BIRC7_XENTR
ID BIRC7_XENTR Reviewed; 365 AA.
AC A9JTP3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Baculoviral IAP repeat-containing protein 7;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96CA5};
DE AltName: Full=E3 ubiquitin-protein ligase EIAP {ECO:0000250|UniProtKB:Q8JHV9};
DE AltName: Full=Embryonic/Egg IAP {ECO:0000250|UniProtKB:Q8JHV9};
DE Short=EIAP/XLX {ECO:0000250|UniProtKB:Q8JHV9};
DE AltName: Full=RING-type E3 ubiquitin transferase BIRC7 {ECO:0000305};
GN Name=birc7;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI55424.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6 {ECO:0000312|EMBL:AAI55424.1};
RC TISSUE=Oviduct {ECO:0000312|EMBL:AAI55424.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-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:Q96CA5};
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}.
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}.
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DR EMBL; BC155423; AAI55424.1; -; mRNA.
DR RefSeq; NP_001106593.2; NM_001113122.1.
DR AlphaFoldDB; A9JTP3; -.
DR SMR; A9JTP3; -.
DR STRING; 8364.ENSXETP00000060882; -.
DR PaxDb; A9JTP3; -.
DR GeneID; 100127811; -.
DR KEGG; xtr:100127811; -.
DR CTD; 79444; -.
DR Xenbase; XB-GENE-5914029; birc7.
DR eggNOG; KOG1101; Eukaryota.
DR InParanoid; A9JTP3; -.
DR OrthoDB; 1340284at2759; -.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
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..365
FT /note="Baculoviral IAP repeat-containing protein 7"
FT /id="PRO_0000379961"
FT REPEAT 7..73
FT /note="BIR 1"
FT /evidence="ECO:0000255"
FT REPEAT 115..180
FT /note="BIR 2"
FT /evidence="ECO:0000255"
FT ZN_FING 318..353
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 186..234
FT /note="Self-inhibits the anti-apoptotic function"
FT /evidence="ECO:0000250|UniProtKB:Q8JHV9"
FT REGION 278..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 176
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 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JHV9"
FT MOD_RES 202
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JHV9"
FT MOD_RES 216
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250"
FT MOD_RES 219
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 40517 MW; 6052953DBD864423 CRC64;
MRSEAERQRS FRAWPHTCRT VSPAELARSG FYYLGPGDRV QCFSCGGVLR SWEPGDRPDT
EHRKFFPSCP FLQVRRGPPG GTDSVDGQIL GQLSGEEPDR TWEPVCPQMA GEGDRLGSFS
TWPRYANGDP QQLAGAGFFY TGHRDHVKCF HCDGGLRNWE QGDDPWTEHA KWFPMCDFLL
QVKGEAFIRS VQESFFSSPE TSPESVGSYE GSPVSSPGSP PVCPFLSTSV AQGALQMGFK
RNRVSSLMIN RFILTGSCYG SVSELVTDLI QAEEIHGTES VSVPRAPTQR ERPEPPKEPA
PPLSTEEQLR QLKEERMCKV CMDNDVSMVF VPCGHLVVCT ECAPNLRHCP ICRAAIRGSV
RAFMS
