BIR7B_XENLA
ID BIR7B_XENLA Reviewed; 345 AA.
AC A9ULZ2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Baculoviral IAP repeat-containing protein 7-B;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8JHV9};
DE AltName: Full=E3 ubiquitin-protein ligase EIAP-B;
DE AltName: Full=Embryonic/Egg IAP-B;
DE Short=EIAP/XLX-B;
DE AltName: Full=RING-type E3 ubiquitin transferase EIAP-B {ECO:0000305};
GN Name=birc7-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAI57459.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Weak apoptotic suppressor. Has E3 ubiquitin-protein ligase
CC activity. Weak inhibitor of caspase activity.
CC {ECO:0000250|UniProtKB:Q8JHV9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8JHV9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P98170}.
CC -!- DOMAIN: The BIR2 domain is required for caspase-inhibition.
CC {ECO:0000250|UniProtKB:Q8JHV9}.
CC -!- DOMAIN: The C-terminal region containing the RING finger domain is
CC required for the initial degradation step, and the final digestion of
CC cleavage fragments. {ECO:0000250|UniProtKB:Q8JHV9}.
CC -!- PTM: Auto-ubiquitinated, and degraded in a 2-step mechanism; a caspase-
CC independent first step and a caspase-dependent second step.
CC {ECO:0000250|UniProtKB:Q8JHV9}.
CC -!- PTM: Phosphorylated via MAPK-dependent and CDK-dependent pathways
CC during oocyte maturation. Phosphorylation does not appear to affect
CC caspase inhibition or autoubiquitination activity.
CC {ECO:0000250|UniProtKB:Q8JHV9}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI57459.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC157458; AAI57459.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A9ULZ2; -.
DR SMR; A9ULZ2; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR CDD; cd00022; BIR; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00653; BIR; 2.
DR SMART; SM00238; BIR; 2.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Developmental protein; Metal-binding; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Repeat; Thiol protease inhibitor;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..345
FT /note="Baculoviral IAP repeat-containing protein 7-B"
FT /id="PRO_0000379960"
FT REPEAT 46..112
FT /note="BIR 1"
FT /evidence="ECO:0000255"
FT REPEAT 154..219
FT /note="BIR 2"
FT /evidence="ECO:0000255"
FT ZN_FING 298..333
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 258..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JHV9"
FT MOD_RES 241
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JHV9"
FT MOD_RES 257
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 38484 MW; 83F64EDC86A8D888 CRC64;
MSRWSVSQGC GNSHKALRMS GNREQLLSGW GAPGMLRPSM RSEAERQRSF RAWPRSCPQL
SPVELARSGF YYLGPGDRVQ CFSCGGVLRS WEPGDRPDTE HRKFFPSCPF LQQQQRGPGA
TDSVDGQVLG QLSGEEPDRT WEPVYPEMSE EQVRLGSFST WPLDVPGSPE VLAGAGFFYT
GHRDHVKCFH CDGGLQNWEQ GDDPWTEHAK WFPMCDFLLQ VKGEAFIRSV QESLFSSPEP
SPESLGSYDY DRSLASSTES VSVPRAPTPG ERSEPPKVSG PPLSTEEQLQ RLKEERMCKV
CMDKDVSMLF VPCGHLVVCT ECAPNLRHCP ICRAAIRGSV RAFMS
