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 Q17405

Entry ID Method Resolution Chain Position Source
AF-Q17405-F1 Predicted AlphaFoldDB

No variants for Q17405

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q17405

No associated diseases with Q17405

2 regional properties for Q17405

Type Name Position InterPro Accession
binding_site Aminotransferases, class-I, pyridoxal-phosphate-binding site 274 - 287 IPR004838
domain Aminotransferase, class I/classII 50 - 429 IPR004839

Functions

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

2 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.

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
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
P55786 NPEPPS Puromycin-sensitive aminopeptidase Homo sapiens (Human) PR
P15144 ANPEP Aminopeptidase N Homo sapiens (Human) PR
Q9UKU6 TRHDE Thyrotropin-releasing hormone-degrading ectoenzyme Homo sapiens (Human) 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
P97449 Anpep Aminopeptidase N Mus musculus (Mouse) PR
Q8K093 Trhde Thyrotropin-releasing hormone-degrading ectoenzyme 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
Q8VZH2 APM1 Aminopeptidase M1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MEDVDLGKDR TQLIDFVYAN GNGSASNLNN RNNIPLSEKA AKEPLQTQPQ EAPPAPKPKV
70 80 90 100 110 120
QKQKPPVKPK KRIACSPGSA ICLFLLAVAA IIFAAFLGHY LTKQNYEMMQ FKSANESMTT
130 140 150 160 170 180
CKNFTRSHKK HQDIVNEEDA DENASIKQPT KEELALPKNV QPVWYDVSLS PKVGGNGTMG
190 200 210 220 230 240
LAHVKLNIEE PTNKIVLNAK DIEFTRNLEK IQLSKEVTKR AKKSVDSGTN STSEMPEGSG
250 260 270 280 290 300
EEAMATTATT TTTESTTPVS SFVDTGIKVT NIEFDENLEK VTLTLDQELK KGSTVVLKIP
310 320 330 340 350 360
FTSKVSNNNG LKEYKYKNSE GKEQSMFTTQ PSYSYLRHVF PSFDQEAFKA PAAITLMHSK
370 380 390 400 410 420
GSIVVANTGV KTKDDGDAQT STLNKVLDPD FVIGDLVASE VNTTSGITIR IWTRPEVKHS
430 440 450 460 470 480
TEQSLDYANQ AIDAMEHILQ SRLESKSLDI VAVPGFQTGN RVSPSFIVLP EEDILYNEQS
490 500 510 520 530 540
NDINQKTRIA RMISNRIAAQ WFGGITNPEE FGTFWLNEAL PRFLEVEALE KILDINSDDL
550 560 570 580 590 600
WTYEMEKILE RDATATSQPL RVKNVFSSAD IAEIDHEFIG KKGAAVLRMI QKSVGVNVFN
610 620 630 640 650 660
KAIRSFVSSY RSAYPYDDGL WKSFEKALGG KLKGWNNEPL DVAKFVNTWV DQIGFPLVSV
670 680 690 700 710 720
EKLDDETVEL SQERFKNDHK TKEQFKFRNA KYWFNWEVPL FLKSSGPVGN VSWLHEAFRL
730 740 750 760 770 780
PLNTSDSIYL NTDSNGVYRV NYEEKRWNDI AKQLEKSHGK LSERTRARLI SDVFALANSG
790 800 810 820 830 840
ALPFETALNV TSYLPMETAT VPWLIATRIF KKLTERLEGA PIQDKLNSFI YQKIHKKFEE
850 860 870 880 890 900
ISSSPGEASS NYLKNRLYAN LLDLMAIVKP EKSNEKLNEL FVEGFLAPCQ FSGNFSSDCS
910 920 930 940 950 960
EVPGDLREKV YCNGVEFGND TVFETVRELA EKEVDGAEKD LLQNSLACFR DPRALRRLIL
970 980 990 1000 1010 1020
DNLNSTSTVT LLLRKMNSRP VGKEIATNWI IDNWSTVLKK KFKNDPETLN AIADAGIILD
1030 1040 1050 1060 1070 1080
NEREKSMIET FMEHHHKSTH GIESLDKKIE EATTDIYWRK QKINELNDYL DGKMKGPAKD
DEMESSEEQE