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Aminopeptidase N (AP-N) (hAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Microsomal aminopeptidase) (Myeloid plasma membrane glycoprotein CD13) (gp150) (CD antigen CD13)

 AMPN_HUMAN              Reviewed;         967 AA.
P15144; Q16728; Q6GT90; Q8IUK3; Q8IVH3; Q9UCE0;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 4.
31-JAN-2018, entry version 206.
RecName: Full=Aminopeptidase N {ECO:0000305};
Short=AP-N;
Short=hAPN;
EC=3.4.11.2 {ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:6149934, ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8887485};
AltName: Full=Alanyl aminopeptidase;
AltName: Full=Aminopeptidase M;
Short=AP-M;
AltName: Full=Microsomal aminopeptidase;
AltName: Full=Myeloid plasma membrane glycoprotein CD13;
AltName: Full=gp150;
AltName: CD_antigen=CD13;
Name=ANPEP; Synonyms=APN, CD13, PEPN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLN-86 AND MET-603.
TISSUE=Intestine;
PubMed=2901990; DOI=10.1016/0014-5793(88)80502-7;
Olsen J., Cowell G.M., Koenigshoefer E., Danielsen E.M., Moeller J.,
Laustsen L., Hansen O.C., Welinder K.G., Engberg J., Hunziker W.,
Spiess M., Sjoestroem H., Noren O.;
"Complete amino acid sequence of human intestinal aminopeptidase N as
deduced from cloned cDNA.";
FEBS Lett. 238:307-314(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21, VARIANT GLN-86,
AND SUBCELLULAR LOCATION.
PubMed=2564851; DOI=10.1172/JCI114015;
Look A.T., Ashmun R.A., Shapiro L.H., Peiper S.C.;
"Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical
to aminopeptidase N.";
J. Clin. Invest. 83:1299-1307(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
TISSUE=Intestinal epithelium;
PubMed=1675638;
Shapiro L.H., Ashmun R.A., Roberts W.M., Look A.T.;
"Separate promoters control transcription of the human aminopeptidase
N gene in myeloid and intestinal epithelial cells.";
J. Biol. Chem. 266:11999-12007(1991).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479 AND 524-967, AND VARIANT
GLN-86.
TISSUE=Peripheral blood;
Eiz-Vesper B., Fuchs N., Gottschalk D., Mueller K., Reuter S.,
Blasczyk R.;
"Genomic organisation of aminopeptidase N.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 2-20 AND 70-81, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=7576235; DOI=10.1515/bchm3.1995.376.7.397;
Watanabe Y., Iwaki-Egawa S., Mizukoshi H., Fujimoto Y.;
"Identification of an alanine aminopeptidase in human maternal serum
as a membrane-bound aminopeptidase N.";
Biol. Chem. Hoppe-Seyler 376:397-400(1995).
[8]
PROTEIN SEQUENCE OF 2-18, AND FUNCTION.
PubMed=8102610; DOI=10.1016/0014-5793(93)80199-5;
Nunez L., Amigo L., Rigotti A., Puglielli L., Mingrone G., Greco A.V.,
Nervi F.;
"Cholesterol crystallization-promoting activity of aminopeptidase-N
isolated from the vesicular carrier of biliary lipids.";
FEBS Lett. 329:84-88(1993).
[9]
CATALYTIC ACTIVITY, CHARACTERIZATION, AND SUBUNIT.
PubMed=6149934;
Tokioka-Terao M., Hiwada K., Kokubu T.;
"Purification and characterization of aminopeptidase N from human
plasma.";
Enzyme 32:65-75(1984).
[10]
GLYCOSYLATION.
PubMed=1705556;
O'Connell P.J., Gerkis V., d'Apice A.J.F.;
"Variable O-glycosylation of CD13 (aminopeptidase N).";
J. Biol. Chem. 266:4593-4597(1991).
[11]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-229E SPIKE
GLYCOPROTEIN (MICROBIAL INFECTION), AND TOPOLOGY.
PubMed=1350662; DOI=10.1038/357420a0;
Yeager C.L., Ashmun R.A., Williams R.K., Cardellichio C.B.,
Shapiro L.H., Look A.T., Holmes K.V.;
"Human aminopeptidase N is a receptor for human coronavirus 229E.";
Nature 357:420-422(1992).
