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 Q9JJ22

Entry ID Method Resolution Chain Position Source
AF-Q9JJ22-F1 Predicted AlphaFoldDB

No variants for Q9JJ22

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9JJ22

No associated diseases with Q9JJ22

3 regional properties for Q9JJ22

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 270 - 513 IPR014782
domain ERAP1-like C-terminal domain 586 - 905 IPR024571
domain Aminopeptidase N-like, N-terminal domain 49 - 235 IPR045357

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass type II membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 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 lumen The volume enclosed by the membranes of the endoplasmic reticulum.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
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.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma 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.

9 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
interleukin-6 receptor binding Binding to an interleukin-6 receptor.
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.
metalloexopeptidase activity Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of 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.
peptidase activity Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
peptide binding Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds.
tumor necrosis factor receptor binding Binding to a tumor necrosis factor receptor.
zinc ion binding Binding to a zinc ion (Zn).

10 GO annotations of biological process

Name Definition
adaptive immune response An immune response mediated by cells expressing specific receptors for antigen produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory).
antigen processing and presentation The process in which an antigen-presenting cell expresses antigen (peptide or lipid) on its cell surface in association with an MHC protein complex.
antigen processing and presentation of endogenous peptide antigen via MHC class I The process in which an antigen-presenting cell expresses a peptide antigen of endogenous origin on its cell surface in association with an MHC class I protein complex. The peptide antigen is typically, but not always, processed from a whole protein. Class I here refers to classical class I molecules.
membrane protein ectodomain proteolysis The proteolytic cleavage of transmembrane proteins and release of their ectodomain (extracellular domain).
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.
positive regulation of angiogenesis Any process that activates or increases angiogenesis.
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
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
P79171 ANPEP Aminopeptidase N Felis catus (Cat) (Felis silvestris catus) PR
Q9UIQ6 LNPEP Leucyl-cystinyl aminopeptidase Homo sapiens (Human) PR
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme Homo sapiens (Human) PR
P15144 ANPEP Aminopeptidase N Homo sapiens (Human) PR
P55786 NPEPPS Puromycin-sensitive aminopeptidase Homo sapiens (Human) PR
Q9NZ08 ERAP1 Endoplasmic reticulum aminopeptidase 1 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
P97449 Anpep Aminopeptidase N Mus musculus (Mouse) PR
Q9EQH2 Erap1 Endoplasmic reticulum aminopeptidase 1 Mus musculus (Mouse) PR
P15145 ANPEP Aminopeptidase N Sus scrofa (Pig) PR
P97629 Lnpep Leucyl-cystinyl aminopeptidase Rattus norvegicus (Rat) PR
P15684 Anpep Aminopeptidase N Rattus norvegicus (Rat) PR
Q10836 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme 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
MPSLLSLVLT FLAVSSPSCC QNSDTASPKA SNGASFPWNN MRLPEYITPI HYDLMIHANL
70 80 90 100 110 120
STLTFWGKTE VEITVSQPTS TIIMHSHQLQ ISKATLRRGA EEMLPEEPLK LMEYSAHEQV
130 140 150 160 170 180
ALLTAQPLLA GSVYTVIITY AANLSENFHG FYKSTYRTQE GERRILAATQ FEPTAARMAF
190 200 210 220 230 240
PCFDEPALKA SFSIKIKRDP RHLAISNMPL VKSVTVAEGL IEDHFDITVK MSTYLVAFII
250 260 270 280 290 300
SDFKSVSKMT KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFSIPY PLPKQDLAAI
310 320 330 340 350 360
PDFQSGAMEN WGLTTYRESA LLYDKEKSSA SSKLGITMTV SHELAHQWFG NLVTMEWWND
370 380 390 400 410 420
LWLNEGFAKF MEFVSVTVTH PELKVEEYFF GKCFNAMEVD ALNSSHPVST PVENPAQIRE
430 440 450 460 470 480
MFDEVSYEKG ACILNMLRDY LSADTFKRGI VQYLQKYSYK NTKNEDLWNS MMHICPTDGT
490 500 510 520 530 540
QTMDGFCSRN QHSSSTSHWR QEVIDIKSMM NTWTLQKGFP LITITVRGRN VHLKQEHYMK
550 560 570 580 590 600
GSECFPETGS LWHVPLTFIT SKSDSVQRFL LKTKTDVIIL PEAVEWIKFN VGMNGYYIVH
610 620 630 640 650 660
YGDDGWASLN GLLKEAHTTI SSNDRASLIN NAFQLVSIGK LSIEKALDLI LYLKNETEIM
670 680 690 700 710 720
PIFQGLNELI PMYKLMEKRD MVEVETQFKD FLLRLLKDLI NKQTWTDEGS VSERMLRSQL
730 740 750 760 770 780
LLLACVHRYQ LCVQRAERYF REWKASNGNM SLPIDVTLAV FAVGAQNTEG WDFLYSKYQS
790 800 810 820 830 840
SLSSTEKSQI EFSLCISQDP EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK
850 860 870 880 890 900
FLKENWNKIV QKFELGSSSI AHMVMGTTNQ FSTRARLEEV KGFFSSLKKN GSQLRCVQQT
910 920
IETIEENIRW MDKNFDKIRL WLQKERQELL