XIAP_XENTR
ID XIAP_XENTR Reviewed; 492 AA.
AC Q5BKL8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=E3 ubiquitin-protein ligase XIAP {ECO:0000250|UniProtKB:P98170};
DE EC=2.3.2.27;
DE AltName: Full=Baculoviral IAP repeat-containing protein 4 {ECO:0000250|UniProtKB:P98170};
DE AltName: Full=RING-type E3 ubiquitin transferase XIAP;
DE AltName: Full=X-linked inhibitor of apoptosis protein {ECO:0000250|UniProtKB:A5D8Q0};
DE Short=X-linked IAP {ECO:0000250|UniProtKB:A5D8Q0};
GN Name=xiap; Synonyms=birc4 {ECO:0000312|EMBL:AAH91027.1};
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:AAH91027.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=F6 {ECO:0000312|EMBL:AAH91027.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multi-functional protein which regulates not only caspases
CC and apoptosis, but also acts as an E3 ubiquitin-protein ligase
CC mediating ubiquitination and subsequent proteasomal degradation of its
CC target proteins. Acts as a direct caspase inhibitor. A key apoptotic
CC suppressor in eggs. Acts as a positive regulator of Wnt signaling.
CC {ECO:0000250}.
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;
CC -!- SUBUNIT: Monomer, and homodimer. {ECO:0000250|UniProtKB:P98170}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P98170}.
CC -!- DOMAIN: The BIR and RING-type domains are dispensable for anti-
CC apoptotic function. {ECO:0000250|UniProtKB:A5D8Q0}.
CC -!- PTM: Degraded in a 2-step mechanism; a caspase-independent first step
CC and a caspase-dependent second step. Stabilized indirectly by MAPK,
CC which acts to delay caspase activation, rather than directly
CC phosphorylating xiap. {ECO:0000250|UniProtKB:A5D8Q0}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000255}.
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DR EMBL; BC091027; AAH91027.1; -; mRNA.
DR RefSeq; NP_001025583.1; NM_001030412.1.
DR AlphaFoldDB; Q5BKL8; -.
DR SMR; Q5BKL8; -.
DR PaxDb; Q5BKL8; -.
DR DNASU; 594971; -.
DR Ensembl; ENSXETT00000035327; ENSXETP00000035327; ENSXETG00000016194.
DR GeneID; 594971; -.
DR KEGG; xtr:594971; -.
DR CTD; 331; -.
DR Xenbase; XB-GENE-948846; xiap.
DR eggNOG; KOG1101; Eukaryota.
DR InParanoid; Q5BKL8; -.
DR OrthoDB; 1340284at2759; -.
DR Reactome; R-XTR-111463; SMAC (DIABLO) binds to IAPs.
DR Reactome; R-XTR-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes.
DR Reactome; R-XTR-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-XTR-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-XTR-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-XTR-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-XTR-5675482; Regulation of necroptotic cell death.
DR Reactome; R-XTR-8948747; Regulation of PTEN localization.
DR Reactome; R-XTR-8948751; Regulation of PTEN stability and activity.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000016194; Expressed in egg cell and 14 other tissues.
DR ExpressionAtlas; Q5BKL8; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; 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:0045861; P:negative regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00022; BIR; 3.
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; 3.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 2.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Developmental protein; Metal-binding;
KW Protease inhibitor; Reference proteome; Repeat; Thiol protease inhibitor;
KW Transferase; Ubl conjugation pathway; Wnt signaling pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..492
FT /note="E3 ubiquitin-protein ligase XIAP"
FT /id="PRO_0000379958"
FT REPEAT 40..105
FT /note="BIR 1"
FT /evidence="ECO:0000255"
FT REPEAT 172..237
FT /note="BIR 2"
FT /evidence="ECO:0000255"
FT REPEAT 271..334
FT /note="BIR 3"
FT /evidence="ECO:0000255"
FT ZN_FING 445..480
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
SQ SEQUENCE 492 AA; 55292 MW; FC13E44849B82AEE CRC64;
MEPQLAEFVL KEEMTCQCPK MSDGAYDMDV DQNYFEEEVR LASFANFPSS YPVSAPALAR
AGFYYTGDGD RVKCFSCLAM VEGWQHGDTA IGKHRKISPN CKFINGFNNL RSDCILTQVP
VMQNGFQNSA EDLAERSSSE IMADYLLRTG RVVDMSTPKY PRHMEMCSEE ARLQTFQNWP
AYSPLTPKEL ANAGLFYTGI NDQVKCFCCG GKLMNWEPSD KAWTEHKKHF PECYFVLGRD
VGNVATEANT HGGRRRGSEL ACPAMNDYNA RLETFSSWSF PIDKETLAKA GFYSIGDGDA
TKCFHCGGVL NCWSATDDPW EEHAKAYPGC KFLIDEKGQH FINHAQLKRP ILHKANSADA
SPALPKDSNL LKSPLVTDAQ QMGFPLEEIK KVMGQKLKTT GKNYTCVEEF VSDLCAQKET
VLEKPKEIEI SLEEKLRQLE EEKICKVCMD RRISIVFIPC GHLVACAVCA DVLDKCPICC
TIVERRQKIF MS
