ID P3H2_HUMAN Reviewed; 708 AA. AC Q8IVL5; B3KPK0; B3KWI9; D3DNV8; Q9NVI2; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 167. DE RecName: Full=Prolyl 3-hydroxylase 2 {ECO:0000312|HGNC:HGNC:19317}; DE EC=1.14.11.7 {ECO:0000269|PubMed:18487197}; DE AltName: Full=Leprecan-like protein 1 {ECO:0000303|PubMed:15063763}; DE AltName: Full=Myxoid liposarcoma-associated protein 4 {ECO:0000303|PubMed:10449603}; DE Flags: Precursor; GN Name=P3H2 {ECO:0000312|HGNC:HGNC:19317}; GN Synonyms=LEPREL1 {ECO:0000303|PubMed:15063763}, MLAT4 GN {ECO:0000303|PubMed:10449603}; 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=Liposarcoma; RX PubMed=10449603; RX DOI=10.1002/(sici)1097-0215(19990924)83:1<30::aid-ijc6>3.0.co;2-4; RA Thelin-Jaernum S., Lassen C., Panagopoulos I., Mandahl N., Aaman P.; RT "Identification of genes differentially expressed in TLS-CHOP carrying RT myxoid liposarcomas."; RL Int. J. Cancer 83:30-33(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND POSSIBLE FUNCTION. RC TISSUE=Liposarcoma; RX PubMed=15063763; DOI=10.1016/j.bbrc.2004.03.060; RA Jaernum S., Kjellman C., Darabi A., Nilsson I., Edvardsen K., Aaman P.; RT "LEPREL1, a novel ER and Golgi resident member of the Leprecan family."; RL Biochem. Biophys. Res. Commun. 317:342-351(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma, and Tongue; 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=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). 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] OF 161-708 (ISOFORM 1). 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 [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY. RX PubMed=18487197; DOI=10.1074/jbc.m802973200; RA Tiainen P., Pasanen A., Sormunen R., Myllyharju J.; RT "Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an RT enzyme modifying the basement membrane collagen IV."; RL J. Biol. Chem. 283:19432-19439(2008). RN [8] RP VARIANT [LARGE SCALE ANALYSIS] ASN-613. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [9] RP VARIANT MCVD VAL-508, AND CHARACTERIZATION OF VARIANT MCVD VAL-508. RX PubMed=21885030; DOI=10.1016/j.ajhg.2011.08.003; RA Mordechai S., Gradstein L., Pasanen A., Ofir R., El Amour K., Levy J., RA Belfair N., Lifshitz T., Joshua S., Narkis G., Elbedour K., Myllyharju J., RA Birk O.S.; RT "High myopia caused by a mutation in LEPREL1, encoding prolyl 3-hydroxylase RT 2."; RL Am. J. Hum. Genet. 89:438-445(2011). CC -!- FUNCTION: Prolyl 3-hydroxylase that catalyzes the post-translational CC formation of 3-hydroxyproline on collagens (PubMed:18487197). CC Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in CC tendons, the eye sclera and in the eye lens capsule (By similarity). CC Has high activity with the type IV collagen COL4A1, and lower activity CC with COL1A1 (PubMed:18487197). Catalyzes hydroxylation of the first Pro CC in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline CC (PubMed:18487197). Has no activity on substrates that lack 4- CC hydroxyproline in the third position (PubMed:18487197). CC {ECO:0000250|UniProtKB:Q8CG71, ECO:0000269|PubMed:18487197}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + CC trans-3-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:22872, Rhea:RHEA- CC COMP:11676, Rhea:RHEA-COMP:11678, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; EC=1.14.11.7; CC Evidence={ECO:0000269|PubMed:18487197}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000305|PubMed:18487197}; CC -!- COFACTOR: CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; CC Evidence={ECO:0000305|PubMed:18487197}; CC -!