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Aminopeptidase N (AP-N) (cAPN) (EC 3.4.11.2) (Alanyl aminopeptidase) (Aminopeptidase M) (AP-M) (Microsomal aminopeptidase) (CD antigen CD13)

 AMPN_CANLF              Reviewed;         975 AA.
P79143; F1PCB5;
23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 2.
28-MAR-2018, entry version 104.
RecName: Full=Aminopeptidase N {ECO:0000305};
Short=AP-N;
Short=cAPN;
EC=3.4.11.2 {ECO:0000250|UniProtKB:P15144};
AltName: Full=Alanyl aminopeptidase;
AltName: Full=Aminopeptidase M;
Short=AP-M;
AltName: Full=Microsomal aminopeptidase;
AltName: CD_antigen=CD13;
Name=ANPEP;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer;
PubMed=16341006; DOI=10.1038/nature04338;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 657-847, FUNCTION (MICROBIAL INFECTION),
INTERACTION WITH CCOV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), AND
IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR CCOV INFECTION
(MICROBIAL INFECTION).
TISSUE=Small intestine;
PubMed=8985407;
Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
"Interspecies aminopeptidase-N chimeras reveal species-specific
receptor recognition by canine coronavirus, feline infectious
peritonitis virus, and transmissible gastroenteritis virus.";
J. Virol. 71:734-737(1997).
-!- 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:0000250|UniProtKB:P15144}.
-!- FUNCTION: (Microbial infection) Probable receptor for canine
coronavirus (CCoV). {ECO:0000269|PubMed:8985407}.
-!- 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:0000250|UniProtKB:P15144}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P15144};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144};
-!- SUBUNIT: (Microbial infection) Interacts with CCoV spike
glycoprotein. {ECO:0000269|PubMed:8985407}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15144}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P15144}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a
soluble form. {ECO:0000250|UniProtKB:P15144}.
-!- DOMAIN: Amino acids 1-191 are essential to mediate susceptibility
to infection with CCV (in canine/human chimeric studies).
{ECO:0000269|PubMed:8985407}.
-!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.
-!- PTM: May undergo proteolysis and give rise to a soluble form.
{ECO:0000250|UniProtKB:P15144}.
-!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AAEX03002325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X98239; CAA66895.1; -; mRNA.
RefSeq; NP_001139506.1; NM_001146034.1.
UniGene; Cfa.3774; -.
ProteinModelPortal; P79143; -.
SMR; P79143; -.
STRING; 9615.ENSCAFP00000017681; -.
MEROPS; M01.001; -.
PaxDb; P79143; -.
PRIDE; F1PCB5; -.
Ensembl; ENSCAFT00000019074; ENSCAFP00000017681; ENSCAFG00000012013.
GeneID; 403913; -.
KEGG; cfa:403913; -.
CTD; 290; -.
eggNOG; KOG1046; Eukaryota.
eggNOG; COG0308; LUCA.
GeneTree; ENSGT00760000119082; -.
HOGENOM; HOG000106482; -.
InParanoid; P79143; -.
KO; K11140; -.
OMA; NNPIHPN; -.
OrthoDB; EOG091G01GH; -.
TreeFam; TF300395; -.
Reactome; R-CFA-6798695; Neutrophil degranulation.
Proteomes; UP000002254; Chromosome 3.
Bgee; ENSCAFG00000012013; -.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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.
1: Evidence at protein level;
Aminopeptidase; Angiogenesis; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Protease; Receptor;
Reference proteome; Signal-anchor; Sulfation; Transmembrane;
Transmembrane helix; Zinc.
CHAIN 1 975 Aminopeptidase N.
/FTId=PRO_0000095079.
TOPO_DOM 1 11 Cytoplasmic.
{ECO:0000250|UniProtKB:P15144}.
TRANSMEM 12 32 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 33 975 Extracellular.
{ECO:0000250|UniProtKB:P15144}.
REGION 33 74 Cytosolic Ser/Thr-rich junction.
{ECO:0000250|UniProtKB:P15144}.
REGION 75 975 Metalloprotease.
REGION 358 362 Substrate binding.
{ECO:0000250|UniProtKB:P15144}.
ACT_SITE 395 395 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 394 394 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 398 398 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 417 417 Zinc; catalytic.
{ECO:0000250|UniProtKB:P15144}.
SITE 483 483 Transition state stabilizer.
{ECO:0000250|UniProtKB:P15144}.
MOD_RES 182 182 Sulfotyrosine. {ECO:0000255}.
MOD_RES 425 425 Sulfotyrosine. {ECO:0000255}.
MOD_RES 430 430 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 633 633 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 689 689 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 747 747 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 826 826 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P15144}.
DISULFID 769 776 {ECO:0000250|UniProtKB:P15144}.
DISULFID 806 842 {ECO:0000250|UniProtKB:P15144}.
SEQUENCE 975 AA; 110257 MW; 921D2446A2F84725 CRC64;
MAKGFYISKA LGILAIVLGI AAVSTIIALS VVYAQEKNKN AESSPVSSPV SSPVSSPVSP
TNPSTTAATT LAQSKPWNHY RLPKTLIPSS YNVTLRPYLT PNSNGLYTFK GSSTVRFTCK
ESTSMIIIHS KKLNYTNIQG QRVALRGVGG SQAPAIDRTE LVEVTEYLVV HLREPLQVNS
QYEMDSKFEG ELADDLAGFY RSEYTENGVK KVLATTQMQA ADARKSFPCF DEPAMKATFN
ITLIHPSNLV ALSNMLPRGP SVPFTEEPNW NVTEFETTPI MSTYLLAYIV SEFKNVQENT
PSNVLIRIWA RPSAMDQGHG NYALRVTGPI LDFFSRHYDT PYPLNKSDQI ALPDFNAGAM
ENWGLVTYRE SALLYDPQSS SIGNKERVVT VIAHELAHQW FGNLVTLEWW NDLWLNEGFA
SYVEYLGADY AEPTWNLKDL IVLNEVYRVM AVDALASSHP LSSPASEVNT PAQISEVFDS
ISYSKGASVL RMLSSFLTED LFKKGVASYL HTFAYQNTIY LDLWNHLQWA LGNQTAINLP
YTVNAIMDRW ILQMGFPVVT VDTTTGTLSQ KHFLLDPQSN VTRPSKFNYL WIIPISSVKS
GTQQAHYWMP DNAKVQNDLF KTTGDEWVLL NLNVTGYYLV NYDQNNWKKI HTQLQTDLSV
IPVINRAQVI HDTFDLASAQ IVPVTLALNS TLFLNQETEY MPWEAALSSL SYFKLMFDRS
EVYGPMKNYL RKQVTPLFNH FEKITQNWTD HPQTLTEQYN EINAVSTACT YGVPKCKDLV
STLFAEWRKN PQNNPIYPNL RSTVYCNAIA QGGEEEWNFV WEQFRNTSLV NEADKLRSAL
ACSTQVWILN RYLSYTLNPE FIRKQDVIST LSSIASNVIG QSLAWDFIQS NWKKLFEDYG
TGSFSFSNLI QAVTRRFSTE FELQQLEQFK ANNMDTGFGS GTRALEQALE KTKANIKWVK
ENKEAVLQWF RENSQ


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