AMPN_HUMAN
ID AMPN_HUMAN Reviewed; 967 AA.
AC P15144; Q16728; Q6GT90; Q8IUK3; Q8IVH3; Q9UCE0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 4.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Aminopeptidase N {ECO:0000305};
DE Short=AP-N;
DE Short=hAPN;
DE EC=3.4.11.2 {ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:6149934, ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8887485};
DE AltName: Full=Alanyl aminopeptidase;
DE AltName: Full=Aminopeptidase M;
DE Short=AP-M;
DE AltName: Full=Microsomal aminopeptidase;
DE AltName: Full=Myeloid plasma membrane glycoprotein CD13;
DE AltName: Full=gp150;
DE AltName: CD_antigen=CD13;
GN Name=ANPEP; Synonyms=APN, CD13, PEPN;
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 VARIANTS GLN-86 AND MET-603.
RC TISSUE=Intestine;
RX PubMed=2901990; DOI=10.1016/0014-5793(88)80502-7;
RA Olsen J., Cowell G.M., Koenigshoefer E., Danielsen E.M., Moeller J.,
RA Laustsen L., Hansen O.C., Welinder K.G., Engberg J., Hunziker W.,
RA Spiess M., Sjoestroem H., Noren O.;
RT "Complete amino acid sequence of human intestinal aminopeptidase N as
RT deduced from cloned cDNA.";
RL FEBS Lett. 238:307-314(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21, VARIANT GLN-86, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2564851; DOI=10.1172/jci114015;
RA Look A.T., Ashmun R.A., Shapiro L.H., Peiper S.C.;
RT "Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to
RT aminopeptidase N.";
RL J. Clin. Invest. 83:1299-1307(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RC TISSUE=Intestinal epithelium;
RX PubMed=1675638; DOI=10.1016/s0021-9258(18)99056-3;
RA Shapiro L.H., Ashmun R.A., Roberts W.M., Look A.T.;
RT "Separate promoters control transcription of the human aminopeptidase N
RT gene in myeloid and intestinal epithelial cells.";
RL J. Biol. Chem. 266:11999-12007(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479 AND 524-967, AND VARIANT GLN-86.
RC TISSUE=Peripheral blood;
RA Eiz-Vesper B., Fuchs N., Gottschalk D., Mueller K., Reuter S., Blasczyk R.;
RT "Genomic organisation of aminopeptidase N.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 2-20 AND 70-81, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7576235; DOI=10.1515/bchm3.1995.376.7.397;
RA Watanabe Y., Iwaki-Egawa S., Mizukoshi H., Fujimoto Y.;
RT "Identification of an alanine aminopeptidase in human maternal serum as a
RT membrane-bound aminopeptidase N.";
RL Biol. Chem. Hoppe-Seyler 376:397-400(1995).
RN [8]
RP PROTEIN SEQUENCE OF 2-18, AND FUNCTION.
RX PubMed=8102610; DOI=10.1016/0014-5793(93)80199-5;
RA Nunez L., Amigo L., Rigotti A., Puglielli L., Mingrone G., Greco A.V.,
RA Nervi F.;
RT "Cholesterol crystallization-promoting activity of aminopeptidase-N
RT isolated from the vesicular carrier of biliary lipids.";
RL FEBS Lett. 329:84-88(1993).
RN [9]
RP CATALYTIC ACTIVITY, CHARACTERIZATION, AND SUBUNIT.
RX PubMed=6149934; DOI=10.1159/000469453;
RA Tokioka-Terao M., Hiwada K., Kokubu T.;
RT "Purification and characterization of aminopeptidase N from human plasma.";
RL Enzyme 32:65-75(1984).
RN [10]
RP GLYCOSYLATION.
RX PubMed=1705556; DOI=10.1016/s0021-9258(20)64364-2;
RA O'Connell P.J., Gerkis V., d'Apice A.J.F.;
RT "Variable O-glycosylation of CD13 (aminopeptidase N).";
RL J. Biol. Chem. 266:4593-4597(1991).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-229E SPIKE
RP GLYCOPROTEIN (MICROBIAL INFECTION), AND TOPOLOGY.
