ID DPEP2_HUMAN Reviewed; 486 AA. AC Q9H4A9; A0A024R6Y5; B2RCF8; B3KS59; I3L248; Q6UX92; Q8TC95; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 27-MAR-2024, entry version 165. DE RecName: Full=Dipeptidase 2; DE EC=3.4.13.19 {ECO:0000269|PubMed:32325220}; DE Flags: Precursor; GN Name=DPEP2; ORFNames=UNQ284/PRO323; 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). RC TISSUE=Uterus; RA Chen J.M., Fortunato M., Barrett A.J.; RT "Cloning and sequencing of a human homologue of renal membrane RT dipeptidase."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-486 (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111 AND ASN-235. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [8] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=32325220; DOI=10.1016/j.jsb.2020.107512; RA Hayashi K., Longenecker K.L., Koenig P., Prashar A., Hampl J., Stoll V., RA Vivona S.; RT "Structure of human DPEP3 in complex with the SC-003 antibody Fab fragment RT reveals basis for lack of dipeptidase activity."; RL J. Struct. Biol. 211:107512-107512(2020). CC -!- FUNCTION: Dipeptidase that hydrolyzes leukotriene D4 (LTD4) into CC leukotriene E4 (LTE4) (PubMed:32325220). Hydrolyzes cystinyl-bis- CC glycine (PubMed:32325220). {ECO:0000269|PubMed:32325220}. CC -!- FUNCTION: Independently of its dipeptidase activity can also modulate CC macrophage inflammatory response by acting as a regulator of NF-kappaB CC inflammatory signaling pathway. {ECO:0000250|UniProtKB:Q8C255}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; CC Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, CC ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10073, ECO:0000269|PubMed:32325220}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + leukotriene D4 = glycine + leukotriene E4; CC Xref=Rhea:RHEA:48616, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:57462, ChEBI:CHEBI:63166; CC Evidence={ECO:0000269|PubMed:32325220}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48617; CC Evidence={ECO:0000305|PubMed:32325220}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O + L-cystine-bis-glycine = 2 glycine + L-cystine; CC Xref=Rhea:RHEA:60520, ChEBI:CHEBI:15377, ChEBI:CHEBI:35491, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:143812; CC Evidence={ECO:0000269|PubMed:32325220}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P16444, ECO:0000255|PROSITE- CC ProRule:PRU10073}; CC -!- ACTIVITY REGULATION: Inhibited by L-penicillamine. CC {ECO:0000250|UniProtKB:Q8C255}. CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000255|PROSITE- CC ProRule:PRU10073}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8C255}; Lipid- CC anchor, GPI-anchor {ECO:0000250|UniProtKB:Q8C255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H4A9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H4A9-2; Sequence=VSP_017851; CC Name=3; CC IsoId=Q9H4A9-3; Sequence=VSP_059428, VSP_059429; CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ88819.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AJ295149; CAC14667.1; -; mRNA. DR EMBL; AK092884; BAG52621.1; -; mRNA. DR EMBL; AK315090; BAG37555.1; -; mRNA. DR EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877614; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471092; EAW83200.1; -; Genomic_DNA. DR EMBL; CH471092; EAW83201.1; -; Genomic_DNA. DR EMBL; CH471092; EAW83202.1; -; Genomic_DNA. DR EMBL; BC024021; AAH24021.1; -; mRNA. DR EMBL; AY358454; AAQ88819.1; ALT_INIT; mRNA. DR CCDS; CCDS10857.1; -. [Q9H4A9-1] DR RefSeq; NP_071750.1; NM_022355.3. [Q9H4A9-1] DR AlphaFoldDB; Q9H4A9; -. DR SMR; Q9H4A9; -. DR BioGRID; 122097; 59. DR IntAct; Q9H4A9; 17. DR STRING; 9606.ENSP00000458977; -. DR MEROPS; M19.002; -. DR GlyCosmos; Q9H4A9; 4 sites, 1 glycan. DR GlyGen; Q9H4A9; 5 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q9H4A9; -. DR PhosphoSitePlus; Q9H4A9; -. DR BioMuta; DPEP2; -. DR MassIVE; Q9H4A9; -. DR PaxDb; 9606-ENSP00000458977; -. DR PeptideAtlas; Q9H4A9; -. DR ProteomicsDB; 46839; -. DR ProteomicsDB; 80812; -. [Q9H4A9-1] DR ProteomicsDB; 80813; -. [Q9H4A9-2] DR Antibodypedia; 29700; 93 antibodies from 19 providers. DR DNASU; 64174; -. DR Ensembl; ENST00000393847.6; ENSP00000377430.1; ENSG00000167261.14. [Q9H4A9-1] DR Ensembl; ENST00000572888.5; ENSP00000458977.1; ENSG00000167261.14. [Q9H4A9-1] DR Ensembl; ENST00000575203.5; ENSP00000459375.1; ENSG00000167261.14. [Q9H4A9-3] DR