ID   LIPR1_HUMAN             Reviewed;         467 AA.
AC   P54315; Q68D83; Q68DR6; Q8TAU2; Q9BS82;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 193.
DE   RecName: Full=Inactive pancreatic lipase-related protein 1;
DE            Short=PL-RP1;
DE   Flags: Precursor;
GN   Name=PNLIPRP1; Synonyms=PLRP1;
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), ABSENCE OF LIPASE ACTIVITY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Pancreas;
RX   PubMed=1379598; DOI=10.1016/s0021-9258(18)42032-7;
RA   Giller T., Buchwald P., Blum-Kaelin D., Hunziker W.;
RT   "Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2.
RT   Differences in colipase dependence and in lipase activity.";
RL   J. Biol. Chem. 267:16509-16516(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Liver;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ASP-414.
RC   TISSUE=Pancreas;
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   FUNCTION, SUBCELLULAR LOCATION, AND ABSENCE OF CATALYTIC ACTIVITY.
RX   PubMed=19824014; DOI=10.1002/mnfr.200800563;
RA   Berton A., Sebban-Kreuzer C., Rouvellac S., Lopez C., Crenon I.;
RT   "Individual and combined action of pancreatic lipase and pancreatic lipase-
RT   related proteins 1 and 2 on native versus homogenized milk fat globules.";
RL   Mol. Nutr. Food Res. 53:1592-1602(2009).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-467 IN COMPLEX WITH CALCIUM
RP   IONS, AND DISULFIDE BONDS.
RG   Structural genomics consortium (SGC);
RT   "Structure of the human pancreatic lipase-related protein 1.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [6]
RP   VARIANT [LARGE SCALE ANALYSIS] CYS-129.
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).
CC   -!- FUNCTION: May function as inhibitor of dietary triglyceride digestion.
CC       Lacks detectable lipase activity towards triglycerides, diglycerides,
CC       phosphatidylcholine, galactolipids or cholesterol esters (in vitro) (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:19824014}.
CC   -!- INTERACTION:
CC       P54315; P41181: AQP2; NbExp=3; IntAct=EBI-8652812, EBI-12701138;
CC       P54315; Q8NFU1: BEST2; NbExp=3; IntAct=EBI-8652812, EBI-19947314;
CC       P54315; P11912: CD79A; NbExp=3; IntAct=EBI-8652812, EBI-7797864;
CC       P54315; Q9HA82: CERS4; NbExp=3; IntAct=EBI-8652812, EBI-2622997;
CC       P54315; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-8652812, EBI-18013275;
CC       P54315; P00387: CYB5R3; NbExp=3; IntAct=EBI-8652812, EBI-1046040;
CC       P54315; Q15125: EBP; NbExp=3; IntAct=EBI-8652812, EBI-3915253;
CC       P54315; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-8652812, EBI-18304435;
CC       P54315; O15552: FFAR2; NbExp=3; IntAct=EBI-8652812, EBI-2833872;
CC       P54315; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-8652812, EBI-11110431;
CC       P54315; P48165: GJA8; NbExp=3; IntAct=EBI-8652812, EBI-17458373;
CC       P54315; O95377: GJB5; NbExp=3; IntAct=EBI-8652812, EBI-3909454;
CC       P54315; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-8652812, EBI-13345167;
CC       P54315; O15529: GPR42; NbExp=3; IntAct=EBI-8652812, EBI-18076404;
CC       P54315; Q8TED1: GPX8; NbExp=3; IntAct=EBI-8652812, EBI-11721746;
CC       P54315; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-8652812, EBI-18053395;
CC       P54315; P48051: KCNJ6; NbExp=3; IntAct=EBI-8652812, EBI-12017638;
CC       P54315; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-8652812, EBI-17490413;
CC       P54315; Q8N386: LRRC25; NbExp=3; IntAct=EBI-8652812, EBI-11304917;
CC       P54315; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-8652812, EBI-2689785;
CC       P54315; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-8652812, EBI-16439278;
CC       P54315; P15941-11: MUC1; NbExp=3; IntAct=EBI-8652812, EBI-17263240;
CC       P54315; Q9Y375: NDUFAF1; NbExp=3; IntAct=EBI-8652812, EBI-741874;
CC       P54315; O14524-2: NEMP1; NbExp=3; IntAct=EBI-8652812, EBI-10969203;
CC       P54315; O00623: PEX12; NbExp=3; IntAct=EBI-8652812, EBI-594836;
CC       P54315; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-8652812, EBI-10192441;
CC       P54315; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-8652812, EBI-18159983;
CC       P54315; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-8652812, EBI-17595455;
CC       P54315; O95436-2: SLC34A2; NbExp=3; IntAct=EBI-8652812, EBI-12811757;
CC       P54315; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-8652812, EBI-17295964;
CC       P54315; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-8652812, EBI-12898013;
CC       P54315; P30825: SLC7A1; NbExp=3; IntAct=EBI-8652812, EBI-4289564;
CC       P54315; Q16623: STX1A; NbExp=3; IntAct=EBI-8652812, EBI-712466;
CC       P54315; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-8652812, EBI-8638294;
CC       P54315; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-8652812, EBI-10982110;
CC       P54315; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-8652812, EBI-11724433;
CC       P54315; Q9Y320: TMX2; NbExp=3; IntAct=EBI-8652812, EBI-6447886;
CC       P54315; P19075: TSPAN8; NbExp=3; IntAct=EBI-8652812, EBI-4289938;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1379598,
CC       ECO:0000269|PubMed:19824014}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P54315-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P54315-2; Sequence=VSP_014097, VSP_014100;
CC       Name=3;
CC         IsoId=P54315-3; Sequence=VSP_014098, VSP_014099;
CC   -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000269|PubMed:1379598}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M93283; AAA59532.1; -; mRNA.
