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 P56203

Entry ID Method Resolution Chain Position Source
AF-P56203-F1 Predicted AlphaFoldDB

28 variants for P56203

Variant ID(s) Position Change Description Diseaes Association Provenance
rs16789981 26 T>I No EVA
rs3389427626 29 A>V No EVA
rs3389517649 42 L>M No EVA
rs3389521788 44 Q>H No EVA
rs3389517665 53 N>D No EVA
rs3389512056 105 R>K No EVA
rs16790002 108 E>K No EVA
rs3389510548 138 I>T No EVA
rs16790003 146 G>E No EVA
rs3389531099 147 S>R No EVA
rs16790005 171 F>L No EVA
rs3389511977 211 K>* No EVA
rs3389527586 218 D>N No EVA
rs3389485081 223 R>T No EVA
rs16790013 250 H>R No EVA
rs16790014 254 V>M No EVA
rs3389510517 279 P>L No EVA
rs3389466014 282 C>S No EVA
rs3389427650 292 L>M No EVA
rs3409288365 305 T>K No EVA
rs3389518680 319 S>F No EVA
rs3389532905 330 A>S No EVA
rs211894509 331 H>Q No EVA
rs3389485107 347 C>R No EVA
rs16790016 349 V>I No EVA
rs3389527570 358 V>M No EVA
rs225000819 366 R>Q No EVA
rs16789887 367 T>I No EVA

No associated diseases with P56203

5 regional properties for P56203

Type Name Position InterPro Accession
domain Peptidase C1A, papain C-terminal 126 - 357 IPR000668
domain Cathepsin propeptide inhibitor domain (I29) 40 - 97 IPR013201
active_site Cysteine peptidase, histidine active site 287 - 297 IPR025660
active_site Cysteine peptidase, asparagine active site 321 - 340 IPR025661
domain Papain-like cysteine endopeptidase 127 - 356 IPR039417

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
lysosome A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.

1 GO annotations of molecular function

Name Definition
cysteine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.

1 GO annotations of biological process

Name Definition
proteolysis involved in protein catabolic process The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P43234 CTSO Cathepsin O Homo sapiens (Human) PR
P56202 CTSW Cathepsin W Homo sapiens (Human) PR
Q8BM88 Ctso Cathepsin O Mus musculus (Mouse) PR
O70370 Ctss Cathepsin S Mus musculus (Mouse) PR
P49935 Ctsh Pro-cathepsin H Mus musculus (Mouse) PR
P43296 RD19A Cysteine protease RD19A Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MTLTAHLSYF LVLLLAGQGL SDSLLTKDAG PRPLELKEVF KLFQIRFNRS YWNPAEYTRR
70 80 90 100 110 120
LSIFAHNLAQ AQRLQQEDLG TAEFGETPFS DLTEEEFGQL YGQERSPERT PNMTKKVESN
130 140 150 160 170 180
TWGESVPRTC DWRKAKNIIS SVKNQGSCKC CWAMAAADNI QALWRIKHQQ FVDVSVQELL
190 200 210 220 230 240
DCERCGNGCN GGFVWDAYLT VLNNSGLASE KDYPFQGDRK PHRCLAKKYK KVAWIQDFTM
250 260 270 280 290 300
LSNNEQAIAH YLAVHGPITV TINMKLLQHY QKGVIKATPS SCDPRQVDHS VLLVGFGKEK
310 320 330 340 350 360
EGMQTGTVLS HSRKRRHSSP YWILKNSWGA HWGEKGYFRL YRGNNTCGVT KYPFTAQVDS
370
PVKKARTSCP P