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Database: UniProt
Entry: A0A2K6CST8_MACNE
LinkDB: A0A2K6CST8_MACNE
Original site: A0A2K6CST8_MACNE 
ID   A0A2K6CST8_MACNE        Unreviewed;       497 AA.
AC   A0A2K6CST8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=XIAP {ECO:0000313|Ensembl:ENSMNEP00000026682.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000026682.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000026682.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the IAP family. {ECO:0000256|ARBA:ARBA00006672}.
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DR   RefSeq; XP_011716890.1; XM_011718588.1.
DR   RefSeq; XP_011716891.1; XM_011718589.1.
DR   RefSeq; XP_011716892.1; XM_011718590.1.
DR   RefSeq; XP_011716893.1; XM_011718591.1.
DR   AlphaFoldDB; A0A2K6CST8; -.
DR   STRING; 9545.ENSMNEP00000026682; -.
DR   Ensembl; ENSMNET00000050968.1; ENSMNEP00000026682.1; ENSMNEG00000036769.1.
DR   GeneID; 105468434; -.
DR   KEGG; mni:105468434; -.
DR   CTD; 331; -.
DR   GeneTree; ENSGT00940000158743; -.
DR   OMA; VKCYFCE; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000036769; Expressed in colon and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0061135; F:endopeptidase regulator activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0120283; F:protein serine/threonine kinase binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR   GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0070427; P:nucleotide-binding oligomerization domain containing 1 signaling pathway; IEA:Ensembl.
DR   GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:1902530; P:positive regulation of protein linear polyubiquitination; IEA:Ensembl.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:Ensembl.
DR   CDD; cd00022; BIR; 3.
DR   CDD; cd16714; RING-HC_BIRC4_8; 1.
DR   CDD; cd14395; UBA_BIRC4_8; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001370; BIR_rpt.
DR   InterPro; IPR048875; BIRC2-3-like_UBA.
DR   InterPro; IPR042579; XIAP/BIRC8_UBA.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10044:SF139; DEATH-ASSOCIATED INHIBITOR OF APOPTOSIS 2; 1.
DR   PANTHER; PTHR10044; INHIBITOR OF APOPTOSIS; 1.
DR   Pfam; PF00653; BIR; 3.
DR   Pfam; PF21290; BIRC2-3-like_UBA; 1.
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; 2.
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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          450..484
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   497 AA;  56671 MW;  6063A6CE47A05724 CRC64;
     MTFNSFEGSK TCVPADINKE EEFVEEFNRL KTFADFPSSS PVSASTLARA GFLYTGEGDT
     VRCFSCHAAV DRWQYGDSAV GRHRKVSPNC RFINGFYFEN SATQSTNSGI QNGQYKVENY
     LGSRNHFALD RPSETHADYL LRTGQVVDIS DTIYPRNPAM YSEEARLKSF QNWPDYAHLT
     PRELASAGLY YTGIGDQVQC FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNLNIRSE
     SDAVSSDRNF PNSTNLPRNP SMADYEARII TFGTWIYSVN KEQLARAGFY ALGEGDKVKC
     FHCGGGLTDW KPSEDPWEQH AKWYPGCKYL LEQKGQEYVN NIHLTHSLEE CLVRTTEKTP
     SLTRRIDDTI FQNPMVQEAI RMGFSFKDIK KIMEEKIQIS GSNYKSLEVL VADLVNAQKD
     STQDESSQTS LQKEISTEEQ LRRLQEEKLC KICMDRNIAI VFVPCGHLVT CKQCAEAVDK
     CPMCYTVITF KQKIFMS
//
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