
CC {ECO:0000269|PubMed:26059764}.
CC -!- SIMILARITY: Belongs to the phosducin family. {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; AF110511; AAG21887.1; -; mRNA.
DR EMBL; AF267853; AAG44722.1; -; mRNA.
DR EMBL; AK313985; BAG36697.1; -; mRNA.
DR EMBL; AC068538; AAX93227.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01838.1; -; Genomic_DNA.
DR EMBL; BC001021; AAH01021.1; -; mRNA.
DR CCDS; CCDS33261.1; -.
DR RefSeq; NP_076970.1; NM_024065.4.
DR PDB; 7NVM; EM; 3.10 A; P=1-239.
DR PDBsum; 7NVM; -.
DR AlphaFoldDB; Q9H2J4; -.
DR BMRB; Q9H2J4; -.
DR SMR; Q9H2J4; -.
DR BioGRID; 122497; 103.
DR IntAct; Q9H2J4; 21.
DR MINT; Q9H2J4; -.
DR STRING; 9606.ENSP00000264254; -.
DR BindingDB; Q9H2J4; -.
DR iPTMnet; Q9H2J4; -.
DR MetOSite; Q9H2J4; -.
DR PhosphoSitePlus; Q9H2J4; -.
DR BioMuta; PDCL3; -.
DR DMDM; 50401164; -.
DR EPD; Q9H2J4; -.
DR jPOST; Q9H2J4; -.
DR MassIVE; Q9H2J4; -.
DR MaxQB; Q9H2J4; -.
DR PaxDb; Q9H2J4; -.
DR PeptideAtlas; Q9H2J4; -.
DR PRIDE; Q9H2J4; -.
DR ProteomicsDB; 80555; -.
DR TopDownProteomics; Q9H2J4; -.
DR Antibodypedia; 17722; 188 antibodies from 26 providers.
DR DNASU; 79031; -.
DR Ensembl; ENST00000264254.11; ENSP00000264254.6; ENSG00000115539.14.
DR GeneID; 79031; -.
DR KEGG; hsa:79031; -.
DR MANE-Select; ENST00000264254.11; ENSP00000264254.6; NM_024065.5; NP_076970.1.
DR UCSC; uc002tao.3; human.
DR CTD; 79031; -.
DR DisGeNET; 79031; -.
DR GeneCards; PDCL3; -.
DR HGNC; HGNC:28860; PDCL3.
DR HPA; ENSG00000115539; Low tissue specificity.
DR MIM; 611678; gene.
DR neXtProt; NX_Q9H2J4; -.
DR OpenTargets; ENSG00000115539; -.
DR PharmGKB; PA134979849; -.
DR VEuPathDB; HostDB:ENSG00000115539; -.
DR eggNOG; KOG3170; Eukaryota.
DR GeneTree; ENSGT00940000154295; -.
DR HOGENOM; CLU_072604_0_0_1; -.
DR InParanoid; Q9H2J4; -.
DR OMA; QKPDYSR; -.
DR OrthoDB; 1247977at2759; -.
DR PhylomeDB; Q9H2J4; -.
DR TreeFam; TF315179; -.
DR PathwayCommons; Q9H2J4; -.
DR SignaLink; Q9H2J4; -.
DR BioGRID-ORCS; 79031; 106 hits in 1073 CRISPR screens.
DR ChiTaRS; PDCL3; human.
DR GenomeRNAi; 79031; -.
DR Pharos; Q9H2J4; Tbio.
DR PRO; PR:Q9H2J4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H2J4; protein.
DR Bgee; ENSG00000115539; Expressed in gastrocnemius and 103 other tissues.
DR ExpressionAtlas; Q9H2J4; baseline and differential.
DR Genevisible; Q9H2J4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097356; C:perinucleolar compartment; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0044183; F:protein folding chaperone; IMP:UniProtKB.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:UniProtKB.
DR GO; GO:1903645; P:negative regulation of chaperone-mediated protein folding; IMP:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02114; Phosducin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Angiogenesis; Apoptosis; Chaperone; Cytoplasm;
KW Endoplasmic reticulum; Phosphoprotein; Reference proteome.
FT CHAIN 1..239
FT /note="Phosducin-like protein 3"
FT /id="PRO_0000163758"
FT REGION 91..239
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT REGION 97..99
FT /note="Interaction with XIAP"
FT /evidence="ECO:0000269|PubMed:19012568"
FT REGION 153..155
FT /note="Interaction with XIAP"
FT /evidence="ECO:0000269|PubMed:19012568"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:26059764"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MUTAGEN 1
FT /note="Missing: Loss of acetylation. Increases protein
FT stability."
FT /evidence="ECO:0000269|PubMed:26059764"
SQ SEQUENCE 239 AA; 27614 MW; D54900B9EEE3A1FB CRC64;
MQDPNADTEW NDILRKKGIL PPKESLKELE EEAEEEQRIL QQSVVKTYED MTLEELEDHE
DEFNEEDERA IEMYRRRRLA EWKATKLKNK FGEVLEISGK DYVQEVTKAG EGLWVILHLY
KQGIPLCALI NQHLSGLARK FPDVKFIKAI STTCIPNYPD RNLPTIFVYL EGDIKAQFIG
PLVFGGMNLT RDELEWKLSE SGAIMTDLEE NPKKPIEDVL LSSVRRSVLM KRDSDSEGD