RX PubMed=1350662; DOI=10.1038/357420a0;
RA Yeager C.L., Ashmun R.A., Williams R.K., Cardellichio C.B., Shapiro L.H.,
RA Look A.T., Holmes K.V.;
RT "Human aminopeptidase N is a receptor for human coronavirus 229E.";
RL Nature 357:420-422(1992).
RN [12]
RP IDENTIFICATION OF SOLUBLE FORM, AND TISSUE SPECIFICITY.
RX PubMed=7902291;
RA Favaloro E.J., Browning T., Facey D.;
RT "CD13 (GP150; aminopeptidase-N): predominant functional activity in blood
RT is localized to plasma and is not cell-surface associated.";
RL Exp. Hematol. 21:1695-1701(1993).
RN [13]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=8105105; DOI=10.1128/jvi.67.11.6576-6585.1993;
RA Soderberg C., Giugni T.D., Zaia J.A., Larsson S., Wahlberg J.M., Moller E.;
RT "CD13 (human aminopeptidase N) mediates human cytomegalovirus infection.";
RL J. Virol. 67:6576-6585(1993).
RN [14]
RP CATALYTIC ACTIVITY, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH
RP HCOV-229E SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), REGION, AND MUTAGENESIS
RP OF HIS-392.
RX PubMed=8887485; DOI=10.1099/0022-1317-77-10-2515;
RA Kolb A.F., Maile J., Heister A., Siddell S.G.;
RT "Characterization of functional domains in the human coronavirus HCV 229E
RT receptor.";
RL J. Gen. Virol. 77:2515-2521(1996).
RN [15]
RP FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9056417; DOI=10.1006/excr.1996.3455;
RA Noren K., Hansen G.H., Clausen H., Noren O., Sjostrom H., Vogel L.K.;
RT "Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13)
RT is normally expressed at the cell surface and has full enzymatic
RT activity.";
RL Exp. Cell Res. 231:112-118(1997).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-229E SPIKE
RP GLYCOPROTEIN (MICROBIAL INFECTION), AND REGION.
RX PubMed=9367365; DOI=10.1099/0022-1317-78-11-2795;
RA Kolb A.F., Hegyi A., Siddell S.G.;
RT "Identification of residues critical for the human coronavirus 229E
RT receptor function of human aminopeptidase N.";
RL J. Gen. Virol. 78:2795-2802(1997).
RN [17]
RP FUNCTION, AND ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
RX PubMed=10605003; DOI=10.4049/jimmunol.164.1.129;
RA Dong X., An B., Salvucci Kierstead L., Storkus W.J., Amoscato A.A.,
RA Salter R.D.;
RT "Modification of the amino terminus of a class II epitope confers
RT resistance to degradation by CD13 on dendritic cells and enhances
RT presentation to T cells.";
RL J. Immunol. 164:129-135(2000).
RN [18]
RP ROLE IN ANGIOGENESIS, AND CHARACTERIZATION OF RECEPTOR FOR TUMOR-HOMING
RP PEPTIDES FUNCTION.
RX PubMed=10676659;
RA Pasqualini R., Koivunen E., Kain R., Lahdenranta J., Sakamoto M.,
RA Stryhn A., Ashmun R.A., Shapiro L.H., Arap W., Ruoslahti E.;
RT "Aminopeptidase N is a receptor for tumor-homing peptides and a target for
RT inhibiting angiogenesis.";
RL Cancer Res. 60:722-727(2000).
RN [19]
RP FUNCTION, AND INDUCTION BY ESTRADIOL AND IL8.
RX PubMed=11384645; DOI=10.1016/s0015-0282(01)01779-4;
RA Seli E., Senturk L.M., Bahtiyar O.M., Kayisli U.A., Arici A.;
RT "Expression of aminopeptidase N in human endometrium and regulation of its
RT activity by estrogen.";
RL Fertil. Steril. 75:1172-1176(2001).