DR   EMBL; CR749299; CAH18154.1; -; mRNA.
DR   EMBL; CR749524; CAH18337.1; -; mRNA.
DR   EMBL; BC005233; AAH05233.1; -; mRNA.
DR   EMBL; BC025784; AAH25784.1; -; mRNA.
DR   CCDS; CCDS7595.1; -. [P54315-1]
DR   PIR; A43357; A43357.
DR   RefSeq; NP_001290064.1; NM_001303135.1. [P54315-1]
DR   RefSeq; NP_006220.1; NM_006229.3. [P54315-1]
DR   RefSeq; XP_011538170.1; XM_011539868.1.
DR   PDB; 2PPL; X-ray; 2.20 A; A=18-467.
DR   PDBsum; 2PPL; -.
DR   AlphaFoldDB; P54315; -.
DR   SMR; P54315; -.
DR   BioGRID; 111408; 167.
DR   IntAct; P54315; 48.
DR   MINT; P54315; -.
DR   STRING; 9606.ENSP00000433933; -.
DR   ESTHER; human-PNLIPRP1; Pancreatic_lipase.
DR   PhosphoSitePlus; P54315; -.
DR   BioMuta; PNLIPRP1; -.
DR   DMDM; 1708837; -.
DR   MassIVE; P54315; -.
DR   PaxDb; 9606-ENSP00000433933; -.
DR   PeptideAtlas; P54315; -.
DR   ProteomicsDB; 56681; -. [P54315-1]
DR   ProteomicsDB; 56682; -. [P54315-2]
DR   ProteomicsDB; 56683; -. [P54315-3]
DR   Antibodypedia; 35303; 91 antibodies from 17 providers.
DR   DNASU; 5407; -.
DR   Ensembl; ENST00000358834.9; ENSP00000351695.4; ENSG00000187021.15. [P54315-1]
DR   Ensembl; ENST00000528052.5; ENSP00000433933.1; ENSG00000187021.15. [P54315-1]
DR   Ensembl; ENST00000709137.1; ENSP00000517519.1; ENSG00000291891.1. [P54315-1]
DR   Ensembl; ENST00000709140.1; ENSP00000517520.1; ENSG00000291891.1. [P54315-1]
DR   GeneID; 5407; -.
DR   KEGG; hsa:5407; -.
DR   MANE-Select; ENST00000358834.9; ENSP00000351695.4; NM_006229.4; NP_006220.1.
DR   UCSC; uc001lco.2; human. [P54315-1]
DR   AGR; HGNC:9156; -.
DR   CTD; 5407; -.
DR   DisGeNET; 5407; -.
DR   GeneCards; PNLIPRP1; -.
DR   HGNC; HGNC:9156; PNLIPRP1.
DR   HPA; ENSG00000187021; Tissue enriched (pancreas).
DR   MIM; 604422; gene.
DR   neXtProt; NX_P54315; -.
DR   OpenTargets; ENSG00000187021; -.
DR   PharmGKB; PA33479; -.
DR   VEuPathDB; HostDB:ENSG00000187021; -.
DR   eggNOG; ENOG502QUK7; Eukaryota.
DR   GeneTree; ENSGT00940000162375; -.
DR   HOGENOM; CLU_027171_0_2_1; -.
DR   InParanoid; P54315; -.
DR   OMA; FAAYPCA; -.
DR   OrthoDB; 3428256at2759; -.
DR   PhylomeDB; P54315; -.
DR   TreeFam; TF324997; -.
DR   BRENDA; 3.1.1.26; 2681.
DR   PathwayCommons; P54315; -.
DR   Reactome; R-HSA-192456; Digestion of dietary lipid.
DR   SignaLink; P54315; -.
