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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.By similarity

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.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi383Zinc; catalytic1
Active sitei384Proton acceptorPROSITE-ProRule annotation1
Metal bindingi387Zinc; catalytic1
Metal bindingi406Zinc; catalytic1
Sitei472Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Developmental protein, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation, Host-virus interaction

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Short name:
pAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Microsomal aminopeptidase
gp130
CD_antigen: CD13
Gene namesi
Name:ANPEP
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 8Cytoplasmic7
Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 963ExtracellularAdd BLAST931

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2590.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000950832 – 963Aminopeptidase NAdd BLAST962

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi82N-linked (GlcNAc...)1 Publication1
Glycosylationi124N-linked (GlcNAc...)1 Publication1
Modified residuei171SulfotyrosineSequence analysis1
Glycosylationi229N-linked (GlcNAc...)1 Publication1
Glycosylationi237N-linked (GlcNAc...)1 Publication1
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Glycosylationi286N-linked (GlcNAc...)Sequence analysis1
Glycosylationi314N-linked (GlcNAc...)1 Publication1
Glycosylationi328N-linked (GlcNAc...)1 Publication1
Glycosylationi506N-linked (GlcNAc...)1 Publication1
Glycosylationi556N-linked (GlcNAc...)Sequence analysis1
Glycosylationi569N-linked (GlcNAc...)Sequence analysis1
Glycosylationi622N-linked (GlcNAc...)1 Publication1
Glycosylationi646N-linked (GlcNAc...)1 Publication1
Glycosylationi736N-linked (GlcNAc...)1 Publication1
Disulfide bondi758 ↔ 7651 Publication
Disulfide bondi795 ↔ 8311 Publication

Post-translational modificationi

Sulfated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiP15145.
PeptideAtlasiP15145.
PRIDEiP15145.

Miscellaneous databases

PMAP-CutDBP15145.

Interactioni

Subunit structurei

Homodimer. Interacts with TGEV and PRCoV spike glycoprotein.2 Publications

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000029051.

Chemistry databases

BindingDBiP15145.

