P79171

PR
Gene name
ANPEP (APN)
Protein name
Aminopeptidase N
Names
Species
Felis catus (Cat) (Felis silvestris catus)
KEGG Pathway
fca:493785
EC number
3.4.11.2: Aminopeptidases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

3-90 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P79171

Entry ID Method Resolution Chain Position Source
AF-P79171-F1 Predicted AlphaFoldDB

No variants for P79171

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P79171

No associated diseases with P79171

3 regional properties for P79171

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 315 - 543 IPR014782
domain ERAP1-like C-terminal domain 620 - 946 IPR024571
domain Aminopeptidase N-like, N-terminal domain 80 - 278 IPR045357

Functions

Description
EC Number 3.4.11.2 Aminopeptidases
Subcellular Localization
  • Cell membrane ; Single-pass type II membrane protein
  • Also found as a soluble form
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

4 GO annotations of molecular function

Name Definition
metalloaminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
peptide binding Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds.
virus receptor activity Combining with a virus component and mediating entry of the virus into the cell.
zinc ion binding Binding to a zinc ion (Zn).

6 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
cell differentiation The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state.
peptide catabolic process The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
regulation of blood pressure Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

22 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P40462 TMA108 Protein TMA108 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P32454 APE2 Aminopeptidase 2, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9UIQ6 LNPEP Leucyl-cystinyl aminopeptidase Homo sapiens (Human) PR
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme Homo sapiens (Human) PR
Q9NZ08 ERAP1 Endoplasmic reticulum aminopeptidase 1 Homo sapiens (Human) PR
P55786 NPEPPS Puromycin-sensitive aminopeptidase Homo sapiens (Human) PR
P15144 ANPEP Aminopeptidase N Homo sapiens (Human) PR
Q11011 Npepps Puromycin-sensitive aminopeptidase Mus musculus (Mouse) PR
Q8C129 Lnpep Leucyl-cystinyl aminopeptidase Mus musculus (Mouse) PR
Q8K093 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Mus musculus (Mouse) PR
Q9EQH2 Erap1 Endoplasmic reticulum aminopeptidase 1 Mus musculus (Mouse) PR
P97449 Anpep Aminopeptidase N Mus musculus (Mouse) PR
P15145 ANPEP Aminopeptidase N Sus scrofa (Pig) PR
Q10836 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Rattus norvegicus (Rat) PR
Q9JJ22 Erap1 Endoplasmic reticulum aminopeptidase 1 Rattus norvegicus (Rat) PR
P97629 Lnpep Leucyl-cystinyl aminopeptidase Rattus norvegicus (Rat) PR
P15684 Anpep Aminopeptidase N Rattus norvegicus (Rat) PR
Q0J5V5 Os08g0398700 Aminopeptidase M1-B Oryza sativa subsp japonica (Rice) PR
Q6Z6L4 Os02g0218200 Aminopeptidase M1-A Oryza sativa subsp japonica (Rice) PR
Q6K4E7 Os09g0362800 Aminopeptidase M1-D Oryza sativa subsp japonica (Rice) PR
Q17405 AC3.5 Aminopeptidase-like protein AC3.5 Caenorhabditis elegans PR
Q8VZH2 APM1 Aminopeptidase M1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAKGFYISKP VGILAILLGV AAVCTIIALS VVYSQEKNRS TESSTAASTA APTGPTTTVA
70 80 90 100 110 120
TTLDQSKPWN VYRLPKTLIP DSYNVTLRPY LTPNNKGLYV FTGTNIVRFT CKESTNIVII
130 140 150 160 170 180
HSKRLNYTSH QGHMVALSGV GGFHPQPVIV RTELVELTEY LVVHLQEPLV AGRQYEMNSE
190 200 210 220 230 240
FQGELADDLA GFYRSEYMEN GVKKVLATTH MQATEARKSF PCFDEPAMKA TFNITIIHPN
250 260 270 280 290 300
NLVALSNMLP RGPSVPFGED PTWKVTEFET TPIMSTYLLA YIVSEFSYVE TRAPSGVLIR
310 320 330 340 350 360
IWARPSAINQ GHGDYALKVT GPILDFFSQH YDTPYPLNKS DQIALPDFNA GAMENWGLVT
370 380 390 400 410 420
YRESALLYDR QSSSSGNQER VVTVIAHELA HQWFGNLVTL EWWNDLWLNE GFASYVEYLG
430 440 450 460 470 480
ADFAEPTWNL KDLMVLNDVY RVMAVDALAS SHPLSTPASE INTPAQISEV FDSISYSKGA
490 500 510 520 530 540
SVLRMLSNFL TEDLFKMGIA SYLHTYKYGN TIYLNLWEHL QQVVDKQPTI KLPDTVSAIM
550 560 570 580 590 600
DRWILQMGFP VITVDTQTGT ISQQHFLLDP QSVVTRPSQF NYLWIVPISS VRSGSPQAHY
610 620 630 640 650 660
WLPGVEKAQN DLFKTTANDW VLLNLNVTGY YLVNYDNENW KKIQTQLQTD LSVIPVINRA
670 680 690 700 710 720
QVIHDAFNLA SAQKVPVTLA LNNTLFLIQE TEYMPWQAAL SSLSYFKLMF DRSEVYGPMK
730 740 750 760 770 780
RYLKKQVTPL FNHFERVTKN WTDHPQTLMD QYSEINAVST ACSYGVPECE KLAATLFAQW
790 800 810 820 830 840
KKNPQNNPIH PNLRSTVYCN AIAQGGEEEW NFVWEQFLKA ELVNEADKLR GALACSNQVW
850 860 870 880 890 900
ILNRFLSYTL DPNLIRKQDV TSTLSSISSN VVGQTLVWDF VQSNWKKLFQ DYGTGSFSFS
910 920 930 940 950 960
NLIQAVTRRF STEFELQQLE QFKKNNMDTG FGSATRALEQ ALEKTKANLK WVKENKDVVL
RWFTENS