GeneID; 64174; -. DR KEGG; hsa:64174; -. DR MANE-Select; ENST00000393847.6; ENSP00000377430.1; NM_022355.4; NP_071750.1. DR UCSC; uc002eve.5; human. [Q9H4A9-1] DR UCSC; uc059wbx.1; human. DR AGR; HGNC:23028; -. DR CTD; 64174; -. DR DisGeNET; 64174; -. DR GeneCards; DPEP2; -. DR HGNC; HGNC:23028; DPEP2. DR HPA; ENSG00000167261; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 609925; gene. DR neXtProt; NX_Q9H4A9; -. DR OpenTargets; ENSG00000167261; -. DR PharmGKB; PA134985997; -. DR VEuPathDB; HostDB:ENSG00000167261; -. DR eggNOG; KOG4127; Eukaryota. DR GeneTree; ENSGT00940000160211; -. DR HOGENOM; CLU_031404_4_1_1; -. DR InParanoid; Q9H4A9; -. DR OMA; WSGNVLR; -. DR OrthoDB; 5476406at2759; -. DR PhylomeDB; Q9H4A9; -. DR TreeFam; TF324523; -. DR BioCyc; MetaCyc:HS09532-MONOMER; -. DR PathwayCommons; Q9H4A9; -. DR Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX). DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification. DR Reactome; R-HSA-9664535; LTC4-CYSLTR mediated IL4 production. DR SignaLink; Q9H4A9; -. DR BioGRID-ORCS; 64174; 11 hits in 1160 CRISPR screens. DR GenomeRNAi; 64174; -. DR Pharos; Q9H4A9; Tbio. DR PRO; PR:Q9H4A9; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9H4A9; Protein. DR Bgee; ENSG00000167261; Expressed in granulocyte and 105 other cell types or tissues. DR ExpressionAtlas; Q9H4A9; baseline and differential. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0016805; F:dipeptidase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro. DR GO; GO:1901749; P:leukotriene D4 catabolic process; IDA:UniProtKB. DR GO; GO:0006691; P:leukotriene metabolic process; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd01301; rDP_like; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR000180; Dipep_AS. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR008257; Pept_M19. DR PANTHER; PTHR10443:SF9; DIPEPTIDASE 2; 1. DR PANTHER; PTHR10443; MICROSOMAL DIPEPTIDASE; 1. DR Pfam; PF01244; Peptidase_M19; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1. DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1. DR Genevisible; Q9H4A9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Dipeptidase; Disulfide bond; Glycoprotein; KW GPI-anchor; Hydrolase; Lipid metabolism; Lipoprotein; Membrane; KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal; Zinc. FT SIGNAL 1..32 FT /evidence="ECO:0000255" FT CHAIN 33..463 FT /note="Dipeptidase 2" FT /id="PRO_0000231603" FT PROPEP 464..486 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:P16444" FT /id="PRO_0000231604" FT BINDING 89 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 91 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 215 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 282 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 293 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT BINDING 351 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT LIPID 463 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000255" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 176 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 235 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT DISULFID 138..217 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT DISULFID 289..321 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT DISULFID 426 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10073" FT VAR_SEQ 43..129 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017851" FT VAR_SEQ 245..258 FT /note="KVVAEMNRLGMMVD -> MLWHGGPWKCHRHL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_059428" FT VAR_SEQ 259..486 FT /note="Missing (in isoform 3)" FT /id="VSP_059429" FT VARIANT 201 FT /note="R -> P (in dbSNP:rs255051)" FT /id="VAR_060230" FT VARIANT 468 FT /note="H -> D (in dbSNP:rs1133090)" FT /id="VAR_033894" SQ SEQUENCE 486 AA; 53365 MW; 8860C41CD9801FAC CRC64; MQPSGLEGPG TFGRWPLLSL LLLLLLLQPV TCAYTTPGPP RALTTLGAPR AHTMPGTYAP STTLSSPSTQ GLQEQARALM RDFPLVDGHN DLPLVLRQVY QKGLQDVNLR NFSYGQTSLD RLRDGLVGAQ FWSAYVPCQT QDRDALRLTL EQIDLIRRMC ASYSELELVT SAKALNDTQK LACLIGVEGG HSLDNSLSIL RTFYMLGVRY LTLTHTCNTP WAESSAKGVH SFYNNISGLT DFGEKVVAEM NRLGMMVDLS HVSDAVARRA LEVSQAPVIF SHSAARGVCN SARNVPDDIL QLLKKNGGVV MVSLSMGVIQ CNPSANVSTV ADHFDHIKAV IGSKFIGIGG DYDGAGKFPQ GLEDVSTYPV LIEELLSRGW SEEELQGVLR GNLLRVFRQV EKVQEENKWQ SPLEDKFPDE QLSSSCHSDL SRLRQRQSLT SGQELTEIPI HWTAKLPAKW SVSESSPHMA PVLAVVATFP VLILWL //