RN [20]
RP MUTAGENESIS OF 288-ASP--SER-295 AND ASN-818.
RX PubMed=11559807; DOI=10.1128/jvi.75.20.9741-9752.2001;
RA Wentworth D.E., Holmes K.V.;
RT "Molecular determinants of species specificity in the coronavirus receptor
RT aminopeptidase N (CD13): influence of N-linked glycosylation.";
RL J. Virol. 75:9741-9752(2001).
RN [21]
RP FUNCTION OF SOLUBLE FORM.
RX PubMed=12473585;
RA van Hensbergen Y., Broxterman H.J., Hanemaaijer R., Jorna A.S.,
RA van Lent N.A., Verheul H.M., Pinedo H.M., Hoekman K.;
RT "Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions and
RT intratumoral fluid.";
RL Clin. Cancer Res. 8:3747-3754(2002).
RN [22]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HCOV-229E SPIKE
RP GLYCOPROTEIN.
RX PubMed=12551991; DOI=10.1128/jvi.77.4.2530-2538.2003;
RA Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.;
RT "Identification of a receptor-binding domain of the spike glycoprotein of
RT human coronavirus HCoV-229E.";
RL J. Virol. 77:2530-2538(2003).
RN [23]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265; ASN-681
RP AND ASN-818.
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 [25]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265; ASN-573;
RP ASN-681 AND ASN-818.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 66-967 IN COMPLEX WITH
RP ANGIOTENSIN-4 AND INHIBITORS, CATALYTIC ACTIVITY, COFACTOR,
RP SUBSTRATE-BINDING REGION, ZINC-BINDING SITES, ACTIVE SITE, GLYCOSYLATION AT
RP ASN-128; ASN-234; ASN-265; ASN-319; ASN-527; ASN-625; ASN-681 AND ASN-818,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=22932899; DOI=10.1074/jbc.m112.398842;
RA Wong A.H., Zhou D., Rini J.M.;
RT "The X-ray crystal structure of human aminopeptidase N reveals a novel
RT dimer and the basis for peptide processing.";
RL J. Biol. Chem. 287:36804-36813(2012).
RN [30]
RP VARIANTS TYR-242 AND PRO-243.
RX PubMed=9452074; DOI=10.1002/humu.1380110153;
RA Lendeckel U., Wex T., Arndt M., Frank K., Franke A., Ansorge S.;
RT "Identification of point mutations in the aminopeptidase N gene by SSCP
RT analysis and sequencing.";
RL Hum. Mutat. Suppl. 1:S158-S160(1998).
CC -!- FUNCTION: Broad specificity aminopeptidase which plays a role in the
CC final digestion of peptides generated from hydrolysis of proteins by
CC gastric and pancreatic proteases. Also involved in the processing of
CC various peptides including peptide hormones, such as angiotensin III
CC and IV, neuropeptides, and chemokines. May also be involved the
CC cleavage of peptides bound to major histocompatibility complex class II
CC molecules of antigen presenting cells. May have a role in angiogenesis
CC and promote cholesterol crystallization. May have a role in amino acid
CC transport by acting as binding partner of amino acid transporter
CC SLC6A19 and regulating its activity (By similarity).
CC {ECO:0000250|UniProtKB:P97449, ECO:0000269|PubMed:10605003,
CC ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645,
CC ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:7576235,
CC ECO:0000269|PubMed:8102610, ECO:0000269|PubMed:9056417}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for human
CC coronavirus 229E/HCoV-229E. In case of human coronavirus 229E (HCoV-
CC 229E) infection, serves as receptor for HCoV-229E spike glycoprotein.
CC {ECO:0000269|PubMed:12551991, ECO:0000269|PubMed:1350662,
CC ECO:0000269|PubMed:8887485, ECO:0000269|PubMed:9367365}.
CC -!- FUNCTION: (Microbial infection) Mediates as well Human cytomegalovirus
CC (HCMV) infection. {ECO:0000269|PubMed:8105105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:6149934,
CC ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8887485};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22932899};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22932899};
CC -!- SUBUNIT: Homodimer. Interacts with SLC6A19 (By similarity).