[12]
IDENTIFICATION OF SOLUBLE FORM, AND TISSUE SPECIFICITY.
PubMed=7902291;
Favaloro E.J., Browning T., Facey D.;
"CD13 (GP150; aminopeptidase-N): predominant functional activity in
blood is localized to plasma and is not cell-surface associated.";
Exp. Hematol. 21:1695-1701(1993).
[13]
FUNCTION (MICROBIAL INFECTION).
PubMed=8105105;
Soderberg C., Giugni T.D., Zaia J.A., Larsson S., Wahlberg J.M.,
Moller E.;
"CD13 (human aminopeptidase N) mediates human cytomegalovirus
infection.";
J. Virol. 67:6576-6585(1993).
[14]
CATALYTIC ACTIVITY, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH
HCOV-229E SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), REGION, AND
MUTAGENESIS OF HIS-392.
PubMed=8887485; DOI=10.1099/0022-1317-77-10-2515;
Kolb A.F., Maile J., Heister A., Siddell S.G.;
"Characterization of functional domains in the human coronavirus HCV
229E receptor.";
J. Gen. Virol. 77:2515-2521(1996).
[15]
FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=9056417; DOI=10.1006/excr.1996.3455;
Noren K., Hansen G.H., Clausen H., Noren O., Sjostrom H., Vogel L.K.;
"Defectively N-glycosylated and non-O-glycosylated aminopeptidase N
(CD13) is normally expressed at the cell surface and has full
enzymatic activity.";
Exp. Cell Res. 231:112-118(1997).
[16]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-229E SPIKE
GLYCOPROTEIN (MICROBIAL INFECTION), AND REGION.
PubMed=9367365;
Kolb A.F., Hegyi A., Siddell S.G.;
"Identification of residues critical for the human coronavirus 229E
receptor function of human aminopeptidase N.";
J. Gen. Virol. 78:2795-2802(1997).
[17]
FUNCTION, AND ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II
MHC.
PubMed=10605003; DOI=10.4049/jimmunol.164.1.129;
Dong X., An B., Salvucci Kierstead L., Storkus W.J., Amoscato A.A.,
Salter R.D.;
"Modification of the amino terminus of a class II epitope confers
resistance to degradation by CD13 on dendritic cells and enhances
presentation to T cells.";
J. Immunol. 164:129-135(2000).
[18]
ROLE IN ANGIOGENESIS, AND CHARACTERIZATION OF RECEPTOR FOR
TUMOR-HOMING PEPTIDES FUNCTION.
PubMed=10676659;
Pasqualini R., Koivunen E., Kain R., Lahdenranta J., Sakamoto M.,
Stryhn A., Ashmun R.A., Shapiro L.H., Arap W., Ruoslahti E.;
"Aminopeptidase N is a receptor for tumor-homing peptides and a target
for inhibiting angiogenesis.";
Cancer Res. 60:722-727(2000).
[19]
FUNCTION, AND INDUCTION BY ESTRADIOL AND IL8.
PubMed=11384645; DOI=10.1016/S0015-0282(01)01779-4;
Seli E., Senturk L.M., Bahtiyar O.M., Kayisli U.A., Arici A.;
"Expression of aminopeptidase N in human endometrium and regulation of
its activity by estrogen.";
Fertil. Steril. 75:1172-1176(2001).
[20]
MUTAGENESIS OF 288-ASP--SER-295 AND ASN-818.
PubMed=11559807; DOI=10.1128/JVI.75.20.9741-9752.2001;
Wentworth D.E., Holmes K.V.;
"Molecular determinants of species specificity in the coronavirus
receptor aminopeptidase N (CD13): influence of N-linked
glycosylation.";
J. Virol. 75:9741-9752(2001).
[21]
FUNCTION OF SOLUBLE FORM.
PubMed=12473585;
van Hensbergen Y., Broxterman H.J., Hanemaaijer R., Jorna A.S.,
van Lent N.A., Verheul H.M., Pinedo H.M., Hoekman K.;
"Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions
and intratumoral fluid.";
Clin. Cancer Res. 8:3747-3754(2002).
[22]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HCOV-229E SPIKE
GLYCOPROTEIN.
