ID A0A3Q2WBK9_HAPBU Unreviewed; 400 AA.
AC A0A3Q2WBK9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=E3 ubiquitin-protein ligase XIAP {ECO:0000256|ARBA:ARBA00044089};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Baculoviral IAP repeat-containing protein 4 {ECO:0000256|ARBA:ARBA00044214};
DE AltName: Full=RING-type E3 ubiquitin transferase XIAP {ECO:0000256|ARBA:ARBA00044244};
DE AltName: Full=X-linked inhibitor of apoptosis protein {ECO:0000256|ARBA:ARBA00044224};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000022561.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000022561.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000256|ARBA:ARBA00006672}.
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DR RefSeq; XP_005916554.1; XM_005916492.2.
DR AlphaFoldDB; A0A3Q2WBK9; -.
DR Ensembl; ENSHBUT00000013318.1; ENSHBUP00000022561.1; ENSHBUG00000002936.1.
DR GeneID; 102307482; -.
DR CTD; 331; -.
DR GeneTree; ENSGT00940000166874; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00022; BIR; 3.
DR CDD; cd16714; RING-HC_BIRC4_8; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10044:SF115; E3 UBIQUITIN-PROTEIN LIGASE XIAP; 1.
DR PANTHER; PTHR10044; INHIBITOR OF APOPTOSIS; 1.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57924; Inhibitor of apoptosis (IAP) repeat; 3.
DR PROSITE; PS01282; BIR_REPEAT_1; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 353..387
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 316..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 45239 MW; 2F4A76AEA0AF8F0E CRC64;
MCDLSQDGVW ESDNAPDFSS LTRRIDSFRG SNLANKVPAE TLAQAGFFYT GESDRVRCFS
CNMTVDNWYS GDRPVDKHKQ FSPSCTFLTC VHRTSFNQNS NTALISEEVG DVEYRLRTGE
VVDEAPYPIV PHMRNEEARL RTFSSWPNRT PVRPRDLAQA GFFYVGQSDK VQCFCCGGRL
NGWEPGDSAW SEHSKHYPNC YFILGHDVGN IPIQTGIEED ASNNRRAIDP ALMQNFEARR
ATFAGVRHPI DHERLARAGF YSTGRGDAVL CFHCSGGLNN WQPEEDPWVE HAKHYPGCSF
LLANKGPEFV NSIQLQRPQH DRAASSHQNP VSEDMEDEDP LEKLQRLQRE KQCKICMDRD
IAIVFIPCAH LVACENCSQA LNKCPICCQD ITQKIKTYIA
//
