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 A1CSW4

Entry ID Method Resolution Chain Position Source
AF-A1CSW4-F1 Predicted AlphaFoldDB

No variants for A1CSW4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1CSW4

No associated diseases with A1CSW4

1 regional properties for A1CSW4

Type Name Position InterPro Accession
domain Peptidase S9, prolyl oligopeptidase, catalytic domain 491 - 702 IPR001375

Functions

Description
EC Number
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.

2 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.
serine-type peptidase activity Catalysis of the hydrolysis of 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
MGALTWLSVV AAAASTALAM TPEKMISAPR RSEVIPNPSG EIGVFSTSQY SFEKHKRSSW
70 80 90 100 110 120
WSLLDLKTGQ SKILTNDSSV SEILWLGTDD STLLYVNGTN ADVPGGVELW VTQVSSFTNG
130 140 150 160 170 180
YKAASLPAAF SGFKTVTTKS GDIRFVAYAQ SYANGTAYNE ELVEKPLSSA RIYDSIYVRH
190 200 210 220 230 240
WDSYLTTTFN AVFSGTLKKG NNKKGYTLDG AVKNLVSPVR NAESPYPPFG GASDYDLSPN
250 260 270 280 290 300
GKWVAFKSKA PELPKANFTT AYIYLVPHDG SEKAFAINGP DSPGTPKGIK GDANSPVFSP
310 320 330 340 350 360
NSEKLAYLQM KDETYEADRR VLYVYSIGSK KTIPSVAGNW DRSPDSIKWT PDGKTLIVGS
370 380 390 400 410 420
EDKGRSRLFA IPATARDDFK PKNFTDGGAV SAYYFLPDRS LLVTGTAIWT NWNVYTASPA
430 440 450 460 470 480
KGVIKTLASA NEIDPELKGL GPSDVSEIYF KGNWTDIHAW VVYPENFDKS KKYPLAFLIH
490 500 510 520 530 540
GGPQGSWADS WSSRWNPKTF ADQGYVVVAP NPTGSTGFGQ KLTDEIQNNW GGAPYDDLVK
550 560 570 580 590 600
CWEYVNKNLP FVDTEHGIAA GASYGGFMVN WIQGNDLGRR FKALVSHDGT FVADAKISTD
610 620 630 640 650 660
ELWFMQREFN GTFWDARDNY RRFDPSAPEH IRQFGTPQLV IHNDKDYRLA VAEGLSLFNV
670 680 690 700 710 720
LQERGVPSRF LNFPDENHWV VNPENSLVWH QQVLGWINKY SGIEKSNPGA VSLDDTIVPV
VNYN