AMPN_CANLF
ID AMPN_CANLF Reviewed; 975 AA.
AC P79143; F1PCB5;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Aminopeptidase N {ECO:0000305};
DE Short=AP-N;
DE Short=cAPN;
DE EC=3.4.11.2 {ECO:0000250|UniProtKB:P15144};
DE AltName: Full=Alanyl aminopeptidase;
DE AltName: Full=Aminopeptidase M;
DE Short=AP-M;
DE AltName: Full=Microsomal aminopeptidase;
DE AltName: CD_antigen=CD13;
GN Name=ANPEP;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 657-847, FUNCTION (MICROBIAL INFECTION),
RP INTERACTION WITH CCOV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), AND
RP IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR CCOV INFECTION (MICROBIAL
RP INFECTION).
RC TISSUE=Small intestine;
RX PubMed=8985407; DOI=10.1128/jvi.71.1.734-737.1997;
RA Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B.;
RT "Interspecies aminopeptidase-N chimeras reveal species-specific receptor
RT recognition by canine coronavirus, feline infectious peritonitis virus, and
RT transmissible gastroenteritis virus.";
RL J. Virol. 71:734-737(1997).
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:P15144, ECO:0000250|UniProtKB:P97449}.
CC -!- FUNCTION: (Microbial infection) Probable receptor for canine
CC coronavirus (CCoV). {ECO:0000269|PubMed:8985407}.
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:0000250|UniProtKB:P15144};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15144};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144};
CC -!- SUBUNIT: (Microbial infection) Interacts with CCoV spike glycoprotein.
CC {ECO:0000269|PubMed:8985407}.
CC -!- SUBUNIT: Homodimer. Interacts with SLC6A19 (By similarity).
CC {ECO:0000250|UniProtKB:P15144, ECO:0000250|UniProtKB:P97449}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15144};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}.
CC Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}.
CC -!- DOMAIN: Amino acids 1-191 are essential to mediate susceptibility to
CC infection with CCV (in canine/human chimeric studies).
CC {ECO:0000269|PubMed:8985407}.
CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.
CC -!- PTM: May undergo proteolysis and give rise to a soluble form.
CC {ECO:0000250|UniProtKB:P15144}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AAEX03002325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X98239; CAA66895.1; -; mRNA.
DR RefSeq; NP_001139506.1; NM_001146034.1.
DR AlphaFoldDB; P79143; -.
DR SMR; P79143; -.
DR STRING; 9612.ENSCAFP00000017681; -.
DR MEROPS; M01.001; -.
DR PaxDb; P79143; -.
DR GeneID; 403913; -.
DR KEGG; cfa:403913; -.
DR CTD; 290; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; P79143; -.
DR OMA; KWFIFNI; -.
DR OrthoDB; 110058at2759; -.
DR TreeFam; TF300395; -.
DR Proteomes; UP000002254; Chromosome 3.
DR Bgee; ENSCAFG00000012013; Expressed in jejunum and 46 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
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.
PE 1: Evidence at protein level;
KW Aminopeptidase; Angiogenesis; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Protease; Receptor;
KW Reference proteome; Signal-anchor; Sulfation; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..975
FT /note="Aminopeptidase N"
FT /id="PRO_0000095079"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..975
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT REGION 33..74
FT /note="Cytosolic Ser/Thr-rich junction"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..975
FT /note="Metalloprotease"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 358..362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT SITE 483
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT MOD_RES 182
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 425
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 430
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT DISULFID 769..776
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT DISULFID 806..842
FT /evidence="ECO:0000250|UniProtKB:P15144"
SQ 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