CC {ECO:0000250|UniProtKB:P97449, ECO:0000269|PubMed:22932899,
CC ECO:0000269|PubMed:6149934}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the S1 domain of human
CC coronavirus 229E/HCoV-229E spike protein. {ECO:0000269|PubMed:12551991,
CC ECO:0000269|PubMed:1350662, ECO:0000269|PubMed:8887485}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2564851,
CC ECO:0000269|PubMed:9056417}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:1350662}. Note=Also found as a soluble form.
CC {ECO:0000269|PubMed:7902291}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells of the kidney,
CC intestine, and respiratory tract; granulocytes, monocytes, fibroblasts,
CC endothelial cells, cerebral pericytes at the blood-brain barrier,
CC synaptic membranes of cells in the CNS. Also expressed in endometrial
CC stromal cells, but not in the endometrial glandular cells. Found in the
CC vasculature of tissues that undergo angiogenesis and in malignant
CC gliomas and lymph node metastases from multiple tumor types but not in
CC blood vessels of normal tissues. A soluble form has been found in
CC plasma. It is found to be elevated in plasma and effusions of cancer
CC patients. {ECO:0000269|PubMed:7902291}.
CC -!- INDUCTION: Estradiol and IL8/interleukin-8 decrease enzymatic activity
CC in vitro in endometrial stromal cells by 40% and 30%, respectively.
CC {ECO:0000269|PubMed:11384645}.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:15084671,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:1705556,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899,
CC ECO:0000269|PubMed:9056417}.
CC -!- PTM: May undergo proteolysis and give rise to a soluble form.
CC {ECO:0000269|PubMed:7902291}.
CC -!- MISCELLANEOUS: Found to serve as a receptor for tumor-homing peptides,
CC more specifically NGR peptides. It could serve thus as a target for
CC delivering drugs into tumors. Concentration in human hepatic bile,
CC varies from 17.3 to 57.6 micrograms/ml. {ECO:0000269|PubMed:10676659}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; X13276; CAA31640.1; -; mRNA.
DR EMBL; M22324; AAA51719.1; -; mRNA.
DR EMBL; AC018988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058928; AAH58928.1; -; mRNA.
DR EMBL; M55522; AAA83399.1; -; Genomic_DNA.
DR EMBL; AJ421875; CAD19098.2; -; Genomic_DNA.
DR EMBL; AJ421876; CAD19098.2; JOINED; Genomic_DNA.
DR EMBL; AJ426050; CAD19802.1; -; Genomic_DNA.
DR EMBL; AJ427985; CAD20931.1; -; Genomic_DNA.
DR EMBL; AJ427986; CAD20931.1; JOINED; Genomic_DNA.
DR EMBL; AJ427987; CAD20931.1; JOINED; Genomic_DNA.
DR EMBL; AJ427988; CAD20931.1; JOINED; Genomic_DNA.
DR CCDS; CCDS10356.1; -.
DR PIR; A30325; A30325.
DR RefSeq; NP_001141.2; NM_001150.2.
DR RefSeq; XP_005254949.1; XM_005254892.4.
DR RefSeq; XP_011519775.1; XM_011521473.1.
DR PDB; 4FYQ; X-ray; 1.90 A; A=66-967.
DR PDB; 4FYR; X-ray; 1.91 A; A=66-967.
DR PDB; 4FYS; X-ray; 2.01 A; A=66-967.
DR PDB; 4FYT; X-ray; 1.85 A; A=66-967.
DR PDB; 5LHD; X-ray; 2.60 A; A/B/C/D=36-967.
DR PDB; 6ATK; X-ray; 3.50 A; A/B/C=66-967.
DR PDB; 6U7E; X-ray; 3.00 A; A/B=66-967.
DR PDB; 6U7F; X-ray; 2.75 A; A/B=66-967.
DR PDB; 6U7G; X-ray; 2.35 A; A/B=66-967.