Structurei

Secondary structure

1963
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi66 – 68Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi74 – 87Combined sources14
Beta strandi93 – 95Combined sources3
Beta strandi98 – 111Combined sources14
Beta strandi113 – 119Combined sources7
Beta strandi122 – 125Combined sources4
Beta strandi128 – 131Combined sources4
Beta strandi133 – 137Combined sources5
Beta strandi145 – 151Combined sources7
Turni152 – 155Combined sources4
Beta strandi156 – 165Combined sources10
Beta strandi170 – 180Combined sources11
Beta strandi183 – 195Combined sources13
Beta strandi198 – 206Combined sources9
Turni208 – 211Combined sources4
Helixi212 – 214Combined sources3
Beta strandi221 – 224Combined sources4
Beta strandi226 – 235Combined sources10
Beta strandi238 – 244Combined sources7
Beta strandi246 – 249Combined sources4
Beta strandi254 – 256Combined sources3
Beta strandi259 – 264Combined sources6
Helixi272 – 274Combined sources3
Beta strandi277 – 281Combined sources5
Beta strandi283 – 288Combined sources6
Beta strandi294 – 299Combined sources6
Helixi301 – 305Combined sources5
Turni306 – 309Combined sources4
Helixi310 – 326Combined sources17
Beta strandi332 – 341Combined sources10
Beta strandi345 – 349Combined sources5
Beta strandi354 – 358Combined sources5
Helixi359 – 362Combined sources4
Turni366 – 368Combined sources3
Helixi371 – 386Combined sources16
Turni387 – 389Combined sources3
Turni391 – 393Combined sources3
Beta strandi394 – 398Combined sources5
Helixi399 – 401Combined sources3
Helixi402 – 420Combined sources19
Helixi426 – 429Combined sources4
Helixi430 – 433Combined sources4
Helixi435 – 442Combined sources8
Helixi454 – 456Combined sources3
Helixi460 – 464Combined sources5
Helixi469 – 486Combined sources18
Helixi488 – 502Combined sources15
Beta strandi505 – 507Combined sources3
Helixi509 – 521Combined sources13
Beta strandi524 – 526Combined sources3
Helixi532 – 540Combined sources9
Beta strandi546 – 550Combined sources5
Turni552 – 554Combined sources3
Beta strandi556 – 561Combined sources6
Beta strandi564 – 567Combined sources4
Turni575 – 578Combined sources4
Beta strandi582 – 584Combined sources3
Beta strandi586 – 588Combined sources3
Beta strandi596 – 598Combined sources3
Beta strandi602 – 605Combined sources4
Helixi607 – 609Combined sources3
Beta strandi617 – 620Combined sources4
Helixi621 – 623Combined sources3
Beta strandi628 – 631Combined sources4
Helixi633 – 645Combined sources13
Helixi647 – 649Combined sources3
Helixi652 – 667Combined sources16
Helixi673 – 678Combined sources6
Helixi679 – 685Combined sources7
Helixi689 – 706Combined sources18
Helixi712 – 733Combined sources22
Turni734 – 738Combined sources5
Helixi744 – 759Combined sources16
Helixi763 – 777Combined sources15
Turni787 – 789Combined sources3
Helixi790 – 800Combined sources11
Helixi803 – 815Combined sources13
Helixi819 – 829Combined sources11
Helixi835 – 844Combined sources10
Turni848 – 850Combined sources3
Helixi853 – 855Combined sources3
Helixi856 – 865Combined sources10
Helixi869 – 880Combined sources12
Turni882 – 886Combined sources5
Beta strandi887 – 890Combined sources4
Helixi895 – 903Combined sources9
Helixi909 – 919Combined sources11
Helixi920 – 922Combined sources3
Beta strandi923 – 925Combined sources3
Helixi928 – 930Combined sources3
Helixi933 – 962Combined sources30

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F5CX-ray3.20A/B36-963[»]
4FKEX-ray1.85A62-963[»]
4FKHX-ray2.05A62-963[»]
4FKKX-ray2.60A62-963[»]
4HOMX-ray1.90A63-963[»]
4NAQX-ray2.10A64-963[»]
4NZ8X-ray2.00A64-963[»]
4OU3X-ray1.95A63-963[»]
SMRiP15145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 64Cytosolic Ser/Thr-rich junctionAdd BLAST32
Regioni65 – 963MetalloproteaseAdd BLAST899
Regioni347 – 351Substrate bindingBy similarity5
Regioni717 – 813Interaction with TGEV spike glycoproteinAdd BLAST97