PubMed=12551991; DOI=10.1128/JVI.77.4.2530-2538.2003;
Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.;
"Identification of a receptor-binding domain of the spike glycoprotein
of human coronavirus HCoV-229E.";
J. Virol. 77:2530-2538(2003).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265;
ASN-681 AND ASN-818.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265;
ASN-573; ASN-681 AND ASN-818.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 66-967 IN COMPLEX WITH
ANGIOTENSIN-4 AND INHIBITORS, CATALYTIC ACTIVITY, COFACTOR,
SUBSTRATE-BINDING REGION, ZINC-BINDING SITES, ACTIVE SITE,
GLYCOSYLATION AT ASN-128; ASN-234; ASN-265; ASN-319; ASN-527; ASN-625;
ASN-681 AND ASN-818, SUBUNIT, AND DISULFIDE BONDS.
PubMed=22932899; DOI=10.1074/jbc.M112.398842;
Wong A.H., Zhou D., Rini J.M.;
"The X-ray crystal structure of human aminopeptidase N reveals a novel
dimer and the basis for peptide processing.";
J. Biol. Chem. 287:36804-36813(2012).
[30]
VARIANTS TYR-242 AND PRO-243.
PubMed=9452074;
Lendeckel U., Wex T., Arndt M., Frank K., Franke A., Ansorge S.;
"Identification of point mutations in the aminopeptidase N gene by
SSCP analysis and sequencing.";
Hum. Mutat. Suppl. 1:S158-S160(1998).
-!- FUNCTION: Broad specificity aminopeptidase which plays a role in
the final digestion of peptides generated from hydrolysis of
proteins by gastric and pancreatic proteases. Also involved in the
processing of various peptides including peptide hormones, such as
angiotensin III and IV, neuropeptides, and chemokines. May also be
involved the cleavage of peptides bound to major
histocompatibility complex class II molecules of antigen
presenting cells. May have a role in angiogenesis and promote
cholesterol crystallization. {ECO:0000269|PubMed:10605003,
ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645,
ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:7576235,
ECO:0000269|PubMed:8102610, ECO:0000269|PubMed:9056417}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for human
coronavirus 229E/HCoV-229E. In case of human coronavirus 229E
(HCoV-229E) infection, serves as receptor for HCoV-229E spike
glycoprotein (PubMed:1350662, PubMed:8887485, PubMed:9367365,
PubMed:12551991). Mediates as well human cytomegalovirus (HCMV)
infection (PubMed:8105105). {ECO:0000269|PubMed:12551991,
ECO:0000269|PubMed:1350662, ECO:0000269|PubMed:8105105,
ECO:0000269|PubMed:8887485, ECO:0000269|PubMed:9367365}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala,
but may be most amino acids including Pro (slow action). When a
terminal hydrophobic residue is followed by a prolyl residue, the
two may be released as an intact Xaa-Pro dipeptide.
{ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:6149934,
ECO:0000269|PubMed:7576235, ECO:0000269|PubMed:8887485}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:22932899};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22932899};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22932899,
ECO:0000269|PubMed:6149934}.
-!- SUBUNIT: (Microbial infection) Interacts with the S1 domain of
human coronavirus 229E/HCoV-229E spike protein.
{ECO:0000269|PubMed:12551991, ECO:0000269|PubMed:1350662,
ECO:0000269|PubMed:8887485}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2564851,
ECO:0000269|PubMed:9056417}; Single-pass type II membrane protein
{ECO:0000305|PubMed:1350662}. Note=Also found as a soluble form.
{ECO:0000269|PubMed:7902291}.
-!- TISSUE SPECIFICITY: Expressed in epithelial cells of the kidney,
intestine, and respiratory tract; granulocytes, monocytes,
fibroblasts, endothelial cells, cerebral pericytes at the blood-
brain barrier, synaptic membranes of cells in the CNS. Also
expressed in endometrial stromal cells, but not in the endometrial
glandular cells. Found in the vasculature of tissues that undergo
angiogenesis and in malignant gliomas and lymph node metastases
from multiple tumor types but not in blood vessels of normal
tissues. A soluble form has been found in plasma. It is found to
be elevated in plasma and effusions of cancer patients.
{ECO:0000269|PubMed:7902291}.
