A0S5V9

PR
Gene name
DPP4
Protein name
Dipeptidyl peptidase 4
Names
Dipeptidyl peptidase IV, DPP IV, DppIV
Species
Arthroderma otae (Microsporum canis)
KEGG Pathway
EC number
3.4.14.5: Dipeptidyl-peptidases and tripeptidyl-peptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-71 (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 A0S5V9

Entry ID Method Resolution Chain Position Source
AF-A0S5V9-F1 Predicted AlphaFoldDB

No variants for A0S5V9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0S5V9

No associated diseases with A0S5V9

1 regional properties for A0S5V9

Type Name Position InterPro Accession
domain Tetrapyrrole methylase 1 - 237 IPR000878

Functions

Description
EC Number 3.4.14.5 Dipeptidyl-peptidases and tripeptidyl-peptidases
Subcellular Localization
  • Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
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.

3 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.
dipeptidyl-peptidase activity Catalysis of the hydrolysis of N-terminal dipeptides from a polypeptide chain.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKFLSLLLLV GVAQAIVPPR EPRPPTGGGK KLLTYKECVP RATLAPRSTS LAWINSDEDG
70 80 90 100 110 120
QYISQSDDGA LILQNIVTNT NKTLVAADKV PKGFYDYWIK PDLTAVLWAT NYTKQYRHSY
130 140 150 160 170 180
FANYFILDIE KGSLTPLAED QSGDIQYAQW NPVDNSIAYV RGNDLYVWNS GKTKRITENG
190 200 210 220 230 240
GPDTFNGVPD WVYEEEIFGD RFALWFSPDG EYLAYLRFNE TGVPTYTVPY YKNKQKIAPA
250 260 270 280 290 300
YPRELEIRYP KVSAKNPTVQ FHLLNLASSE ETSIPVTAFP EDDLIIGEVA WLSSGHDSVA
310 320 330 340 350 360
FRAFNRVQDT EKIVNVKVGS KESKVIRERD GTDGWIDNLL SMSYIGKVNG KEYYVDISDA
370 380 390 400 410 420
SGWAHLYLYP VDGGKEIALT KGEWEVTAIL KVDTKSKLIY FTSTKFHSTT RHVYSVSYDT
430 440 450 460 470 480
KVMTPLVNDR EAAYYSASFS AKGGYYILSY QGPNVPYQEL YSVKDKKKPI KTITSNDALI
490 500 510 520 530 540
EKLKDYKLPK ITFFEIKLPS GESLNVMQRL PPNFNPFKKY PVLFTPYGGP GAQEVSQAWK
550 560 570 580 590 600
ALDFKAYITS DPELEYVTWT VDNRGTGFKG RKFRSTVTKR LGFLEPQDQV FAAKEILKNR
610 620 630 640 650 660
WADKDHVGMW GWSYGGFLTA KTMETDSGVF TFGMSTAPVS DFRLYDSMYT ERYMKTVELN
670 680 690 700 710 720
ADGYSETAVH KTDGFKNLKG HYLIQHGTGD DNVHFQNSAV LSNTLMNGGV TPDRLTTQWF
730 740 750 760 770
TDSDHGVRYD NDSTFQYKQL TKMVYDQKQP RPQTTPLHQW SKRVLAALFG EEAEE