XPP2_HUMAN
ID XPP2_HUMAN Reviewed; 674 AA.
AC O43895; A0AV16; O75994;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Xaa-Pro aminopeptidase 2;
DE EC=3.4.11.9 {ECO:0000269|PubMed:15361070};
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Membrane-bound aminopeptidase P;
DE Short=Membrane-bound APP;
DE Short=Membrane-bound AmP;
DE Short=mAmP;
DE AltName: Full=X-Pro aminopeptidase 2;
DE Flags: Precursor;
GN Name=XPNPEP2;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney, and Lung;
RX PubMed=9375790; DOI=10.1016/s0167-4781(97)00126-7;
RA Venema R.C., Ju H., Zou R., Venema V.J., Ryan J.W.;
RT "Cloning and tissue distribution of human membrane-bound aminopeptidase
RT P.";
RL Biochim. Biophys. Acta 1354:45-48(1997).
RN [2]
RP SEQUENCE REVISION.
RA Sprinkle T.J.C., Venema R.C., Ju H., Zou R., Venema V.J., Ryan J.W.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ryan J.W., Jin L., Horvath I., Sprinkle T.J.C.;
RT "Human membrane-bound aminopeptidase P genomic DNA.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 INVOLVEMENT IN AEACEI.
RX PubMed=16175507; DOI=10.1086/496899;
RA Duan Q.L., Nikpoor B., Dube M.P., Molinaro G., Meijer I.A., Dion P.,
RA Rochefort D., Saint-Onge J., Flury L., Brown N.J., Gainer J.V.,
RA Rouleau J.L., Agostoni A., Cugno M., Simon P., Clavel P., Potier J.,
RA Wehbe B., Benarbia S., Marc-Aurele J., Chanard J., Foroud T., Adam A.,
RA Rouleau G.A.;
RT "A variant in XPNPEP2 is associated with angioedema induced by angiotensin
RT I-converting enzyme inhibitors.";
RL Am. J. Hum. Genet. 77:617-626(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND GLYCOSYLATION.
RX PubMed=15361070; DOI=10.1042/bj20040849;
RA Molinaro G., Carmona A.K., Juliano M.A., Juliano L., Malitskaya E.,
RA Yessine M.A., Chagnon M., Lepage Y., Simmons W.H., Boileau G., Adam A.;
RT "Human recombinant membrane-bound aminopeptidase P: production of a soluble
RT form and characterization using novel, internally quenched fluorescent
RT substrates.";
RL Biochem. J. 385:389-397(2005).
RN [8]
RP INVOLVEMENT IN AEACEI.
RX PubMed=20625347; DOI=10.1097/fpc.0b013e32833d3acb;
RA Woodard-Grice A.V., Lucisano A.C., Byrd J.B., Stone E.R., Simmons W.H.,
RA Brown N.J.;
RT "Sex-dependent and race-dependent association of XPNPEP2 C-2399A
RT polymorphism with angiotensin-converting enzyme inhibitor-associated
RT angioedema.";
RL Pharmacogenet. Genomics 20:532-536(2010).
RN [9]
RP INVOLVEMENT IN AEACEI, AND VARIANTS ILE-215; ILE-223 AND ASN-232.
RX PubMed=21898657; DOI=10.1002/humu.21579;
RA Cilia La Corte A.L., Carter A.M., Rice G.I., Duan Q.L., Rouleau G.A.,
RA Adam A., Grant P.J., Hooper N.M.;
RT "A functional XPNPEP2 promoter haplotype leads to reduced plasma
RT aminopeptidase P and increased risk of ACE inhibitor-induced angioedema.";
RL Hum. Mutat. 32:1326-1331(2011).
CC -!- FUNCTION: Membrane-bound metalloprotease which catalyzes the removal of
CC a penultimate prolyl residue from the N-termini of peptides, such as
CC Arg-Pro-Pro. May play a role in the metabolism of the vasodilator
CC bradykinin. {ECO:0000269|PubMed:15361070}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9; Evidence={ECO:0000269|PubMed:15361070};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q95333};
CC -!- ACTIVITY REGULATION: Inhibited by apstatin and the chelating agent
CC 1,10-phenanthroline. Also inhibited by high concentrations of Zn(2+).
CC Not significantly inhibited by bestatin or phosphoramidon.
CC {ECO:0000269|PubMed:15361070}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.837 mM for Arg-Pro-Pro {ECO:0000269|PubMed:15361070};
CC KM=75 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg (bradykinin)
CC {ECO:0000269|PubMed:15361070};
CC KM=56 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe (bradykinin[1-8])
CC {ECO:0000269|PubMed:15361070};
CC KM=18 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Gly-
CC Phe-Ser-Pro-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070};
CC KM=20 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Gly-
CC Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070};
CC KM=19 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-
CC Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:15361070};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q95333}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q95333};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q95333}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung, heart, placenta, liver,
CC small intestine and colon. No expression in brain, skeletal muscle,
CC pancreas, spleen, thymus, prostate, testis and ovary.
CC {ECO:0000269|PubMed:9375790}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15361070}.
CC -!- DISEASE: Angioedema induced by ACE inhibitors (AEACEI) [MIM:300909]: A
CC potentially life-threatening side effect of ACE inhibitors that appears
CC in a subset of patients taking these drugs for hypertension and
CC cardiovascular disease treatment. AEACEI is characterized by swelling
CC of the face, lips, tongue, and airway that can lead to suffocation and
CC death if severe. {ECO:0000269|PubMed:16175507,
CC ECO:0000269|PubMed:20625347, ECO:0000269|PubMed:21898657}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase M24B 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; U90724; AAB96394.2; -; mRNA.
DR EMBL; AF195953; AAG28480.1; -; Genomic_DNA.