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP15145.
KOiK11140.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGFYISKA LGILGILLGV AAVATIIALS VVYAQEKNKN AEHVPQAPTS
60 70 80 90 100
PTITTTAAIT LDQSKPWNRY RLPTTLLPDS YNVTLRPYLT PNADGLYIFK
110 120 130 140 150
GKSIVRLLCQ EPTDVIIIHS KKLNYTTQGH MVVLRGVGDS QVPEIDRTEL
160 170 180 190 200
VELTEYLVVH LKGSLQPGHM YEMESEFQGE LADDLAGFYR SEYMEGNVKK
210 220 230 240 250
VLATTQMQST DARKSFPCFD EPAMKATFNI TLIHPNNLTA LSNMPPKGSS
260 270 280 290 300
TPLAEDPNWS VTEFETTPVM STYLLAYIVS EFQSVNETAQ NGVLIRIWAR
310 320 330 340 350
PNAIAEGHGM YALNVTGPIL NFFANHYNTS YPLPKSDQIA LPDFNAGAME
360 370 380 390 400
NWGLVTYREN ALLFDPQSSS ISNKERVVTV IAHELAHQWF GNLVTLAWWN
410 420 430 440 450
DLWLNEGFAS YVEYLGADHA EPTWNLKDLI VPGDVYRVMA VDALASSHPL
460 470 480 490 500
TTPAEEVNTP AQISEMFDSI SYSKGASVIR MLSNFLTEDL FKEGLASYLH
510 520 530 540 550
AFAYQNTTYL DLWEHLQKAV DAQTSIRLPD TVRAIMDRWT LQMGFPVITV
560 570 580 590 600
DTKTGNISQK HFLLDSESNV TRSSAFDYLW IVPISSIKNG VMQDHYWLRD
610 620 630 640 650
VSQAQNDLFK TASDDWVLLN VNVTGYFQVN YDEDNWRMIQ HQLQTNLSVI
660 670 680 690 700
PVINRAQVIY DSFNLATAHM VPVTLALDNT LFLNGEKEYM PWQAALSSLS
710 720 730 740 750
YFSLMFDRSE VYGPMKKYLR KQVEPLFQHF ETLTKNWTER PENLMDQYSE
760 770 780 790 800
INAISTACSN GLPQCENLAK TLFDQWMSDP ENNPIHPNLR STIYCNAIAQ
810 820 830 840 850
GGQDQWDFAW GQLQQAQLVN EADKLRSALA CSNEVWLLNR YLGYTLNPDL
860 870 880 890 900
IRKQDATSTI NSIASNVIGQ PLAWDFVQSN WKKLFQDYGG GSFSFSNLIQ
910 920 930 940 950
GVTRRFSSEF ELQQLEQFKK NNMDVGFGSG TRALEQALEK TKANIKWVKE
960
NKEVVLNWFI EHS
Length:963
Mass (Da):108,832
Last modified:February 6, 2013 - v4
Checksum:i0C55FDD2CE1F3E10
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82N → F in CAA82641 (PubMed:7913510).Curated1
Sequence conflicti82N → F in CAA34216 (PubMed:2568950).Curated1
Sequence conflicti107 – 108LL → FI in CAA23291 (PubMed:8672129).Curated2
Sequence conflicti111E → G in CAA23291 (PubMed:8672129).Curated1
Sequence conflicti126T → N in CAA23291 (PubMed:8672129).Curated1
Sequence conflicti140S → F in CAA23291 (PubMed:8672129).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29522 mRNA. Translation: CAA82641.1.
X16088 Genomic DNA. Translation: CAA34216.1. Different termination.
F14846 mRNA. Translation: CAA23291.1.
PIRiA53984.
RefSeqiNP_999442.1. NM_214277.1.
UniGeneiSsc.820.

Genome annotation databases

GeneIDi397520.
KEGGissc:397520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29522 mRNA. Translation: CAA82641.1.
X16088 Genomic DNA. Translation: CAA34216.1. Different termination.
F14846 mRNA. Translation: CAA23291.1.
PIRiA53984.
RefSeqiNP_999442.1. NM_214277.1.
UniGeneiSsc.820.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F5CX-ray3.20A/B36-963[»]
4FKEX-ray1.85A62-963[»]
4FKHX-ray2.05A62-963[»]
4FKKX-ray2.60A62-963[»]
4HOMX-ray1.90A63-963[»]
4NAQX-ray2.10A64-963[»]
4NZ8X-ray2.00A64-963[»]
4OU3X-ray1.95A63-963[»]
SMRiP15145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000029051.

Chemistry databases

BindingDBiP15145.
ChEMBLiCHEMBL2590.

Protein family/group databases

MEROPSiM01.001.

Proteomic databases

PaxDbiP15145.
PeptideAtlasiP15145.
PRIDEiP15145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397520.
KEGGissc:397520.

Organism-specific databases

CTDi290.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP15145.
KOiK11140.

Miscellaneous databases

PMAP-CutDBP15145.
PROiP15145.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMPN_PIG
AccessioniPrimary (citable) accession number: P15145
Secondary accession number(s): Q29242
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 6, 2013
Last modified: November 2, 2016
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.