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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity
(Microbial infection) Probable receptor for canine coronavirus (CCoV).1 Publication

Catalytic activityi

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.By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi394Zinc; catalyticPROSITE-ProRule annotation1
Active sitei395Proton acceptorPROSITE-ProRule annotation1
Metal bindingi398Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi417Zinc; catalyticBy similarity1
Sitei483Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminopeptidase, Developmental protein, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor
Biological processAngiogenesis, Differentiation, Host-virus interaction
LigandMetal-binding, Zinc

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase NCurated (EC:3.4.11.2By similarity)
Short name:
AP-N
Short name:
cAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Microsomal aminopeptidase
CD_antigen: CD13
Gene namesi
Name:ANPEP
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componentsi: Chromosome 3, Unplaced

Subcellular locationi

  • Cell membrane By similarity; Single-pass type II membrane protein By similarity

  • Note: Also found as a soluble form.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 11CytoplasmicBy similarity10
Transmembranei12 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini33 – 975ExtracellularBy similarityAdd BLAST943

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000950792 – 975Aminopeptidase NAdd BLAST974

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi134N-linked (GlcNAc...)By similarity1
Modified residuei182SulfotyrosineSequence analysis1
Glycosylationi240N-linked (GlcNAc...)By similarity1
Glycosylationi271N-linked (GlcNAc...)By similarity1
Modified residuei425SulfotyrosineSequence analysis1
Modified residuei430SulfotyrosineSequence analysis1
Glycosylationi533N-linked (GlcNAc...)By similarity1
Glycosylationi580N-linked (GlcNAc...)By similarity1
Glycosylationi633N-linked (GlcNAc...)By similarity1
Glycosylationi689N-linked (GlcNAc...)By similarity1
Glycosylationi747N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi769 ↔ 776By similarity
Disulfide bondi806 ↔ 842By similarity
Glycosylationi826N-linked (GlcNAc...)By similarity1

Post-translational modificationi

Sulfated.By similarity
N- and O-glycosylated.By similarity
May undergo proteolysis and give rise to a soluble form.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiF1PCB5.
P79143.
PRIDEiF1PCB5.

Interactioni

Subunit structurei

(Microbial infection) Interacts with CCoV spike glycoprotein.1 Publication
Homodimer.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000017681.

Structurei

3D structure databases

ProteinModelPortaliP79143.
SMRiP79143.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 74Cytosolic Ser/Thr-rich junctionBy similarityAdd BLAST42
Regioni75 – 975MetalloproteaseAdd BLAST901
Regioni358 – 362Substrate bindingBy similarity5

Domaini

Amino acids 1-191 are essential to mediate susceptibility to infection with CCV (in canine/human chimeric studies).1 Publication

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
InParanoidiP79143.
OMAiQISEMFD.
TreeFamiTF300395.

Family and domain databases

InterProiView protein in InterPro
IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiView protein in Pfam
PF11838. ERAP1_C. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P79143-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGFYISKA LGILAIVLGI AAVSTIIALS VVYAQEKNKN AESSPVSSPV
60 70 80 90 100
SSPVSSPVSP TNPSTTAATT LAQSKPWNHY RLPKTLIPSS YNVTLRPYLT
110 120 130 140 150
PNSNGLYTFK GSSTVRFTCK ESTSMIIIHS KKLNYTNIQG QRVALRGVGG
160 170 180 190 200
SQAPAIDRTE LVEVTEYLVV HLREPLQVNS QYEMDSKFEG ELADDLAGFY
210 220 230 240 250
RSEYTENGVK KVLATTQMQA ADARKSFPCF DEPAMKATFN ITLIHPSNLV
260 270 280 290 300
ALSNMLPRGP SVPFTEEPNW NVTEFETTPI MSTYLLAYIV SEFKNVQENT
310 320 330 340 350
PSNVLIRIWA RPSAMDQGHG NYALRVTGPI LDFFSRHYDT PYPLNKSDQI
360 370 380 390 400
ALPDFNAGAM ENWGLVTYRE SALLYDPQSS SIGNKERVVT VIAHELAHQW
410 420 430 440 450
FGNLVTLEWW NDLWLNEGFA SYVEYLGADY AEPTWNLKDL IVLNEVYRVM
460 470 480 490 500
AVDALASSHP LSSPASEVNT PAQISEVFDS ISYSKGASVL RMLSSFLTED
510 520 530 540 550
LFKKGVASYL HTFAYQNTIY LDLWNHLQWA LGNQTAINLP YTVNAIMDRW
560 570 580 590 600
ILQMGFPVVT VDTTTGTLSQ KHFLLDPQSN VTRPSKFNYL WIIPISSVKS
610 620 630 640 650
GTQQAHYWMP DNAKVQNDLF KTTGDEWVLL NLNVTGYYLV NYDQNNWKKI
660 670 680 690 700
HTQLQTDLSV IPVINRAQVI HDTFDLASAQ IVPVTLALNS TLFLNQETEY
710 720 730 740 750
MPWEAALSSL SYFKLMFDRS EVYGPMKNYL RKQVTPLFNH FEKITQNWTD
760 770 780 790 800
HPQTLTEQYN EINAVSTACT YGVPKCKDLV STLFAEWRKN PQNNPIYPNL
810 820 830 840 850
RSTVYCNAIA QGGEEEWNFV WEQFRNTSLV NEADKLRSAL ACSTQVWILN
860 870 880 890 900
RYLSYTLNPE FIRKQDVIST LSSIASNVIG QSLAWDFIQS NWKKLFEDYG
910 920 930 940 950
TGSFSFSNLI QAVTRRFSTE FELQQLEQFK ANNMDTGFGS GTRALEQALE
960 970
KTKANIKWVK ENKEAVLQWF RENSQ
Length:975
Mass (Da):110,257
Last modified:March 15, 2017 - v2
Checksum:i921D2446A2F84725
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03002325 Genomic DNA. No translation available.
X98239 mRNA. Translation: CAA66895.1.
UniGeneiCfa.3774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03002325 Genomic DNA. No translation available.
X98239 mRNA. Translation: CAA66895.1.
UniGeneiCfa.3774.

3D structure databases

ProteinModelPortaliP79143.
SMRiP79143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000017681.

Protein family/group databases

MEROPSiM01.001.

Proteomic databases

PaxDbiF1PCB5.
P79143.
PRIDEiF1PCB5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
InParanoidiP79143.
OMAiQISEMFD.
TreeFamiTF300395.

Family and domain databases

InterProiView protein in InterPro
IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiView protein in Pfam
PF11838. ERAP1_C. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMPN_CANLF
AccessioniPrimary (citable) accession number: P79143
Secondary accession number(s): F1PCB5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: March 15, 2017
Last modified: March 15, 2017
This is version 96 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.