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 Q8VZH2

Entry ID Method Resolution Chain Position Source
AF-Q8VZH2-F1 Predicted AlphaFoldDB

53 variants for Q8VZH2

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH06816404 12 K>N No 1000Genomes
ENSVATH06816403 33 T>I No 1000Genomes
tmp_4_15970310_C_T 37 A>T No 1000Genomes
ENSVATH06816402 39 D>H No 1000Genomes
tmp_4_15970303_T_A 39 D>V No 1000Genomes
tmp_4_15970288_G_T 44 A>D No 1000Genomes
ENSVATH12363123 70 S>Y No 1000Genomes
ENSVATH06816399 72 K>M No 1000Genomes
ENSVATH06816399 72 K>T No 1000Genomes
tmp_4_15969777_T_A 108 N>Y No 1000Genomes
ENSVATH14330039 109 G>R No 1000Genomes
ENSVATH06816392 125 H>N No 1000Genomes
ENSVATH06816391 126 N>H No 1000Genomes
ENSVATH06816390 131 N>K No 1000Genomes
tmp_4_15969414_T_A 162 L>F No 1000Genomes
tmp_4_15969368_C_T 178 E>K No 1000Genomes
ENSVATH06816386 180 K>N No 1000Genomes
tmp_4_15969169_C_T 218 G>E No 1000Genomes
tmp_4_15969152_A_G 224 Y>H No 1000Genomes
tmp_4_15968715_C_T 306 A>T No 1000Genomes
ENSVATH12363041 344 L>M No 1000Genomes
tmp_4_15968204_A_C 410 V>G No 1000Genomes
ENSVATH12363035 413 K>N No 1000Genomes
tmp_4_15968019_G_A 425 S>L No 1000Genomes
tmp_4_15967984_C_G 437 E>Q No 1000Genomes
tmp_4_15967977_C_T 439 G>E No 1000Genomes
tmp_4_15967902_A_T 464 I>K No 1000Genomes
ENSVATH06816359 527 S>N No 1000Genomes
ENSVATH06816358 530 I>N No 1000Genomes
tmp_4_15967530_C_T 557 A>T No 1000Genomes
ENSVATH06816357 564 E>D No 1000Genomes
ENSVATH00549731 584 T>S No 1000Genomes
ENSVATH06816353 598 C>F No 1000Genomes
ENSVATH06816354 598 C>S No 1000Genomes
tmp_4_15967186_T_C 616 I>V No 1000Genomes
tmp_4_15967175_T_G 619 K>N No 1000Genomes
ENSVATH12362994 630 E>* No 1000Genomes
ENSVATH12362993 630 E>V No 1000Genomes
ENSVATH00549727 644 Q>H No 1000Genomes
tmp_4_15967101_T_G 644 Q>P No 1000Genomes
tmp_4_15967096_C_T 646 A>T No 1000Genomes
tmp_4_15966895_T_C 681 T>A No 1000Genomes
tmp_4_15966853_C_G 695 D>H No 1000Genomes
ENSVATH00549725 718 N>K Number of days following stratification to opening of first flower. the experiment was stopped at 200 d and accessions that had not flowered at that point were assigned a value of 200 [18c with 16 hrs daylight and vernalized (5 wks at 4c)] Plants were checked bi-weekly for presence of first buds and the average flowering time of 4 plants of the same accession were collected [10c and 16 hrs daylight] Number of days following stratification to opening of first flower. the experiment was stopped at 200 d and accessions that had not flowered at that point were assigned a value of 200 [18c and 16 hrs daylight] Number of days following stratification to opening of first flower. the experiment was stopped at 200 d and accessions that had not flowered at that point were assigned a value of 200 [18c and 8 hrs daylight] Plants were checked bi-weekly for presence of first buds and the average flowering time of 4 plants of the same accession were collected [22c and 16 hrs daylight] Plants were checked bi-weekly for presence of first buds and the average flowering time of 4 plants of the same accession were collected [16c and 16 hrs daylight] Number of days required for the bolt height to reach 5cm [23c and 16hrs daylight. vernalized for 8 wks at 5c and 8hrs daylight] Flowering time was scored as the number of days between germination date and appearance of the first flower [growth in field with natural light and started in october] Number of days required for the bolt height to reach 5cm [23c and 16hrs daylight. vernalized for 2 wks at 5c and 8hrs daylight] Flowering time was scored as the number of days for the bolt to reach 5cm [20-22c and natural light from the middle of october 2002 till march 2003] Plants were checked bi-weekly for presence of first buds and the average leaf number at flowering time of 4 plants of the same accession were collected [22c and 16 hrs daylight] [EnsemblGenome] No 1000Genomes
ENSVATH06816343 754 P>L No 1000Genomes
ENSVATH12362959 757 V>D No 1000Genomes
tmp_4_15966478_C_A 759 D>Y No 1000Genomes
tmp_4_15966321_C_A 777 G>V No 1000Genomes
ENSVATH06816342 820 P>S No 1000Genomes
ENSVATH12362927 824 F>Y No 1000Genomes
ENSVATH12362926 868 N>T No 1000Genomes
ENSVATH12362925 875 Q>K No 1000Genomes
tmp_4_15965929_G_A 876 L>F No 1000Genomes

