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 Q8K093

Entry ID Method Resolution Chain Position Source
AF-Q8K093-F1 Predicted AlphaFoldDB

41 variants for Q8K093

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389129311 147 K>R No EVA
rs3389114147 182 V>I No EVA
rs3389129113 197 E>G No EVA
rs3389125940 200 A>* No EVA
rs3389138002 200 A>V No EVA
rs3389129307 211 L>F No EVA
rs3389114197 221 V>I No EVA
rs3389114126 240 A>V No EVA
rs3389126387 247 L>F No EVA
rs3389131440 261 R>* No EVA
rs3389138029 278 P>Q No EVA
rs3389129168 283 P>T No EVA
rs3389125975 295 H>Q No EVA
rs3389137975 296 Q>* No EVA
rs3389099914 304 N>S No EVA
rs3389092142 305 M>I No EVA
rs8275351 336 A>G No EVA
rs8275352 339 N>K No EVA
rs8275353 345 T>N No EVA
rs8275354 346 T>S No EVA
rs8275355 347 T>P No EVA
rs8275356 349 S>R No EVA
rs3389135403 351 V>I No EVA
rs3401011669 412 L>P No EVA
rs3401011596 417 E>Q No EVA
rs3389123433 431 Y>F No EVA
rs236659285 607 T>M No EVA
rs8275447 650 N>K No EVA
rs3389138000 659 I>F No EVA
rs3389131410 662 V>L No EVA
rs3389126197 673 Y>F No EVA
rs3401753378 761 A>G No EVA
rs221988824 797 R>K No EVA
rs3389104014 836 T>A No EVA
rs3389092196 863 S>* No EVA
rs3389137991 864 L>V No EVA
rs3389126323 865 L>M No EVA
rs3389124053 866 D>V No EVA
rs3389129321 873 I>V No EVA
rs3389131472 954 E>D No EVA
rs3389119409 980 K>E No EVA

No associated diseases with Q8K093

3 regional properties for Q8K093

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 369 - 592 IPR014782
domain ERAP1-like C-terminal domain 679 - 1005 IPR024571
domain Aminopeptidase N-like, N-terminal domain 147 - 332 IPR045357

Functions

Description
EC Number 3.4.19.6 Omega peptidases
Subcellular Localization
  • Membrane ; Single-pass type II membrane protein
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.
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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

4 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.
pyroglutamyl-peptidase activity Catalysis of the release of the N-terminal pyroglutamyl group from a peptide or protein.
zinc ion binding Binding to a zinc ion (Zn).

4 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.
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
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
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme 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
Q9EQH2 Erap1 Endoplasmic reticulum aminopeptidase 1 Mus musculus (Mouse) PR
P15145 ANPEP Aminopeptidase N Sus scrofa (Pig) PR
Q9JJ22 Erap1 Endoplasmic reticulum aminopeptidase 1 Rattus norvegicus (Rat) 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
MGEDDAALRA SGRGLSDPWA DSVGVRPRTT ERHIAVHKRL VLAFAVSIVA LLAVTMLAVL
70 80 90 100 110 120
LSLRFDECGA SAAMPGTDGG LGGFPERDSN SSFPGSARRN HHAGGESSQR ESGEVGTPGT
130 140 150 160 170 180
PSAQPPSEEE REQWQPWTQL RLSGHLKPLH YNLMLTAFME NFTFSGEVNV EIACRNATRY
190 200 210 220 230 240
VVLHASRVAV EKVQVAEDRA FGAVPVAGFF LYPQTQVLVV VLNRTLDAQR HYNLKIIYNA
250 260 270 280 290 300
LIENELLGFF RSSYVIHGER RFLGVTQFSP THARKAFPCF DEPIYKATFK ISIKHQATYL
310 320 330 340 350 360
SLSNMPVETS VFEEDGWVTD HFSQTPLMST YYLAWAICNF TYRETTTKSG VVVRLYARPD
370 380 390 400 410 420
AIRRGSGDYA LHITKRLIEF YEDYFKVPYS LPKLDLLAVP KHPYAAMENW GLSIFVEQRI
430 440 450 460 470 480
LLDPSVSSIS YLLDVTMVIV HEICHQWFGD LVTPVWWEDV WLKEGFAHYF EFVGTDYLYP
490 500 510 520 530 540
AWNMEKQRFL TDVLHEVMLL DGLASSHPVS QEVLRATDID RVFDWIAYKK GAALIRMLAN
550 560 570 580 590 600
FMGHSVFQRG LQDYLTIHKY GNAARNDLWN TLSEALRRNG KYVNIQEVMD QWTLQMGYPV
610 620 630 640 650 660
ITILGNTTAE NRILITQQHF IYDIGAKTKA LQLQNSSYLW QIPLTIVVGN RSHVSSEAII
670 680 690 700 710 720
WVSNKSEHHR IAYLDRGSWI LGNINQTGYF RVNYDLRNWR LLIDQLIRNH EVLSVSNRAA
730 740 750 760 770 780
LIDDAFSLAR AGYLPQNIPL EIIRYLSEEK DFLPWHAASR ALYPLDKLLD RMENYNIFNE
790 800 810 820 830 840
YILKQVATTY IKLGWPRNNF NGSLVQASYQ HEELRREVIM LACSFGNKHC HQQASTLISD
850 860 870 880 890 900
WISSNRNRIP LNVRDIVYCT GVSLLDEDVW EFIWMKFHST TAVSEKKILL EALTCSDDRN
910 920 930 940 950 960
LLSRLLNLSL NSEVVLDQDA IDVIIHVARN PHGRDLAWKF FRDKWKILNT RYGEALFMNS
970 980 990 1000 1010 1020
KLISGVTEFL NTEGELKELK NFMKSYDGVA SASFSRAVET VEANVRWKRF YQDELFQWLG
KAMRH