Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q0J5V5

Entry ID Method Resolution Chain Position Source
AF-Q0J5V5-F1 Predicted AlphaFoldDB

No variants for Q0J5V5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0J5V5

No associated diseases with Q0J5V5

3 regional properties for Q0J5V5

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 233 - 449 IPR014782
domain ERAP1-like C-terminal domain 530 - 848 IPR024571
domain Aminopeptidase N-like, N-terminal domain 20 - 198 IPR045357

Functions

Description
EC Number 3.4.11.2 Aminopeptidases
Subcellular Localization
  • Membrane ; Peripheral membrane protein
  • Microsome membrane ; Peripheral membrane protein
  • Cytoplasm
  • The dileucine internalization motif may be involved in intracellular sequestration
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.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

3 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.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
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.

23 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
P79171 ANPEP Aminopeptidase N Felis catus (Cat) (Felis silvestris catus) PR
P15144 ANPEP Aminopeptidase N Homo sapiens (Human) PR
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme Homo sapiens (Human) PR
Q9UIQ6 LNPEP Leucyl-cystinyl aminopeptidase Homo sapiens (Human) PR
Q9NZ08 ERAP1 Endoplasmic reticulum aminopeptidase 1 Homo sapiens (Human) PR
P55786 NPEPPS Puromycin-sensitive aminopeptidase Homo sapiens (Human) PR
A6NEC2 NPEPPSL1 Puromycin-sensitive aminopeptidase-like protein Homo sapiens (Human) PR
P97449 Anpep Aminopeptidase N Mus musculus (Mouse) 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
P15145 ANPEP Aminopeptidase N Sus scrofa (Pig) PR
P15684 Anpep Aminopeptidase N Rattus norvegicus (Rat) PR
P97629 Lnpep Leucyl-cystinyl aminopeptidase Rattus norvegicus (Rat) PR
Q9JJ22 Erap1 Endoplasmic reticulum aminopeptidase 1 Rattus norvegicus (Rat) PR
Q10836 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Rattus norvegicus (Rat) 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
MAASPEQFRG QARLPRCASP LSYDLRLRPD LAACAFSGSA AVAVAVSAPT RFLVLNAAEL
70 80 90 100 110 120
AVDGSSVRFQ DLVPSEVVQF EEDEIVVIGF GQDLPIGEGV LKMDFTGTLN DQMRGFYRSK
130 140 150 160 170 180
YEYKGESRNM AVTQFEAADA RRCFPCWDEP AFKAKFKLTL EVPSELVALS NMPVIKETVH
190 200 210 220 230 240
GPLKTVYYEE SPLMSTYLVA IVVGLFDYIE GSTLEGTKVR VYTQVGKSNQ GKFALDVAVK
250 260 270 280 290 300
SLDLFKDYFA TPYPLPKLDM VAIPDFAAGA MENYGLVTYR ETALLYDELL SSASNKQQVA
310 320 330 340 350 360
ITVAHELAHQ WFGNLVTMEW WTHLWLNEGF ASWVSYLAVE ALFPEWNNWT QFLDETTSGL
370 380 390 400 410 420
RLDALAESHP IEVDINHASE IDAIFDSISY DKGASVIRML QSYLGAERFQ KALASYIKKY
430 440 450 460 470 480
AYSNAKTEDL WAVLEEESGE PVKDLMTTWT KQQGYPVIYA KLDGHDLHLE QAQFLSDGSS
490 500 510 520 530 540
GPGLWIVPIT SCCGSYDAQK KFLLKGKTDK VHIDLTASQN AGGEKGENCW IKLNVDQTGF
550 560 570 580 590 600
YRVKYDDELA AGLEKAIKAN KLSLMDKIGI VEDSYSLSVA RKQTLTSLLR LLNAYRNESD
610 620 630 640 650 660
YTVLSHVTSV CLGIDKISVD ATPELSRDIK QLLINLLLSA AKTLGWDPKE GESHLDVMLR
670 680 690 700 710 720
SLLLIALVKL GHDETINEGV RRFHIFIKDR KTNILPPDTR KASYLAVMRT VTTSSRAGYD
730 740 750 760 770 780
ALLKIYRETA EAQEKSRILG SLSSCLDKDI VLEALNFMLT DEVRNQDAFY VLGGISLEGR
790 800 810 820 830 840
EVAWAWLKEN WDHVLKTWPS SSLISDFVKS TVSRFTTEEK AAEVSEFFAG KTKPSFERAL
850 860 870
KQSLERVRIS ARWIESIRSE PNLAQTVNEL LQHDM