- ACTIVITY REGULATION: Inhibited by pyridine 2,4-dicarboxylate, an analog CC of 2-oxoglutarate. {ECO:0000269|PubMed:18487197}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=80 uM for 2-oxoglutarate {ECO:0000269|PubMed:18487197}; CC KM=110 uM for ascorbate {ECO:0000269|PubMed:18487197}; CC KM=0.5 uM for Fe(2+) {ECO:0000269|PubMed:18487197}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE- CC ProRule:PRU10138, ECO:0000269|PubMed:15063763}. Sarcoplasmic reticulum CC {ECO:0000305|PubMed:15063763}. Golgi apparatus CC {ECO:0000269|PubMed:15063763}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IVL5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IVL5-2; Sequence=VSP_053814; CC -!- TISSUE SPECIFICITY: Expression localized to the epithelia of bile ducts CC and to the sacroplasm of heart muscle and skeletal muscle. In the CC pancreas, localized to a subpopulation of Langerhans islet cells and in CC the salivary gland, expressed in acinar cells (at protein level) CC (PubMed:15063763). Expressed in adult heart, placenta, lung, liver, CC skeletal muscle and kidney (PubMed:15063763, PubMed:18487197). Detected CC in fetal heart, spleen, lung, liver skeletal muscle and kidney CC (PubMed:18487197). {ECO:0000269|PubMed:15063763, CC ECO:0000269|PubMed:18487197}. CC -!- DISEASE: Myopia, high, with cataract and vitreoretinal degeneration CC (MCVD) [MIM:614292]: A disorder characterized by severe myopia with CC variable expressivity of cataract and vitreoretinal degeneration. Some CC patients manifest lens subluxation, lens instability and retinal CC detachment. {ECO:0000269|PubMed:21885030}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91769.1; 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; AJ430351; CAD23039.2; -; mRNA. DR EMBL; AK001580; BAA91769.1; ALT_INIT; mRNA. DR EMBL; AK056447; BAG51712.1; -; mRNA. DR EMBL; AK125134; BAG54151.1; -; mRNA. DR EMBL; AC016966; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC063939; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78109.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78110.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78111.1; -; Genomic_DNA. DR EMBL; BC005029; AAH05029.1; -; mRNA. DR CCDS; CCDS3294.1; -. [Q8IVL5-1] DR CCDS; CCDS46981.1; -. [Q8IVL5-2] DR RefSeq; NP_001127890.1; NM_001134418.1. [Q8IVL5-2] DR RefSeq; NP_060662.2; NM_018192.3. [Q8IVL5-1] DR RefSeq; XP_011511257.1; XM_011512955.1. DR AlphaFoldDB; Q8IVL5; -. DR SMR; Q8IVL5; -. DR BioGRID; 120510; 29. DR IntAct; Q8IVL5; 16. DR STRING; 9606.ENSP00000316881; -. DR DrugBank; DB00126; Ascorbic acid. DR DrugBank; DB00172; Proline. DR DrugBank; DB00139; Succinic acid. DR GlyCosmos; Q8IVL5; 2 sites, No reported glycans. DR GlyGen; Q8IVL5; 2 sites. DR iPTMnet; Q8IVL5; -. DR PhosphoSitePlus; Q8IVL5; -. DR BioMuta; P3H2; -. DR DMDM; 74714365; -. DR EPD; Q8IVL5; -. DR jPOST; Q8IVL5; -. DR MassIVE; Q8IVL5; -. DR MaxQB; Q8IVL5; -. DR PaxDb; 9606-ENSP00000316881; -. DR PeptideAtlas; Q8IVL5; -. DR ProteomicsDB; 12740; -. DR ProteomicsDB; 70737; -. [Q8IVL5-1] DR Pumba; Q8IVL5; -. DR Antibodypedia; 1998; 139 antibodies from 20 providers. DR DNASU; 55214; -. DR Ensembl; ENST00000319332.10; ENSP00000316881.5; ENSG00000090530.10. [Q8IVL5-1] DR Ensembl; ENST00000427335.6; ENSP00000408947.2; ENSG00000090530.10. [Q8IVL5-2] DR GeneID; 55214; -. DR KEGG; hsa:55214; -. DR MANE-Select; ENST00000319332.10; ENSP00000316881.5; NM_018192.4; NP_060662.2. DR UCSC; uc003fsg.4; human. [Q8IVL5-1] DR AGR; HGNC:19317; -. DR CTD; 55214; -. DR DisGeNET; 55214; -. DR GeneCards; P3H2; -. DR HGNC; HGNC:19317; P3H2. DR HPA; ENSG00000090530; Low tissue specificity. DR MalaCards; P3H2; -. DR MIM; 610341; gene. DR MIM; 614292; phenotype. DR neXtProt; NX_Q8IVL5; -. DR OpenTargets; ENSG00000090530; -. DR Orphanet; 98619; Rare isolated myopia. DR PharmGKB; PA134922807; -. DR VEuPathDB; HostDB:ENSG00000090530; -. DR eggNOG; KOG4459; Eukaryota. DR GeneTree; ENSGT00940000159593; -. DR HOGENOM; CLU_017820_0_0_1; -. DR InParanoid; Q8IVL5; -. DR OMA; NEDTECR; -. DR OrthoDB; 5398065at2759; -. DR PhylomeDB; Q8IVL5; -. DR TreeFam; TF320837; -. DR BRENDA; 1.14.11.7; 2681. DR PathwayCommons; Q8IVL5; -. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR SignaLink; Q8IVL5; -. DR BioGRID-ORCS; 55214; 5 hits in 1145 CRISPR screens. DR ChiTaRS; P3H2; human. DR GenomeRNAi; 55214; -. DR Pharos; Q8IVL5; Tbio. DR PRO; PR:Q8IVL5; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8IVL5; Protein. DR Bgee; ENSG00000090530; Expressed in adrenal tissue and 138 other cell types or tissues. DR ExpressionAtlas; Q8IVL5; baseline and differential. DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IDA:UniProtKB. DR GO; GO:0032963; P:collagen metabolic process; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0019511; P:peptidyl-proline hydroxylation; IDA:UniProtKB. DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR039575; P3H. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR14049; LEPRECAN 1; 1. DR PANTHER; PTHR14049:SF1; PROLYL 3-HYDROXYLASE 2; 1. DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1. DR SMART; SM00702; P4Hc; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR Genevisible; Q8IVL5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Dioxygenase; Disease variant; Endoplasmic reticulum; KW Glycoprotein; Golgi apparatus; Iron; Metal-binding; Oxidoreductase; KW Reference proteome; Repeat; Sarcoplasmic reticulum; Signal; TPR repeat; KW Vitamin C. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..708 FT /note="Prolyl 3-hydroxylase 2" FT /id="PRO_0000240356" FT REPEAT 44..77 FT /note="TPR 1" FT REPEAT 148..181 FT /note="TPR 2" FT REPEAT 210..243 FT /note="TPR 3" FT REPEAT 306..339 FT /note="TPR 4" FT DOMAIN 557..671 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT MOTIF 705..708 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT ACT_SITE 662 FT /evidence="ECO:0000250" FT BINDING 580 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 582 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 652 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT CARBOHYD 449 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 549 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..181 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_053814" FT VARIANT 508 FT /note="G -> V (in MCVD; loss of function; FT dbSNP:rs724159988)" FT /evidence="ECO:0000269|PubMed:21885030" FT /id="VAR_066637" FT VARIANT 613 FT /note="D -> N (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036123" FT CONFLICT 477 FT /note="R -> Q (in Ref. 3; BAG51712)" FT /evidence="ECO:0000305" SQ SEQUENCE 708 AA; 80984 MW; B9E680C90D607291 CRC64; MRERIWAPPL LLLLPLLLPP PLWGGPPDSP RRELELEPGP LQPFDLLYAS GAAAYYSGDY ERAVRDLEAA LRSHRRLREI RTRCARHCAA RHPLPPPPPG EGPGAELPLF RSLLGRARCY RSCETQRLGG PASRHRVSED VRSDFQRRVP YNYLQRAYIK LNQLEKAVEA AHTFFVANPE HMEMQQNIEN YRATAGVEAL QLVDREAKPH MESYNAGVKH YEADDFEMAI RHFEQALREY FVEDTECRTL CEGPQRFEEY EYLGYKAGLY EAIADHYMQV LVCQHECVRE LATRPGRLSP IENFLPLHYD YLQFAYYRVG EYVKALECAK AYLLCHPDDE DVLDNVDYYE SLLDDSIDPA SIEAREDLTM FVKRHKLESE LIKSAAEGLG FSYTEPNYWI RYGGRQDENR VPSGVNVEGA EVHGFSMGKK LSPKIDRDLR EGGPLLYENI TFVYNSEQLN GTQRVLLDNV LSEEQCRELH SVASGIMLVG DGYRGKTSPH TPNEKFEGAT VLKALKSGYE GRVPLKSARL FYDISEKARR IVESYFMLNS TLYFSYTHMV CRTALSGQQD RRNDLSHPIH ADNCLLDPEA NECWKEPPAY TFRDYSALLY MNDDFEGGEF IFTEMDAKTV TASIKPKCGR MISFSSGGEN PHGVKAVTKG KRCAVALWFT LDPLYRELER IQADEVIAIL DQEQQGKHEL NINPKDEL //