DR   BioGRID-ORCS; 5407; 11 hits in 1149 CRISPR screens.
DR   ChiTaRS; PNLIPRP1; human.
DR   EvolutionaryTrace; P54315; -.
DR   GenomeRNAi; 5407; -.
DR   Pharos; P54315; Tbio.
DR   PRO; PR:P54315; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; P54315; Protein.
DR   Bgee; ENSG00000187021; Expressed in body of pancreas and 99 other cell types or tissues.
DR   ExpressionAtlas; P54315; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0004806; F:triglyceride lipase activity; TAS:ProtInc.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   CDD; cd01759; PLAT_PL; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR016272; Lipase_LIPH.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR002331; Lipase_panc.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610:SF108; INACTIVE PANCREATIC LIPASE-RELATED PROTEIN 1; 1.
DR   PANTHER; PTHR11610; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR   PRINTS; PR00823; PANCLIPASE.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   Genevisible; P54315; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Disulfide bond; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..467
FT                   /note="Inactive pancreatic lipase-related protein 1"
FT                   /id="PRO_0000017790"
FT   DOMAIN          356..467
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   ACT_SITE        171
FT                   /note="Nucleophile"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT   ACT_SITE        281
FT                   /note="Charge relay system"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT   DISULFID        21..27
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|Ref.5"
FT   DISULFID        109..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|Ref.5"
FT   DISULFID        255..279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|Ref.5"
FT   DISULFID        303..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|Ref.5"
FT   DISULFID        317..322
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|Ref.5"
FT   DISULFID        451..467
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT                   ECO:0000269|Ref.5"
FT   VAR_SEQ         111..186
FT                   /note="KLFEVEEVNCICVDWKKGSQATYTQAANNVRVVGAQVAQMLDILLTEYSYPP
FT                   SKVHLIGHSLGAHVAGEAGSKTPG -> VGASSDPCGQLRPTLLLTSLHHFMHSRNLYI
FT                   LGNFMQLKCFSSQKLKCLSMFPHYICTLKQPHLLLEKYSYYLISG (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014097"
FT   VAR_SEQ         111..117
FT                   /note="KLFEVEE -> PGASPRA (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_014098"
FT   VAR_SEQ         118..467
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_014099"
FT   VAR_SEQ         187..467
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014100"
FT   VARIANT         61
FT                   /note="N -> D (in dbSNP:rs11197744)"
FT                   /id="VAR_049820"
FT   VARIANT         129
FT                   /note="S -> C (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036379"
FT   VARIANT         271
FT                   /note="A -> V (in dbSNP:rs2305205)"
FT                   /id="VAR_022082"
FT   VARIANT         414
FT                   /note="E -> D (in dbSNP:rs2305204)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_022659"
FT   VARIANT         461
FT                   /note="L -> P (in dbSNP:rs1049125)"
FT                   /id="VAR_014915"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          35..40
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           49..52
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          55..63
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           104..115
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          118..124
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           126..129
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           133..158
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          165..170
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           173..182
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          189..194
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   TURN            198..202
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   TURN            205..207
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          214..220
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          240..246
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          249..251
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           266..270
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           279..293
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   TURN            295..298
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           306..310
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          324..326
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   HELIX           327..331
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          341..345
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          349..352
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          356..367
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          369..379
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          387..394
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          399..408
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          412..421
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          432..441
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          447..451
FT                   /evidence="ECO:0007829|PDB:2PPL"
FT   STRAND          462..466
FT                   /evidence="ECO:0007829|PDB:2PPL"
SQ   SEQUENCE   467 AA;  51848 MW;  2781EA1E22E39E78 CRC64;
     MLIFWTITLF LLGAAKGKEV CYEDLGCFSD TEPWGGTAIR PLKILPWSPE KIGTRFLLYT
     NENPNNFQIL LLSDPSTIEA SNFQMDRKTR FIIHGFIDKG DESWVTDMCK KLFEVEEVNC
     ICVDWKKGSQ ATYTQAANNV RVVGAQVAQM LDILLTEYSY PPSKVHLIGH SLGAHVAGEA
     GSKTPGLSRI TGLDPVEASF ESTPEEVRLD PSDADFVDVI HTDAAPLIPF LGFGTNQQMG
     HLDFFPNGGE SMPGCKKNAL SQIVDLDGIW AGTRDFVACN HLRSYKYYLE SILNPDGFAA
     YPCTSYKSFE SDKCFPCPDQ GCPQMGHYAD KFAGRTSEEQ QKFFLNTGEA SNFARWRYGV
     SITLSGRTAT GQIKVALFGN KGNTHQYSIF RGILKPGSTH SYEFDAKLDV GTIEKVKFLW
     NNNVINPTLP KVGATKITVQ KGEEKTVYNF CSEDTVREDT LLTLTPC
//