-!- INDUCTION: Estradiol and IL8/interleukin-8 decrease enzymatic
activity in vitro in endometrial stromal cells by 40% and 30%,
respectively. {ECO:0000269|PubMed:11384645}.
-!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:1705556,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899,
ECO:0000269|PubMed:9056417}.
-!- PTM: May undergo proteolysis and give rise to a soluble form.
{ECO:0000269|PubMed:7902291}.
-!- MISCELLANEOUS: Found to serve as a receptor for tumor-homing
peptides, more specifically NGR peptides. It could serve thus as a
target for delivering drugs into tumors. Concentration in human
hepatic bile, varies from 17.3 to 57.6 micrograms/ml.
{ECO:0000269|PubMed:10676659}.
-!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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EMBL; X13276; CAA31640.1; -; mRNA.
EMBL; M22324; AAA51719.1; -; mRNA.
EMBL; AC018988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC058928; AAH58928.1; -; mRNA.
EMBL; M55522; AAA83399.1; -; Genomic_DNA.
EMBL; AJ421875; CAD19098.2; -; Genomic_DNA.
EMBL; AJ421876; CAD19098.2; JOINED; Genomic_DNA.
EMBL; AJ426050; CAD19802.1; -; Genomic_DNA.
EMBL; AJ427985; CAD20931.1; -; Genomic_DNA.
EMBL; AJ427986; CAD20931.1; JOINED; Genomic_DNA.
EMBL; AJ427987; CAD20931.1; JOINED; Genomic_DNA.
EMBL; AJ427988; CAD20931.1; JOINED; Genomic_DNA.
CCDS; CCDS10356.1; -.
PIR; A30325; A30325.
RefSeq; NP_001141.2; NM_001150.2.
RefSeq; XP_005254949.1; XM_005254892.4.
RefSeq; XP_011519775.1; XM_011521473.1.
UniGene; Hs.1239; -.
PDB; 4FYQ; X-ray; 1.90 A; A=66-967.
PDB; 4FYR; X-ray; 1.91 A; A=66-967.
PDB; 4FYS; X-ray; 2.01 A; A=66-967.
PDB; 4FYT; X-ray; 1.85 A; A=66-967.
PDB; 5LHD; X-ray; 2.60 A; A/B/C/D=36-967.
PDB; 6ATK; X-ray; 3.50 A; A/B/C=66-967.
PDBsum; 4FYQ; -.
PDBsum; 4FYR; -.
PDBsum; 4FYS; -.
PDBsum; 4FYT; -.
PDBsum; 5LHD; -.
PDBsum; 6ATK; -.
ProteinModelPortal; P15144; -.
SMR; P15144; -.
BioGrid; 106787; 3.
IntAct; P15144; 5.
STRING; 9606.ENSP00000300060; -.
BindingDB; P15144; -.
ChEMBL; CHEMBL1907; -.
DrugBank; DB00973; Ezetimibe.
DrugBank; DB06196; Icatibant.
GuidetoPHARMACOLOGY; 1560; -.
MEROPS; M01.001; -.
iPTMnet; P15144; -.
PhosphoSitePlus; P15144; -.
SwissPalm; P15144; -.
UniCarbKB; P15144; -.
BioMuta; ANPEP; -.
DMDM; 143811362; -.
EPD; P15144; -.
MaxQB; P15144; -.
PaxDb; P15144; -.
PeptideAtlas; P15144; -.
PRIDE; P15144; -.
DNASU; 290; -.
Ensembl; ENST00000300060; ENSP00000300060; ENSG00000166825.
GeneID; 290; -.
KEGG; hsa:290; -.
UCSC; uc002bop.5; human.
CTD; 290; -.
DisGeNET; 290; -.
EuPathDB; HostDB:ENSG00000166825.13; -.
GeneCards; ANPEP; -.
H-InvDB; HIX0038141; -.
HGNC; HGNC:500; ANPEP.
HPA; CAB002417; -.
HPA; HPA004625; -.
MIM; 151530; gene.
neXtProt; NX_P15144; -.
OpenTargets; ENSG00000166825; -.
PharmGKB; PA24815; -.
eggNOG; KOG1046; Eukaryota.
eggNOG; COG0308; LUCA.
GeneTree; ENSGT00760000119082; -.
HOVERGEN; HBG006616; -.