DR PDB; 6XWD; X-ray; 1.60 A; P=38-46.
DR PDB; 7AEW; X-ray; 1.20 A; BBB/CCC=36-73.
DR PDB; 7VPQ; X-ray; 3.10 A; A/C/E=62-963.
DR PDBsum; 4FYQ; -.
DR PDBsum; 4FYR; -.
DR PDBsum; 4FYS; -.
DR PDBsum; 4FYT; -.
DR PDBsum; 5LHD; -.
DR PDBsum; 6ATK; -.
DR PDBsum; 6U7E; -.
DR PDBsum; 6U7F; -.
DR PDBsum; 6U7G; -.
DR PDBsum; 6XWD; -.
DR PDBsum; 7AEW; -.
DR PDBsum; 7VPQ; -.
DR AlphaFoldDB; P15144; -.
DR SMR; P15144; -.
DR BioGRID; 106787; 162.
DR IntAct; P15144; 12.
DR MINT; P15144; -.
DR STRING; 9606.ENSP00000300060; -.
DR BindingDB; P15144; -.
DR ChEMBL; CHEMBL1907; -.
DR DrugBank; DB00973; Ezetimibe.
DR DrugBank; DB06773; Human calcitonin.
DR DrugBank; DB06196; Icatibant.
DR DrugBank; DB16627; Melphalan flufenamide.
DR DrugCentral; P15144; -.
DR GuidetoPHARMACOLOGY; 1560; -.
DR MEROPS; M01.001; -.
DR GlyConnect; 815; 35 N-Linked glycans (6 sites).
DR GlyGen; P15144; 17 sites, 44 N-linked glycans (7 sites), 7 O-linked glycans (4 sites).
DR iPTMnet; P15144; -.
DR MetOSite; P15144; -.
DR PhosphoSitePlus; P15144; -.
DR SwissPalm; P15144; -.
DR BioMuta; ANPEP; -.
DR DMDM; 143811362; -.
DR CPTAC; CPTAC-460; -.
DR CPTAC; CPTAC-461; -.
DR EPD; P15144; -.
DR jPOST; P15144; -.
DR MassIVE; P15144; -.
DR MaxQB; P15144; -.
DR PaxDb; P15144; -.
DR PeptideAtlas; P15144; -.
DR PRIDE; P15144; -.
DR ProteomicsDB; 53109; -.
DR ABCD; P15144; 5 sequenced antibodies.
DR Antibodypedia; 3713; 1941 antibodies from 48 providers.
DR DNASU; 290; -.
DR Ensembl; ENST00000300060.7; ENSP00000300060.6; ENSG00000166825.15.
DR Ensembl; ENST00000559874.2; ENSP00000452934.2; ENSG00000166825.15.
DR Ensembl; ENST00000560137.2; ENSP00000453413.2; ENSG00000166825.15.
DR Ensembl; ENST00000679248.1; ENSP00000502886.1; ENSG00000166825.15.
DR GeneID; 290; -.
DR KEGG; hsa:290; -.
DR MANE-Select; ENST00000300060.7; ENSP00000300060.6; NM_001150.3; NP_001141.2.
DR UCSC; uc002bop.5; human.
DR CTD; 290; -.
DR DisGeNET; 290; -.
DR GeneCards; ANPEP; -.
DR HGNC; HGNC:500; ANPEP.
DR HPA; ENSG00000166825; Group enriched (intestine, pancreas).
DR MIM; 151530; gene.
DR neXtProt; NX_P15144; -.
DR OpenTargets; ENSG00000166825; -.
DR PharmGKB; PA24815; -.
DR VEuPathDB; HostDB:ENSG00000166825; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000154876; -.
DR HOGENOM; CLU_003705_2_0_1; -.
DR InParanoid; P15144; -.
DR OMA; KWFIFNI; -.
DR OrthoDB; 110058at2759; -.
DR PhylomeDB; P15144; -.
DR TreeFam; TF300395; -.
DR BRENDA; 3.4.11.2; 2681.
DR PathwayCommons; P15144; -.
DR Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; P15144; -.
