Q8C129

PR
Gene name
Lnpep
Protein name
Leucyl-cystinyl aminopeptidase
Names
Cystinyl aminopeptidase, Oxytocinase, OTase
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:240028
EC number
3.4.11.3: Aminopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-185 (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 Q8C129

Entry ID Method Resolution Chain Position Source
AF-Q8C129-F1 Predicted AlphaFoldDB

42 variants for Q8C129

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389429340 49 R>Q No EVA
rs225276307 68 E>D No EVA
rs33762345 105 L>V No EVA
rs3389384053 107 S>F No EVA
rs3389414868 108 A>D No EVA
rs3389446613 137 T>I No EVA
rs3389414915 166 I>L No EVA
rs250480487 180 S>N No EVA
rs3389383999 186 T>A No EVA
rs3389429048 190 F>L No EVA
rs3389433020 213 G>E No EVA
rs3407357330 298 A>P No EVA
rs3389394881 321 R>K No EVA
rs3389394871 352 V>M No EVA
rs1134284661 367 R>K No EVA
rs1131891190 376 T>I No EVA
rs3389426544 419 L>W No EVA
rs3389429274 430 M>V No EVA
rs3389446632 570 H>L No EVA
rs3389384029 573 I>S No EVA
rs3412732710 573 I>T No EVA
rs3389433470 588 D>E No EVA
rs3389433449 634 R>T No EVA
rs3389348454 645 P>H No EVA
rs229215825 659 V>I No EVA
rs3389384039 660 T>N No EVA
rs33761082 664 N>S No EVA
rs33756219 692 V>I No EVA
rs238784386 707 D>E No EVA
rs249064772 763 A>T No EVA
rs33757446 775 I>M No EVA
rs3389446660 786 D>N No EVA
rs246165846 833 E>A No EVA
rs3389426538 859 V>I No EVA
rs3389433451 867 G>S No EVA
rs253152637 875 L>S No EVA
rs3389452483 888 A>P No EVA
rs3389433057 912 S>N No EVA
rs3389426462 950 N>K No EVA
rs33761488 996 K>Q No EVA
rs3412965788 1010 N>T No EVA
rs3407287458 1012 Q>H No EVA

No associated diseases with Q8C129

3 regional properties for Q8C129

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 393 - 610 IPR014782
domain ERAP1-like C-terminal domain 689 - 1008 IPR024571
domain Aminopeptidase N-like, N-terminal domain 174 - 358 IPR045357

Functions

Description
EC Number 3.4.11.3 Aminopeptidases
Subcellular Localization
  • Cell membrane ; Single-pass type II membrane protein
  • Endomembrane system ; Single-pass type II membrane protein
  • Localized mainly in intracellular vesicles together with GLUT4
  • Relocalizes to the plasma membrane in response to insulin
  • The dileucine internalization motif and/or the interaction with tankyrases may be involved in intracellular sequestration (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

12 GO annotations of cellular component

Name Definition
cell surface The external part of the cell wall and/or plasma membrane.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic vesicle membrane The lipid bilayer surrounding a cytoplasmic vesicle.
insulin-responsive compartment A small membrane-bounded vesicle that releases its contents by exocytosis in response to insulin stimulation; the contents are enriched in GLUT4, IRAP and VAMP2.
integral component of plasma membrane The component of the plasma 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.
intracellular organelle Organized structure of distinctive morphology and function, occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
vesicle Any small, fluid-filled, spherical organelle enclosed by membrane.

4 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.
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).

11 GO annotations of biological process

Name Definition
negative regulation of cold-induced thermogenesis Any process that stops, prevents, or reduces the rate of cold-induced thermogenesis.
neuropeptide catabolic process The chemical reactions and pathways resulting in the breakdown of neuropeptides. Neuropeptides are signaling peptides that travel across a synaptic junction.
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 blood pressure Any process in which the force of blood traveling through the circulatory system is increased.
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.
regulation of long-term neuronal synaptic plasticity A process that modulates long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
response to hormone Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hormone stimulus.
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.
SMAD protein signal transduction The cascade of processes by which a signal interacts with a receptor, causing a change in the activity of a SMAD protein, and ultimately effecting a change in the functioning of the 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
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme Homo sapiens (Human) PR
Q9NZ08 ERAP1 Endoplasmic reticulum aminopeptidase 1 Homo sapiens (Human) PR
P15144 ANPEP Aminopeptidase N Homo sapiens (Human) PR
P55786 NPEPPS Puromycin-sensitive aminopeptidase Homo sapiens (Human) PR
Q9UIQ6 LNPEP Leucyl-cystinyl aminopeptidase Homo sapiens (Human) PR
P97449 Anpep Aminopeptidase N Mus musculus (Mouse) PR
Q11011 Npepps Puromycin-sensitive 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
Q10836 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Rattus norvegicus (Rat) PR
Q9JJ22 Erap1 Endoplasmic reticulum aminopeptidase 1 Rattus norvegicus (Rat) PR
P15684 Anpep Aminopeptidase N Rattus norvegicus (Rat) PR
P97629 Lnpep Leucyl-cystinyl aminopeptidase 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
MESFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE
70 80 90 100 110 120
HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRQSPD GTCSLPSART LVICVFVIVV
130 140 150 160 170 180
AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL IQPVATNGKV FPWAQIRLPT AIIPLCYELS
190 200 210 220 230 240
LHPNLTSMTF RGSVTISLQA LQDTRDIILH STGHNISRVT FMSAVSSQEK QVEILEYPYH
250 260 270 280 290 300
EQIAVVAPEP LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKYFA ATQFEPLAAR
310 320 330 340 350 360
SAFPCFDEPA FKATFIIKIT RNEHHTALSN MPKKSSVPAE EGLIQDEFSE SVKMSTYLVA
370 380 390 400 410 420
FIVGEMRNLS QDVNGTLVSV YAVPEKIGQV HHALDTTIKL LEFYQTYFEI QYPLKKLDLV
430 440 450 460 470 480
AIPDFEAGAM ENWGLLTFRE ETLLYDNATS SVADRKLVTK IIAHELAHQW FGNLVTMQWW
490 500 510 520 530 540
NDLWLNEGFA TFMEYFSVEK IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI
550 560 570 580 590 600
EEMFDSLSYF KGASLLLMLK SYLSEDVFRH AVILYLHNHS YAAIQSDDLW DSFNEVTDKT
610 620 630 640 650 660
LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFLRMQ PESQPSDTSH LWHIPISYVT
670 680 690 700 710 720
DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNSNMTGYY IVHYAHDDWT ALINQLKRNP
730 740 750 760 770 780
YVLSDKDRAN LINNIFELAG LGKVPLRMAF DLIDYLKNET HTAPITEALF QTNLIYNLLE
790 800 810 820 830 840
KLGHMDLSSR LVARVHKLLQ NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT
850 860 870 880 890 900
NLFDSWMASN GTQSLPTDVM VTVFKVGART EKGWLFLFSM YSSMGSEAEK NKILEALASS
910 920 930 940 950 960
EDVHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRHFPGHLL AWDFVKENWN KLVHKFHLGS
970 980 990 1000 1010 1020
YTIQSIVAGS THLFSTKTHL SEVQAFFENQ SEATLKLRCV QEALEVIQLN IQWMVRNLKT
LSQWL