DPEP2_HUMAN
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 03-AUG-2022, entry version 156.
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,
CC ECO:0000255|PROSITE-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};
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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; 58.
DR IntAct; Q9H4A9; 17.
DR STRING; 9606.ENSP00000458977; -.
DR MEROPS; M19.002; -.
DR GlyGen; Q9H4A9; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H4A9; -.
DR PhosphoSitePlus; Q9H4A9; -.
DR BioMuta; DPEP2; -.
DR MassIVE; Q9H4A9; -.
DR PaxDb; Q9H4A9; -.
DR PeptideAtlas; Q9H4A9; -.
DR PRIDE; Q9H4A9; -.
DR ProteomicsDB; 46839; -.
DR ProteomicsDB; 80812; -. [Q9H4A9-1]
DR ProteomicsDB; 80813; -. [Q9H4A9-2]
DR Antibodypedia; 29700; 73 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 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; KHIFHIA; -.
DR OrthoDB; 1272387at2759; -.
DR PhylomeDB; Q9H4A9; -.
DR TreeFam; TF324523; -.
DR BioCyc; MetaCyc:HS09532-MON; -.
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 1077 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 103 other tissues.
DR ExpressionAtlas; Q9H4A9; baseline and differential.
DR Genevisible; Q9H4A9; HS.
DR GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01301; rDP_like; 1.
DR InterPro; IPR000180; Dipep_AS.
DR InterPro; IPR028531; Dpep2/3.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008257; Pept_M19.
DR PANTHER; PTHR10443; PTHR10443; 1.
DR PANTHER; PTHR10443:SF14; PTHR10443:SF14; 1.
DR Pfam; PF01244; Peptidase_M19; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1.
DR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
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