DR SignaLink; P15144; -.
DR SIGNOR; P15144; -.
DR BioGRID-ORCS; 290; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; ANPEP; human.
DR GeneWiki; Alanine_aminopeptidase; -.
DR GenomeRNAi; 290; -.
DR Pharos; P15144; Tchem.
DR PRO; PR:P15144; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P15144; protein.
DR Bgee; ENSG00000166825; Expressed in jejunal mucosa and 146 other tissues.
DR ExpressionAtlas; P15144; baseline and differential.
DR Genevisible; P15144; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Angiogenesis; Cell membrane;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Receptor; Reference proteome; Signal-anchor;
KW Sulfation; Transmembrane; Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2564851,
FT ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8102610"
FT CHAIN 2..967
FT /note="Aminopeptidase N"
FT /id="PRO_0000095081"
FT TOPO_DOM 2..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1350662"
FT TRANSMEM 9..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..967
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:1350662"
FT REGION 33..68
FT /note="Cytosolic Ser/Thr-rich junction"
FT REGION 40..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..967
FT /note="Metalloprotease"
FT REGION 288..295
FT /note="Necessary and sufficient to mediate interaction with
FT HCoV-229E"
FT /evidence="ECO:0000269|PubMed:1350662,
FT ECO:0000269|PubMed:8887485"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:22932899"
FT BINDING 352..356
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22932899"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22932899,
FT ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR,
FT ECO:0007744|PDB:4FYT"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22932899,
FT ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR,
FT ECO:0007744|PDB:4FYT"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:22932899,
FT ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR,
FT ECO:0007744|PDB:4FYT"
FT SITE 477
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:22932899"
FT MOD_RES 176
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 419
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 424
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 913
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:22932899"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22932899"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22932899"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22932899"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899"
FT DISULFID 761..768
FT /evidence="ECO:0000269|PubMed:22932899"
FT DISULFID 798..834
FT /evidence="ECO:0000269|PubMed:22932899"
FT VARIANT 20
FT /note="V -> M (in dbSNP:rs10152474)"
FT /id="VAR_031262"
FT VARIANT 86
FT /note="R -> Q (in dbSNP:rs25653)"
FT /evidence="ECO:0000269|PubMed:2564851,
FT ECO:0000269|PubMed:2901990, ECO:0000269|Ref.6"
FT /id="VAR_014736"
FT VARIANT 242
FT /note="D -> Y"
FT /evidence="ECO:0000269|PubMed:9452074"
FT /id="VAR_006727"
FT VARIANT 243
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:9452074"
FT /id="VAR_006728"
FT VARIANT 311
FT /note="A -> V (in dbSNP:rs17240268)"
FT /id="VAR_031263"
FT VARIANT 321
FT /note="T -> M (in dbSNP:rs8179199)"
FT /id="VAR_031264"
FT VARIANT 603
FT /note="I -> K (in dbSNP:rs17240212)"
FT /id="VAR_031265"
FT VARIANT 603
FT /note="I -> M (in dbSNP:rs8192297)"
FT /evidence="ECO:0000269|PubMed:2901990"
FT /id="VAR_031266"
FT VARIANT 752
FT /note="S -> N (in dbSNP:rs25651)"
FT /id="VAR_014737"
FT MUTAGEN 288..295
FT /note="DYVEKQAS->QSVEETAQ: No change in receptor activity
FT and HCoV-229E infection."
FT /evidence="ECO:0000269|PubMed:11559807"
FT MUTAGEN 288..295
FT /note="DYVEKQAS->QSVNEQAQ: No change in receptor activity
FT and HCoV-229E infection."
FT /evidence="ECO:0000269|PubMed:11559807"
FT MUTAGEN 288..295
FT /note="DYVEKQAS->QSVNETAQ: Complete loss of receptor
FT activity and blocks HCoV-229E infection. No loss of
FT enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11559807"
FT MUTAGEN 291..293
FT /note="EKQ->NKT: Complete loss of receptor activity and
FT blocks HCoV-229E infection. No loss of enzymatic activity."