DR EMBL; AL023653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126174; AAI26175.1; -; mRNA.
DR CCDS; CCDS14613.1; -.
DR RefSeq; NP_003390.4; NM_003399.5.
DR AlphaFoldDB; O43895; -.
DR SMR; O43895; -.
DR BioGRID; 113347; 2.
DR IntAct; O43895; 1.
DR STRING; 9606.ENSP00000360147; -.
DR BindingDB; O43895; -.
DR ChEMBL; CHEMBL4610; -.
DR GuidetoPHARMACOLOGY; 1579; -.
DR MEROPS; M24.005; -.
DR GlyGen; O43895; 5 sites.
DR iPTMnet; O43895; -.
DR PhosphoSitePlus; O43895; -.
DR BioMuta; XPNPEP2; -.
DR EPD; O43895; -.
DR jPOST; O43895; -.
DR MassIVE; O43895; -.
DR PaxDb; O43895; -.
DR PeptideAtlas; O43895; -.
DR PRIDE; O43895; -.
DR ProteomicsDB; 49219; -.
DR Antibodypedia; 16116; 181 antibodies from 28 providers.
DR DNASU; 7512; -.
DR Ensembl; ENST00000371106.4; ENSP00000360147.3; ENSG00000122121.12.
DR GeneID; 7512; -.
DR KEGG; hsa:7512; -.
DR MANE-Select; ENST00000371106.4; ENSP00000360147.3; NM_003399.6; NP_003390.4.
DR UCSC; uc004eut.2; human.
DR CTD; 7512; -.
DR DisGeNET; 7512; -.
DR GeneCards; XPNPEP2; -.
DR HGNC; HGNC:12823; XPNPEP2.
DR HPA; ENSG00000122121; Group enriched (intestine, kidney).
DR MalaCards; XPNPEP2; -.
DR MIM; 300145; gene.
DR MIM; 300909; phenotype.
DR neXtProt; NX_O43895; -.
DR OpenTargets; ENSG00000122121; -.
DR Orphanet; 100057; Renin-angiotensin-aldosterone system-blocker-induced angioedema.
DR PharmGKB; PA37416; -.
DR VEuPathDB; HostDB:ENSG00000122121; -.
DR eggNOG; KOG2413; Eukaryota.
DR GeneTree; ENSGT00940000157196; -.
DR HOGENOM; CLU_011781_2_2_1; -.
DR InParanoid; O43895; -.
DR OMA; WQDGLNY; -.
DR OrthoDB; 417805at2759; -.
DR PhylomeDB; O43895; -.
DR TreeFam; TF314183; -.
DR BRENDA; 3.4.11.9; 2681.
DR PathwayCommons; O43895; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; O43895; -.
DR BioGRID-ORCS; 7512; 8 hits in 693 CRISPR screens.
DR GeneWiki; XPNPEP2; -.
DR GenomeRNAi; 7512; -.
DR Pharos; O43895; Tchem.
DR PRO; PR:O43895; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O43895; protein.
DR Bgee; ENSG00000122121; Expressed in ileal mucosa and 92 other tissues.
DR Genevisible; O43895; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.40.350.10; -; 2.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..649
FT /note="Xaa-Pro aminopeptidase 2"
FT /id="PRO_0000026829"
FT PROPEP 650..674
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026830"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 524
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 533
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 555
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O44750"
FT LIPID 649
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000250|UniProtKB:Q95333"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 215
FT /note="T -> I (in dbSNP:rs138365897)"
FT /evidence="ECO:0000269|PubMed:21898657"
FT /id="VAR_071310"
FT VARIANT 223
FT /note="V -> I (in dbSNP:rs61733030)"
FT /evidence="ECO:0000269|PubMed:21898657"
FT /id="VAR_071311"
FT VARIANT 232
FT /note="K -> N (in dbSNP:rs41311662)"
FT /evidence="ECO:0000269|PubMed:21898657"
FT /id="VAR_071312"
FT CONFLICT 26
FT /note="V -> L (in Ref. 1; AAB96394)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="K -> R (in Ref. 1; AAB96394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 674 AA; 75625 MW; 75949336EDD0F3B4 CRC64;
MARAHWGCCP WLVLLCACAW GHTKPVDLGG QDVRNCSTNP PYLPVTVVNT TMSLTALRQQ
MQTQNLSAYI IPGTDAHMNE YIGQHDERRA WITGFTGSAG TAVVTMKKAA VWTDSRYWTQ
AERQMDCNWE LHKEVGTTPI VTWLLTEIPA GGRVGFDPFL LSIDTWESYD LALQGSNRQL
VSITTNLVDL VWGSERPPVP NQPIYALQEA FTGSTWQEKV SGVRSQMQKH QKVPTAVLLS
ALEETAWLFN LRASDIPYNP FFYSYTLLTD SSIRLFANKS RFSSETLSYL NSSCTGPMCV
QIEDYSQVRD SIQAYSLGDV RIWIGTSYTM YGIYEMIPKE KLVTDTYSPV MMTKAVKNSK
EQALLKASHV RDAVAVIRYL VWLEKNVPKG TVDEFSGAEI VDKFRGEEQF SSGPSFETIS
ASGLNAALAH YSPTKELNRK LSSDEMYLLD SGGQYWDGTT DITRTVHWGT PSAFQKEAYT
RVLIGNIDLS RLIFPAATSG RMVEAFARRA LWDAGLNYGH GTGHGIGNFL CVHEWPVGFQ
SNNIAMAKGM FTSIEPGYYK DGEFGIRLED VALVVEAKTK YPGSYLTFEV VSFVPYDRNL
IDVSLLSPEH LQYLNRYYQT IREKVGPELQ RRQLLEEFEW LQQHTEPLAA RAPDTASWAS
VLVVSTLAIL GWSV
