Q4JHS0

SS
Gene name
BID
Protein name
BH3-interacting domain death agonist
Names
p22 BID , BID [Cleaved into: BH3-interacting domain death agonist p15 , p15 BID; BH3-interacting domain death agonist p13 , p13 BID; BH3-interacting domain death agonist p11 , p11 BID]
Species
Sus scrofa (Pig)
KEGG Pathway
ssc:594852
EC number
Protein Class

Descriptions

BID is a proapoptotic member of the BCL2 family that shares only the BH3 domain homology with other members of the family in its amino acid sequence. The full-length BID is inactive and present in the cytosolic fraction of living cells. Upon cleavage by Caspase 8, the C-terminal part of BID translocates to mitochondria and is sufficient to trigger cytochrome c release in isolated mitochondria. The N-terminal segment may serve as an internal inhibitor of proapoptotic activity. The proapoptotic activity of BID is expected to require dissociation of the N-terminal segment including H1(14-29) and H2(33-41).

Autoinhibitory domains (AIDs)

14-41 (N-terminal autoinhibitory segment including two helices H1 and H2) SS

Target domain

83-99 (BH3 domain)

Relief mechanism

Cleavage

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for Q4JHS0

Entry ID Method Resolution Chain Position Source
5UA4 X-ray 260 A B 73-106 PDB
AF-Q4JHS0-F1 Predicted AlphaFoldDB

5 variants for Q4JHS0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs700956925 15 R>C No EVA
rs788609921 68 A>S No EVA
rs697649085 76 Q>E No EVA
rs321037631 86 H>Q No EVA
rs700739156 124 L>M No EVA

No associated diseases with Q4JHS0

No regional properties for Q4JHS0

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q4JHS0

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Mitochondrion membrane
  • Mitochondrion outer membrane
  • When uncleaved, it is predominantly cytoplasmic (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrial outer membrane The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
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.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

5 GO annotations of biological process

Name Definition
apoptotic mitochondrial changes The morphological and physiological alterations undergone by mitochondria during apoptosis.
hepatocyte apoptotic process Any apoptotic process in a hepatocyte, the main structural component of the liver.
positive regulation of extrinsic apoptotic signaling pathway Any process that activates or increases the frequency, rate or extent of extrinsic apoptotic signaling pathway.
positive regulation of intrinsic apoptotic signaling pathway Any process that activates or increases the frequency, rate or extent of intrinsic apoptotic signaling pathway.
positive regulation of release of cytochrome c from mitochondria Any process that increases the rate, frequency or extent of release of cytochrome c from mitochondria, the process in which cytochrome c is enabled to move from the mitochondrial intermembrane space into the cytosol, which is an early step in apoptosis and leads to caspase activation.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P55957 BID BH3-interacting domain death agonist Homo sapiens (Human) EV
P70444 Bid BH3-interacting domain death agonist Mus musculus (Mouse) PR
Q9JLT6 Bid BH3-interacting domain death agonist Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MDSKVSNGSS LQDERITNLL VFGFLQSCPH ASFHKELEVL GHELPVHTSG SDELQTDGNR
70 80 90 100 110 120
CSYFMEDAAE TDSESQEAVI RDIARHLARI GDRMEYGIRP GLVDSLAAQF RNQSLSEEDR
130 140 150 160 170 180
RQGLAAVLQQ LVHSYPADMG QEKTLLVLTM LLARKVAEHS PALLRDVFHT TVNFINQNLL
190
TYLRNLVQSE MD