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 27-MAR-2024, entry version 244. 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}. 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; 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; 177. 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 GlyCosmos; P15144; 15 sites, 51 glycans. DR GlyGen; P15144; 18 sites, 44 N-linked glycans (7 sites), 9 O-linked glycans (5 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; 9606-ENSP00000300060; -. DR PeptideAtlas; P15144; -. DR ProteomicsDB; 53109; -. DR Pumba; P15144; -. DR ABCD; P15144; 5 sequenced antibodies. DR Antibodypedia; 3713; 2164 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 AGR; HGNC:500; -. 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; TTVRNIM; -. DR OrthoDB; 3085317at2759; -. 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; 10 hits in 1157 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 148 other cell types or tissues. DR ExpressionAtlas; P15144; baseline and differential. 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: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 CDD; cd09601; M1_APN-Q_like; 1. DR Gene3D; 1.25.50.20; -; 1. DR Gene3D; 2.60.40.1910; -; 1. DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1. DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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 PANTHER; PTHR11533:SF172; AMINOPEPTIDASE N; 1. DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1. 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; Leukotriene A4 hydrolase N-terminal domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; P15144; HS. 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 STRAND 742..746 FT /evidence="ECO:0007829|PDB:7VPQ" 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 //