InParanoid; P15144; -.
KO; K11140; -.
OMA; PTWNLKD; -.
OrthoDB; EOG091G01GH; -.
PhylomeDB; P15144; -.
TreeFam; TF300395; -.
BRENDA; 3.4.11.2; 2681.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P15144; -.
SIGNOR; P15144; -.
ChiTaRS; ANPEP; human.
GeneWiki; Alanine_aminopeptidase; -.
GenomeRNAi; 290; -.
PRO; PR:P15144; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000166825; -.
CleanEx; HS_ANPEP; -.
ExpressionAtlas; P15144; baseline and differential.
Genevisible; P15144; HS.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
GO; GO:0042277; F:peptide binding; IBA:GO_Central.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
CDD; cd09601; M1_APN_2; 1.
InterPro; IPR024571; ERAP1-like_C_dom.
InterPro; IPR034016; M1_APN-typ.
InterPro; IPR001930; Peptidase_M1.
InterPro; IPR014782; Peptidase_M1_N.
PANTHER; PTHR11533; PTHR11533; 1.
Pfam; PF11838; ERAP1_C; 1.
Pfam; PF01433; Peptidase_M1; 1.
PRINTS; PR00756; ALADIPTASE.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Aminopeptidase; Angiogenesis; Cell membrane;
Complete proteome; Developmental protein; Differentiation;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease;
Receptor; Reference proteome; Signal-anchor; Sulfation; Transmembrane;
Transmembrane helix; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2564851,
ECO:0000269|PubMed:7576235,
ECO:0000269|PubMed:8102610}.
CHAIN 2 967 Aminopeptidase N.
/FTId=PRO_0000095081.
TOPO_DOM 2 8 Cytoplasmic.
{ECO:0000305|PubMed:1350662}.
TRANSMEM 9 32 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 33 967 Extracellular.
{ECO:0000269|PubMed:1350662}.
REGION 33 68 Cytosolic Ser/Thr-rich junction.
REGION 69 967 Metalloprotease.
REGION 288 295 Necessary and sufficient to mediate
interaction with HCoV-229E.
{ECO:0000269|PubMed:1350662,
ECO:0000269|PubMed:8887485}.
REGION 352 356 Substrate binding.
{ECO:0000269|PubMed:22932899}.
ACT_SITE 389 389 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10095,
ECO:0000269|PubMed:22932899}.
METAL 388 388 Zinc; catalytic. {ECO:0000244|PDB:4FYQ,
ECO:0000244|PDB:4FYR,
ECO:0000244|PDB:4FYT,
ECO:0000269|PubMed:22932899}.
METAL 392 392 Zinc; catalytic. {ECO:0000244|PDB:4FYQ,
ECO:0000244|PDB:4FYR,
ECO:0000244|PDB:4FYT,
ECO:0000269|PubMed:22932899}.
METAL 411 411 Zinc; catalytic. {ECO:0000244|PDB:4FYQ,
ECO:0000244|PDB:4FYR,
ECO:0000244|PDB:4FYT,
ECO:0000269|PubMed:22932899}.
SITE 477 477 Transition state stabilizer.
{ECO:0000269|PubMed:22932899}.
MOD_RES 176 176 Sulfotyrosine. {ECO:0000255}.
MOD_RES 419 419 Sulfotyrosine. {ECO:0000255}.
MOD_RES 424 424 Sulfotyrosine. {ECO:0000255}.
MOD_RES 913 913 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:22932899}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:22932899}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:22932899}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22932899}.
CARBOHYD 527 527 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22932899}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 625 625 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22932899}.
CARBOHYD 681 681 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:22932899}.
CARBOHYD 735 735 N-linked (GlcNAc...) asparagine.
CARBOHYD 818 818 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:22932899}.
DISULFID 761 768 {ECO:0000269|PubMed:22932899}.
DISULFID 798 834 {ECO:0000269|PubMed:22932899}.
VARIANT 20 20 V -> M (in dbSNP:rs10152474).
/FTId=VAR_031262.
VARIANT 86 86 R -> Q (in dbSNP:rs25653).
{ECO:0000269|PubMed:2564851,
ECO:0000269|PubMed:2901990,
ECO:0000269|Ref.6}.
/FTId=VAR_014736.
