XIAP_XENLA
ID XIAP_XENLA Reviewed; 488 AA.
AC A5D8Q0; Q50L37;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 64.
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:0000303|PubMed:15853809};
DE Short=X-linked IAP {ECO:0000303|PubMed:15853809};
DE Short=xXIAP {ECO:0000303|PubMed:15853809};
GN Name=xiap; Synonyms=birc4 {ECO:0000250|UniProtKB:Q5BKL8};
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 [MRNA] (ISOFORM 2), FUNCTION, DEVELOPMENTAL STAGE,
RP DOMAIN FUNCTION, AND PROTEIN DEGRADATION.
RX PubMed=15853809; DOI=10.1111/j.1742-4658.2005.04648.x;
RA Tsuchiya Y., Murai S., Yamashita S.;
RT "Apoptosis-inhibiting activities of BIR family proteins in Xenopus egg
RT extracts.";
RL FEBS J. 272:2237-2250(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fat body {ECO:0000312|EMBL:AAI41766.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032;
RA Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.;
RT "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling.";
RL Mol. Cell 45:619-628(2012).
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:0000269|PubMed:15853809, ECO:0000269|PubMed:22304967}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A5D8Q0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15853809};
CC IsoId=A5D8Q0-2; Sequence=VSP_053138, VSP_053139;
CC -!- DEVELOPMENTAL STAGE: Expressed maternally.
CC {ECO:0000269|PubMed:15853809}.
CC -!- DOMAIN: The BIR and RING-type domains are dispensable for anti-
CC apoptotic function. {ECO:0000269|PubMed:15853809}.
CC -!- PTM: Degraded in a 2-step mechanism; a caspase-independent first step
CC and a caspase-dependent second step (PubMed:15853809). Stabilized
CC indirectly by MAPK, which acts to delay caspase activation, rather than
CC directly phosphorylating xiap (PubMed:15853809).
CC {ECO:0000269|PubMed:15853809}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI41766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB197252; BAD98268.1; -; mRNA.
DR EMBL; BC141765; AAI41766.1; ALT_INIT; mRNA.
DR RefSeq; NP_001089083.1; NM_001095614.1.
DR AlphaFoldDB; A5D8Q0; -.
DR SMR; A5D8Q0; -.
DR MaxQB; A5D8Q0; -.
DR PRIDE; A5D8Q0; -.
DR DNASU; 733235; -.
DR GeneID; 733235; -.
DR KEGG; xla:733235; -.
DR CTD; 733235; -.
DR Xenbase; XB-GENE-948852; xiap.L.
DR OrthoDB; 1340284at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 733235; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP: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; IDA:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0045861; P:negative regulation of proteolysis; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00022; BIR; 3.
DR CDD; cd14395; UBA_BIRC4_8; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR042579; XIAP/BIRC8_UBA.
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 Alternative splicing; Apoptosis; Cytoplasm; Developmental protein;
KW Metal-binding; Protease inhibitor; Reference proteome; Repeat;
KW Thiol protease inhibitor; Transferase; Ubl conjugation pathway;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="E3 ubiquitin-protein ligase XIAP"
FT /id="PRO_0000379957"
FT REPEAT 40..105
FT /note="BIR 1"
FT /evidence="ECO:0000255"
FT REPEAT 176..241
FT /note="BIR 2"
FT /evidence="ECO:0000255"
FT REPEAT 266..329
FT /note="BIR 3"
FT /evidence="ECO:0000255"
FT ZN_FING 441..476
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15853809"
FT /id="VSP_053138"
FT VAR_SEQ 362..424
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15853809"
FT /id="VSP_053139"
FT CONFLICT 231
FT /note="K -> Q (in Ref. 1; BAD98268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55129 MW; D83F7081FF6EB528 CRC64;
MEPQIVKFVF KEEMTCQCPK MSDSACDVDT DQNYFEEEVR LASFANFSSS YPVSAPALAR
AGFYYTGDGD RVKCFSCMAM VEDWQHGDTA IGKHRKISPN CKFINGFNNF RSDCIQTQAP
VMQNSHANGF PNSAEDPGEK SSSEIMADYM LRTGRVVDMS KPKYPRHMAM CSEEARLQTF
QNWPGYSPLM PKELANAGLF YTGINDQVKC FCCGGKLMNW EPSDRAWTEH KKHFPECYFV
LGRDVGNVTR DASVQGSTYM NSYNARLETF SSWPFPIDKE TLAKAGFYRI GDEDATKCFS
CGGMLNCWAA NDDPWEEHAK AYPGCQFLIE EKGQQFINNA QLQRPILHKA NSGEASPALP
KDTSFLKNPL VIYAQQMGFP LEEIKKVMGQ KLKTTGNNYT CVEEFVSDLL CAQSETIADK
PMKREISIEE KLRQLEEEKV CKVCMDRRIT IVFIPCGHLV ACAVCADVLD KCPICCTIIE
RRQKIFMS
