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 P32454

Entry ID Method Resolution Chain Position Source
AF-P32454-F1 Predicted AlphaFoldDB

12 variants for P32454

Variant ID(s) Position Change Description Diseaes Association Provenance
s11-155002 3 I>V No SGRP
s11-155028 11 S>R No SGRP
s11-155160 55 M>I No SGRP
s11-155190 65 R>S No SGRP
s11-155672 98 N>K No SGRP
s11-155824 149 T>I No SGRP
s11-155880 168 E>K No SGRP
s11-156735 453 S>G No SGRP
s11-156977 533 D>E No SGRP
s11-157354 659 L>Q No SGRP
s11-158097 907 K>Q No SGRP
s11-158234 952 Y>F No SGRP

No associated diseases with P32454

3 regional properties for P32454

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 324 - 541 IPR014782
domain ERAP1-like C-terminal domain 614 - 928 IPR024571
domain Aminopeptidase N-like, N-terminal domain 107 - 290 IPR045357

Functions

Description
EC Number
Subcellular Localization
  • Periplasm
  • Cytoplasm
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cell wall-bounded periplasmic space The region between the plasma membrane and the cell wall in organisms lacking an outer cell membrane such as yeast and Gram positive bacteria. The region is thinner than the equivalent in Gram negative bacteria.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

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.

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
P79171 ANPEP Aminopeptidase N Felis catus (Cat) (Felis silvestris catus) PR
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme Homo sapiens (Human) PR
P15144 ANPEP Aminopeptidase N 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
Q8K093 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Mus musculus (Mouse) PR
P97449 Anpep Aminopeptidase N Mus musculus (Mouse) PR
Q8C129 Lnpep Leucyl-cystinyl aminopeptidase Mus musculus (Mouse) PR
Q9EQH2 Erap1 Endoplasmic reticulum aminopeptidase 1 Mus musculus (Mouse) PR
Q11011 Npepps Puromycin-sensitive aminopeptidase Mus musculus (Mouse) PR
P15145 ANPEP Aminopeptidase N Sus scrofa (Pig) PR
Q10836 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme Rattus norvegicus (Rat) 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
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
MPIVRWLLLK SAVRGSSLIG KAHPCLRSIA AHPRYLSNVY SPPAGVSRSL RINVMWKQSK
70 80 90 100 110 120
LTPPRFVKIM NRRPLFTETS HACAKCQKTS QLLNKTPNRE ILPDNVVPLH YDLTVEPDFK
130 140 150 160 170 180
TFKFEGSVKI ELKINNPAID TVTLNTVDTD IHSAKIGDVT SSEIISEEEQ QVTTFAFPKG
190 200 210 220 230 240
TMSSFKGNAF LDIKFTGILN DNMAGFYRAK YEDKLTGETK YMATTQMEPT DARRAFPCFD
250 260 270 280 290 300
EPNLKASFAI TLVSDPSLTH LSNMDVKNEY VKDGKKVTLF NTTPKMSTYL VAFIVAELKY
310 320 330 340 350 360
VESKNFRIPV RVYATPGNEK HGQFAADLTA KTLAFFEKTF GIQYPLPKMD NVAVHEFSAG
370 380 390 400 410 420
AMENWGLVTY RVVDLLLDKD NSTLDRIQRV AEVVQHELAH QWFGNLVTMD WWEGLWLNEG
430 440 450 460 470 480
FATWMSWYSC NEFQPEWKVW EQYVTDTLQH ALSLDSLRSS HPIEVPVKKA DEINQIFDAI
490 500 510 520 530 540
SYSKGASLLR MISKWLGEET FIKGVSQYLN KFKYGNAKTE DLWDALADAS GKDVRSVMNI
550 560 570 580 590 600
WTKKVGFPVI SVSEDGNGKI TFRQNRYLST ADVKPDEDKT IYPVFLALKT KNGVDSSVVL
610 620 630 640 650 660
SERSKTIELE DPTFFKVNSE QSGIYITSYT DERWAKLGQQ ADLLSVEDRV GLVADVKTLS
670 680 690 700 710 720
ASGYTSTTNF LNLVSKWNNE KSFVVWDQII NSISSMKSTW LFEPKETQDA LDNFTKQLIS
730 740 750 760 770 780
GMTHHLGWEF KSSDSFSTQR LKVTMFGAAC AARDADVEKA ALKMFTDYCS GNKEAIPALI
790 800 810 820 830 840
KPIVFNTVAR VGGAENYEKV YKIYLDPISN DEKLAALRSL GRFKEPKLLE RTLGYLFDGT
850 860 870 880 890 900
VLNQDIYIPM QGMRAHQEGV EALWNWVKKN WDELVKRLPP GLSMLGSVVT LGTSGFTSMQ
910 920 930 940 950
KIDEIKKFFA TKSTKGFDQS LAQSLDTITS KAQWVNRDRD VVNKYLKENG YY