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 O35350

Entry ID Method Resolution Chain Position Source
AF-O35350-F1 Predicted AlphaFoldDB

32 variants for O35350

Variant ID(s) Position Change Description Diseaes Association Provenance
rs258891646 2 T>A No EVA
rs3406973343 10 Y>* No EVA
rs3406973327 10 Y>H No EVA
rs3408817481 11 C>Y No EVA
rs3389429152 32 E>D No EVA
rs3389521540 84 K>Q No EVA
rs3408972220 164 I>K No EVA
rs3408928391 197 K>N No EVA
rs3389525358 198 V>E No EVA
rs3389525312 251 S>C No EVA
rs3389532685 340 D>E No EVA
rs3389521004 374 T>I No EVA
rs3389521524 379 S>I No EVA
rs8276852 410 Y>C No EVA
rs3389486655 430 R>S No EVA
rs3389468297 432 R>C No EVA
rs3389468297 432 R>G No EVA
rs3389476803 433 R>C No EVA
rs3389486617 434 F>L No EVA
rs3389514628 447 Q>H No EVA
rs3389468306 451 E>G No EVA
rs37004166 453 A>V No EVA
rs3389486611 471 A>T No EVA
rs3389532649 513 F>Y No EVA
rs3408222526 526 Q>H No EVA
rs3389476770 546 F>L No EVA
rs3389512929 549 L>F No EVA
rs3389468271 599 D>E No EVA
rs3389521546 613 W>C No EVA
rs3389529005 621 T>I No EVA
rs3389429093 695 L>P No EVA
rs3389528995 701 F>L No EVA

No associated diseases with O35350

2 regional properties for O35350

Type Name Position InterPro Accession
domain Potassium channel domain 87 - 145 IPR013099-1
domain Potassium channel domain 181 - 251 IPR013099-2

Functions

Description
EC Number 3.4.22.52 Cysteine endopeptidases
Subcellular Localization
  • Cytoplasm
  • Cell membrane
  • Translocates to the plasma membrane upon Ca(2+) binding
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
calpain complex A calcium-dependent protease complex that processes its substrate by limited proteolysis rather than degrading it. In some cases limited proteolysis is required for the activation of its substrate.
cornified envelope A type of plasma membrane that has been modified through addition of distinct intracellular and extracellular components, including ceramide, found in cornifying epithelial cells (corneocytes).
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
calcium-dependent cysteine-type endopeptidase activity Catalysis of the hydrolysis of nonterminal peptide bonds in a polypeptide chain by a mechanism using a cysteine residue at the enzyme active center, and requiring the presence of calcium.
cytoskeletal protein binding Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
enzyme binding Binding to an enzyme, a protein with catalytic activity.
peptidase activity Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.

14 GO annotations of biological process

Name Definition
cellular response to hydrogen peroxide Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
mammary gland involution The tissue remodeling that removes differentiated mammary epithelia during weaning.
negative regulation of actin filament polymerization Any process that stops, prevents, or reduces the frequency, rate or extent of actin polymerization.
negative regulation of NIK/NF-kappaB signaling Any process that stops, prevents or reduces the frequency, rate or extent of NIK/NF-kappaB signaling.
positive regulation of cardiac muscle cell apoptotic process Any process that increases the rate or extent of cardiac cell apoptotic process, a form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases whose actions dismantle a cardiac muscle cell and result in its death.
positive regulation of leukocyte tethering or rolling Any process that activates or increases the frequency, rate or extent of leukocyte tethering or rolling.
positive regulation of vascular permeability Any process that increases the extent to which blood vessels can be pervaded by fluid.
protein autoprocessing Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein.
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
receptor catabolic process The chemical reactions and pathways resulting in the breakdown of a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
regulation of catalytic activity Any process that modulates the activity of an enzyme.
response to angiotensin Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an angiotensin stimulus. Angiotensin is any of three physiologically active peptides (angiotensin II, III, or IV) processed from angiotensinogen.
self proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds.

19 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q27971 CAPN2 Calpain-2 catalytic subunit Bos taurus (Bovine) PR
Q27970 CAPN1 Calpain-1 catalytic subunit Bos taurus (Bovine) PR
P00789 Calpain-1 catalytic subunit Gallus gallus (Chicken) PR
Q9VXH6 CalpC Calpain-C Drosophila melanogaster (Fruit fly) PR
O14815 CAPN9 Calpain-9 Homo sapiens (Human) PR
Q6MZZ7 CAPN13 Calpain-13 Homo sapiens (Human) PR
Q9HC96 CAPN10 Calpain-10 Homo sapiens (Human) PR
P07384 CAPN1 Calpain-1 catalytic subunit Homo sapiens (Human) PR
G3UZ78 Adgb Androglobin Mus musculus (Mouse) PR
O08529 Capn2 Calpain-2 catalytic subunit Mus musculus (Mouse) PR
Q3UW68 Capn13 Calpain-13 Mus musculus (Mouse) PR
Q9D805 Capn9 Calpain-9 Mus musculus (Mouse) PR
Q9ESK3 Capn10 Calpain-10 Mus musculus (Mouse) PR
P43367 CAPN2 Calpain-2 catalytic subunit Sus scrofa (Pig) PR
P35750 CAPN1 Calpain-1 catalytic subunit Sus scrofa (Pig) PR
O35920 Capn9 Calpain-9 Rattus norvegicus (Rat) PR
Q5BK10 Capn13 Calpain-13 Rattus norvegicus (Rat) PR
Q07009 Capn2 Calpain-2 catalytic subunit Rattus norvegicus (Rat) PR
P97571 Capn1 Calpain-1 catalytic subunit Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MTEELITPVY CTGVSAQVQK KRDKELGLGR HENAIKYLGQ DYETLRARCL QSGVLFQDEA
70 80 90 100 110 120
FPPVSHSLGF KELGPHSSKT YGIKWKRPTE LMSNPQFIVD GATRTDICQG ALGDCWLLAA
130 140 150 160 170 180
IASLTLNETI LHRVVPYGQS FQDGYAGIFH FQLWQFGEWV DVVIDDLLPT KDGKLVFVHS
190 200 210 220 230 240
AQGNEFWSAL LEKAYAKVNG SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK
250 260 270 280 290 300
ALERGSLLGC SINISDIRDL EAITFKNLVR GHAYSVTGAK QVTYQGQRVN LIRMRNPWGE
310 320 330 340 350 360
VEWKGPWSDS SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI CNLTPDALKS
370 380 390 400 410 420
RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LEEVDDADDY DNRESGCSFL
430 440 450 460 470 480
LALMQKHRRR ERRFGRDMET IGFAVYQVPR ELAGQPVHLK RDFFLANASR AQSEHFINLR
490 500 510 520 530 540
EVSNRIRLPP GEYIVVPSTF EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE
550 560 570 580 590 600
EIDDNFKTLF SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG
610 620 630 640 650 660
NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL NKKLHELIIT
670 680 690 700 710
RYSEPDLAVD FDNFVCCLVR LETMFRFFKL LDTDLDGVVT FDLFKWLQLT MFA