A1E2V0

SS
Gene name
BIRC3
Protein name
Baculoviral IAP repeat-containing protein 3
Names
EC 2.3.2.27 , RING-type E3 ubiquitin transferase BIRC3
Species
Canis lupus familiaris (Dog) (Canis familiaris)
KEGG Pathway
cfa:489433
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

E3 ligases mediate the covalent attachment of ubiquitin to target proteins thereby enabling ubiquitin dependent signaling. Baculoviral IAP repeat-containing protein 2 (BIRC2) protein is an E3 ligase that modulates diverse biological processes such as cell survival, proliferation, and migration. Full-length BIRC2 fails to associate with E2, but CARD-deleted mutant BIRC2 readily interacts with E2. The CARD inhibits activation of BIRC2’s E3 activity by preventing RING dimerization, E2 binding, and E2 activation. In addition, BIRC2 lacking only the BIR3 domain readily associates with the E2, representing that the CARD and BIR3 domains are both required for inhibition of E3 activity of BIRC2.

Autoinhibitory domains (AIDs)

421-548 (CARD domain) SS

Target domain

557-602 (RING domain)

Relief mechanism

Ligand binding

Assay

253-324 (BIR3 domain) SS

Target domain

557-602 (RING domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A1E2V0

Entry ID Method Resolution Chain Position Source
AF-A1E2V0-F1 Predicted AlphaFoldDB

8 variants for A1E2V0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3329338362 60 A>S No EVA
rs3329639016 65 R>Q No EVA
rs3329403240 137 S>F No EVA
rs3329338268 147 D>G No EVA
rs3329338529 353 E>G No EVA
rs3329073635 423 V>M No EVA
rs852375326 472 G>R No EVA
rs3329516603 518 D>N No EVA

No associated diseases with A1E2V0

7 regional properties for A1E2V0

Type Name Position InterPro Accession
domain CARD domain 439 - 529 IPR001315
repeat BIR repeat 27 - 98 IPR001370-1
repeat BIR repeat 167 - 237 IPR001370-2
repeat BIR repeat 253 - 324 IPR001370-3
domain Zinc finger, RING-type 557 - 592 IPR001841
domain BIRC2/BIRC3, UBA domain 377 - 421 IPR041933
domain BIRC2/3-like, UBA domain 374 - 426 IPR048875

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

3 GO annotations of molecular function

Name Definition
cysteine-type endopeptidase inhibitor activity involved in apoptotic process Binds to and stops, prevents or reduces the activity of a cysteine-type endopeptidase involved in the apoptotic process.
metal ion binding Binding to a metal ion.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond

5 GO annotations of biological process

Name Definition
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
negative regulation of necroptotic process Any process that decreases the rate, frequency or extent of a necroptotic process, a necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors.
positive regulation of protein ubiquitination Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
regulation of cell cycle Any process that modulates the rate or extent of progression through the cell cycle.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q90660 ITA Inhibitor of apoptosis protein Gallus gallus (Chicken) SS
Q13489 BIRC3 Baculoviral IAP repeat-containing protein 3 Homo sapiens (Human) SS
Q13490 BIRC2 Baculoviral IAP repeat-containing protein 2 Homo sapiens (Human) EV
Q96P09 BIRC8 Baculoviral IAP repeat-containing protein 8 Homo sapiens (Human) PR
O08863 Birc3 Baculoviral IAP repeat-containing protein 3 Mus musculus (Mouse) SS
Q62210 Birc2 Baculoviral IAP repeat-containing protein 2 Mus musculus (Mouse) SS
O62640 PIAP Putative inhibitor of apoptosis Sus scrofa (Pig) SS
10 20 30 40 50 60
MNIVQNSIFL SNLLRSSPVF ELKYDHSCEL YRMSTYSTFP AGVPVSERSL ARAGFYYTGA
70 80 90 100 110 120
KDRVRCFCCG LMLDNWKAGD SPTGKHRNLY PSCSFIQNLS AVSTVGAASQ PPAPLSEARS
130 140 150 160 170 180
THAQSPGLER SSYFSASYSS FPVDPVDFRP SPAMSPWRAG PSCVTMKSEE DRLCTFQGWP
190 200 210 220 230 240
LAFPLPSALA RAGFYYVGPG DRVACFACGG KLSNWEPDDD ALSEHLRHFP DCPFVEGQLQ
250 260 270 280 290 300
ATVRYTASNL SMQTLAARSR TFCNWPPRAP VHPEQLASAG FYYMGHSDDV KCFCCDGGLR
310 320 330 340 350 360
CWESGDDPWV EHAKWFPRCE YLIRIKGQEF ISQIQASYPH LLEQLLSTSD NTEDENTESP
370 380 390 400 410 420
IVHFGPGEYH SEDAVMMNTP VVMAALEMGF SRSLVRQTVQ SKILSTGENY RTVNEIVSDL
430 440 450 460 470 480
LHVEDEIREE EKERAAENRE SDDVSLIRKN KMVLFQHLTY VLPILDSLLM AGVLNEQEHS
490 500 510 520 530 540
SIKQKARTSL QARELIDTVL VKGSSAVTIF KNSLQEIDPM LYKRFFVQQD RKYIPTEDIS
550 560 570 580 590 600
DLPVEEQLRR LQEERTCKVC MDKEVSIVFI PCGHLVVCRD CAPSLRKCPI CRGTVRGTVR
TFLS