FT MUTAGEN 291
FT /note="E->N: No change of receptor activity and HCoV-229E
FT infection."
FT MUTAGEN 293
FT /note="Q->T: No change of receptor activity and HCoV-229E
FT infection."
FT MUTAGEN 392
FT /note="H->A: Loss of aminopeptidase activity."
FT /evidence="ECO:0000269|PubMed:8887485"
FT MUTAGEN 818
FT /note="N->E: Very low receptor activity and HCoV-229E
FT infection."
FT /evidence="ECO:0000269|PubMed:11559807"
FT CONFLICT 536
FT /note="V -> E (in Ref. 1; CAA31640)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="L -> P (in Ref. 1; CAA31640)"
FT /evidence="ECO:0000305"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 78..91
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 102..115
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5LHD"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 188..200
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 315..331
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 376..394
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 408..425
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 440..447
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 493..507
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 514..527
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 536..544
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 556..559
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 560..565
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:4FYT"
FT STRAND 631..634
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 636..649
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 655..670
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 676..681
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 682..688
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 692..709
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 715..736
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 737..741
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 747..762
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 766..781
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 790..792
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 793..803
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 806..817
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 822..832
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 838..848
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 851..853
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 856..858
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 859..868
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 872..882
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 884..890
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 891..894
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 898..906
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 912..924
FT /evidence="ECO:0007829|PDB:4FYT"
FT TURN 925..928
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:4FYT"
FT HELIX 934..965
FT /evidence="ECO:0007829|PDB:4FYT"
SQ SEQUENCE 967 AA; 109540 MW; 37B6BC1BF0D6B1F2 CRC64;
MAKGFYISKS LGILGILLGV AAVCTIIALS VVYSQEKNKN ANSSPVASTT PSASATTNPA
SATTLDQSKA WNRYRLPNTL KPDSYRVTLR PYLTPNDRGL YVFKGSSTVR FTCKEATDVI
IIHSKKLNYT LSQGHRVVLR GVGGSQPPDI DKTELVEPTE YLVVHLKGSL VKDSQYEMDS
EFEGELADDL AGFYRSEYME GNVRKVVATT QMQAADARKS FPCFDEPAMK AEFNITLIHP
KDLTALSNML PKGPSTPLPE DPNWNVTEFH TTPKMSTYLL AFIVSEFDYV EKQASNGVLI
RIWARPSAIA AGHGDYALNV TGPILNFFAG HYDTPYPLPK SDQIGLPDFN AGAMENWGLV
TYRENSLLFD PLSSSSSNKE RVVTVIAHEL AHQWFGNLVT IEWWNDLWLN EGFASYVEYL
GADYAEPTWN LKDLMVLNDV YRVMAVDALA SSHPLSTPAS EINTPAQISE LFDAISYSKG
ASVLRMLSSF LSEDVFKQGL ASYLHTFAYQ NTIYLNLWDH LQEAVNNRSI QLPTTVRDIM
NRWTLQMGFP VITVDTSTGT LSQEHFLLDP DSNVTRPSEF NYVWIVPITS IRDGRQQQDY
WLIDVRAQND LFSTSGNEWV LLNLNVTGYY RVNYDEENWR KIQTQLQRDH SAIPVINRAQ
IINDAFNLAS AHKVPVTLAL NNTLFLIEER QYMPWEAALS SLSYFKLMFD RSEVYGPMKN
YLKKQVTPLF IHFRNNTNNW REIPENLMDQ YSEVNAISTA CSNGVPECEE MVSGLFKQWM
ENPNNNPIHP NLRSTVYCNA IAQGGEEEWD FAWEQFRNAT LVNEADKLRA ALACSKELWI
LNRYLSYTLN PDLIRKQDAT STIISITNNV IGQGLVWDFV QSNWKKLFND YGGGSFSFSN
LIQAVTRRFS TEYELQQLEQ FKKDNEETGF GSGTRALEQA LEKTKANIKW VKENKEVVLQ
WFTENSK