VARIANT 242 242 D -> Y. {ECO:0000269|PubMed:9452074}.
/FTId=VAR_006727.
VARIANT 243 243 L -> P. {ECO:0000269|PubMed:9452074}.
/FTId=VAR_006728.
VARIANT 311 311 A -> V (in dbSNP:rs17240268).
/FTId=VAR_031263.
VARIANT 321 321 T -> M (in dbSNP:rs8179199).
/FTId=VAR_031264.
VARIANT 603 603 I -> K (in dbSNP:rs17240212).
/FTId=VAR_031265.
VARIANT 603 603 I -> M (in dbSNP:rs8192297).
{ECO:0000269|PubMed:2901990}.
/FTId=VAR_031266.
VARIANT 752 752 S -> N (in dbSNP:rs25651).
/FTId=VAR_014737.
MUTAGEN 288 295 DYVEKQAS->QSVEETAQ: No change in receptor
activity and HCoV-229E infection.
{ECO:0000269|PubMed:11559807}.
MUTAGEN 288 295 DYVEKQAS->QSVNEQAQ: No change in receptor
activity and HCoV-229E infection.
{ECO:0000269|PubMed:11559807}.
MUTAGEN 288 295 DYVEKQAS->QSVNETAQ: Complete loss of
receptor activity and blocks HCoV-229E
infection. No loss of enzymatic activity.
{ECO:0000269|PubMed:11559807}.
MUTAGEN 291 293 EKQ->NKT: Complete loss of receptor
activity and blocks HCoV-229E infection.
No loss of enzymatic activity.
MUTAGEN 291 291 E->N: No change of receptor activity and
HCoV-229E infection.
MUTAGEN 293 293 Q->T: No change of receptor activity and
HCoV-229E infection.
MUTAGEN 392 392 H->A: Loss of aminopeptidase activity.
{ECO:0000269|PubMed:8887485}.
MUTAGEN 818 818 N->E: Very low receptor activity and
HCoV-229E infection.
{ECO:0000269|PubMed:11559807}.
CONFLICT 536 536 V -> E (in Ref. 1; CAA31640).
{ECO:0000305}.
CONFLICT 887 887 L -> P (in Ref. 1; CAA31640).
{ECO:0000305}.
HELIX 70 72 {ECO:0000244|PDB:4FYT}.
STRAND 73 75 {ECO:0000244|PDB:4FYT}.
STRAND 78 91 {ECO:0000244|PDB:4FYT}.
STRAND 102 115 {ECO:0000244|PDB:4FYT}.
STRAND 118 123 {ECO:0000244|PDB:4FYT}.
STRAND 126 129 {ECO:0000244|PDB:5LHD}.
STRAND 135 142 {ECO:0000244|PDB:4FYT}.
STRAND 150 156 {ECO:0000244|PDB:4FYT}.
TURN 157 160 {ECO:0000244|PDB:4FYT}.
STRAND 161 168 {ECO:0000244|PDB:4FYT}.
STRAND 175 185 {ECO:0000244|PDB:4FYT}.
STRAND 188 200 {ECO:0000244|PDB:4FYT}.
STRAND 203 211 {ECO:0000244|PDB:4FYT}.
TURN 213 216 {ECO:0000244|PDB:4FYT}.
HELIX 217 219 {ECO:0000244|PDB:4FYT}.
STRAND 231 240 {ECO:0000244|PDB:4FYT}.
STRAND 243 249 {ECO:0000244|PDB:4FYT}.
STRAND 251 253 {ECO:0000244|PDB:4FYT}.
STRAND 256 258 {ECO:0000244|PDB:4FYT}.
STRAND 261 269 {ECO:0000244|PDB:4FYT}.
HELIX 277 279 {ECO:0000244|PDB:4FYT}.
STRAND 282 285 {ECO:0000244|PDB:4FYT}.
STRAND 288 293 {ECO:0000244|PDB:4FYT}.
STRAND 299 304 {ECO:0000244|PDB:4FYT}.
HELIX 306 310 {ECO:0000244|PDB:4FYT}.
TURN 311 314 {ECO:0000244|PDB:4FYT}.
HELIX 315 331 {ECO:0000244|PDB:4FYT}.
STRAND 338 348 {ECO:0000244|PDB:4FYT}.