No associated diseases with Q8VZH2

3 regional properties for Q8VZH2

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 235 - 451 IPR014782
domain ERAP1-like C-terminal domain 536 - 854 IPR024571
domain Aminopeptidase N-like, N-terminal domain 15 - 200 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

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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).
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 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.
N-1-naphthylphthalamic acid binding Binding to N-1-naphthylphthalamic acid, an auxin transport inhibitor.
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).

3 GO annotations of biological process

Name Definition
auxin polar transport The unidirectional movement of auxin in the stem from tip to base along the vector of gravity or basipetally.
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
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
10 20 30 40 50 60
MDQFKGEPRL PKFAVPKRYD LRLNPDLIAC TFTGTVAIDL DIVADTRFIV LNAADLSVND
70 80 90 100 110 120
ASVSFTPPSS SKALAAPKVV LFEEDEILVL EFGEILPHGV GVLKLGFNGV LNDKMKGFYR
130 140 150 160 170 180
STYEHNGEKK NMAVTQFEPA DARRCFPCWD EPACKATFKI TLEVPTDLVA LSNMPIMEEK
190 200 210 220 230 240
VNGNLKIVSY QESPIMSTYL VAIVVGLFDY VEDHTSDGIK VRVYCQVGKA DQGKFALHVG
250 260 270 280 290 300
AKTLDLFKEY FAVPYPLPKM DMIAIPDFAA GAMENYGLVT YRETALLYDE QHSAASNKQR
310 320 330 340 350 360
VATVVAHELA HQWFGNLVTM EWWTHLWLNE GFATWVSYLA TDSLFPEWKI WTQFLDESTE
370 380 390 400 410 420
GLRLDGLEES HPIEVEVNHA AEIDEIFDAI SYRKGASVIR MLQSYLGAEV FQKSLAAYIK
430 440 450 460 470 480
NHAYSNAKTE DLWAALEAGS GEPVNKLMSS WTKQKGYPVV SAKIKDGKLE LEQSRFLSSG
490 500 510 520 530 540
SPGEGQWIVP VTLCCGSYEK RKNFLLESKS GAYDLKELLG CSIADGSDKI NGTCSWIKIN
550 560 570 580 590 600
VDQAGFYRVK YDDSLAAGLR NATESQSLTS IDRYGILDDS FALTMARQQS LASLLTLCSA
610 620 630 640 650 660
YKKELDYTVL SNLIAISYKV VKIGADANQE LMSGIKHFFI GVFQFAAGKL GWDPKQGESH
670 680 690 700 710 720
LDAMLRGEVL TALAVFGHDE TLKEAVRRFD AFLADRNTPL LPPDIRRAAY VAVMQRANKS
730 740 750 760 770 780
DKSGYESLLR VYRETDLSQE KTRILGSLAS CPDPTIVQDV LNFVLSDEVR NQDALYGLSG
790 800 810 820 830 840
VSWEGREVAW KWLQEKWEYI GNTWGSGFLI TRFISAVVSP FASFEKAKEV EEFFATRSKP
850 860 870
SMARTLKQSI ERVHINANWV ESIKKEDNLT QLVAQLSSN