STRAND 350 354 {ECO:0000244|PDB:4FYT}.
STRAND 359 363 {ECO:0000244|PDB:4FYT}.
HELIX 364 367 {ECO:0000244|PDB:4FYT}.
TURN 371 373 {ECO:0000244|PDB:4FYT}.
HELIX 376 394 {ECO:0000244|PDB:4FYT}.
TURN 396 398 {ECO:0000244|PDB:4FYT}.
STRAND 399 403 {ECO:0000244|PDB:4FYT}.
HELIX 404 407 {ECO:0000244|PDB:4FYT}.
HELIX 408 425 {ECO:0000244|PDB:4FYT}.
HELIX 427 429 {ECO:0000244|PDB:4FYT}.
HELIX 431 434 {ECO:0000244|PDB:4FYT}.
HELIX 435 438 {ECO:0000244|PDB:4FYT}.
HELIX 440 447 {ECO:0000244|PDB:4FYT}.
HELIX 459 461 {ECO:0000244|PDB:4FYT}.
HELIX 465 470 {ECO:0000244|PDB:4FYT}.
HELIX 474 491 {ECO:0000244|PDB:4FYT}.
HELIX 493 507 {ECO:0000244|PDB:4FYT}.
STRAND 510 512 {ECO:0000244|PDB:4FYT}.
HELIX 514 527 {ECO:0000244|PDB:4FYT}.
HELIX 536 544 {ECO:0000244|PDB:4FYT}.
STRAND 550 555 {ECO:0000244|PDB:4FYT}.
TURN 556 559 {ECO:0000244|PDB:4FYT}.
STRAND 560 565 {ECO:0000244|PDB:4FYT}.
TURN 579 582 {ECO:0000244|PDB:4FYT}.
STRAND 586 588 {ECO:0000244|PDB:4FYT}.
STRAND 590 592 {ECO:0000244|PDB:4FYT}.
STRAND 600 602 {ECO:0000244|PDB:4FYT}.
STRAND 604 608 {ECO:0000244|PDB:4FYT}.
HELIX 610 612 {ECO:0000244|PDB:4FYT}.
STRAND 620 623 {ECO:0000244|PDB:4FYT}.
HELIX 624 626 {ECO:0000244|PDB:4FYT}.
STRAND 631 634 {ECO:0000244|PDB:4FYT}.
HELIX 636 649 {ECO:0000244|PDB:4FYT}.
HELIX 650 652 {ECO:0000244|PDB:4FYT}.
HELIX 655 670 {ECO:0000244|PDB:4FYT}.
HELIX 676 681 {ECO:0000244|PDB:4FYT}.
HELIX 682 688 {ECO:0000244|PDB:4FYT}.
HELIX 692 709 {ECO:0000244|PDB:4FYT}.
HELIX 715 736 {ECO:0000244|PDB:4FYT}.
TURN 737 741 {ECO:0000244|PDB:4FYT}.
HELIX 747 762 {ECO:0000244|PDB:4FYT}.
HELIX 766 781 {ECO:0000244|PDB:4FYT}.
HELIX 790 792 {ECO:0000244|PDB:4FYT}.
HELIX 793 803 {ECO:0000244|PDB:4FYT}.
HELIX 806 817 {ECO:0000244|PDB:4FYT}.
HELIX 822 832 {ECO:0000244|PDB:4FYT}.
HELIX 838 848 {ECO:0000244|PDB:4FYT}.
TURN 851 853 {ECO:0000244|PDB:4FYT}.
HELIX 856 858 {ECO:0000244|PDB:4FYT}.
HELIX 859 868 {ECO:0000244|PDB:4FYT}.
HELIX 872 882 {ECO:0000244|PDB:4FYT}.
HELIX 884 890 {ECO:0000244|PDB:4FYT}.
TURN 891 894 {ECO:0000244|PDB:4FYT}.
HELIX 898 906 {ECO:0000244|PDB:4FYT}.
HELIX 912 924 {ECO:0000244|PDB:4FYT}.
TURN 925 928 {ECO:0000244|PDB:4FYT}.
HELIX 931 933 {ECO:0000244|PDB:4FYT}.
HELIX 934 965 {ECO:0000244|PDB:4FYT}.
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


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