ID   XAF1_BOVIN              Reviewed;         297 AA.
AC   Q58DH1; Q05B53;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=XIAP-associated factor 1;
GN   Name=XAF1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Seems to function as a negative regulator of members of the
CC       IAP (inhibitor of apoptosis protein) family. Inhibits anti-caspase
CC       activity of BIRC4. Induces cleavage and inactivation of BIRC4
CC       independent of caspase activation. Mediates TNF-alpha-induced apoptosis
CC       and is involved in apoptosis in trophoblast cells. May inhibit BIRC4
CC       indirectly by activating the mitochondrial apoptosis pathway. After
CC       translocation to mitochondria, promotes translocation of BAX to
CC       mitochondria and cytochrome c release from mitochondria. Seems to
CC       promote the redistribution of BIRC4 from the cytoplasm to the nucleus,
CC       probably independent of BIRC4 inactivation which seems to occur in the
CC       cytoplasm. The BIRC4-XAF1 complex mediates down-regulation of
CC       BIRC5/survivin; the process requires the E3 ligase activity of BIRC4.
CC       Seems to be involved in cellular sensitivity to the proapoptotic
CC       actions of TRAIL. May be a tumor suppressor by mediating apoptosis
CC       resistance of cancer cells (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with BIRC1, BIRC2, BIRC3, BIRC4, BIRC7 and BIRC8.
CC       Part of an complex consisting of BIRC4, XAF1 and BIRC5; the complex
CC       formation requires IFN-beta stimulation. Interacts with RNF114, the
CC       interaction increases XAF1 stability and proapoptotic effects, and may
CC       regulate IFN signaling (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Mitochondrion {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q58DH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q58DH1-2; Sequence=VSP_032917;
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DR   EMBL; BT021626; AAX46473.1; -; mRNA.
DR   EMBL; BC122801; AAI22802.1; -; mRNA.
DR   RefSeq; NP_001030247.1; NM_001035075.1. [Q58DH1-2]
DR   RefSeq; XP_005220269.1; XM_005220212.2.
DR   AlphaFoldDB; Q58DH1; -.
DR   STRING; 9913.ENSBTAP00000015077; -.
DR   PaxDb; Q58DH1; -.
DR   PRIDE; Q58DH1; -.
DR   GeneID; 509740; -.
DR   KEGG; bta:509740; -.
DR   CTD; 54739; -.
DR   eggNOG; ENOG502QQRU; Eukaryota.
DR   HOGENOM; CLU_066148_0_0_1; -.
DR   InParanoid; Q58DH1; -.
DR   OrthoDB; 1113262at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR031220; XAF1.
DR   InterPro; IPR041386; XAF1_C.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR16295:SF17; PTHR16295:SF17; 1.
DR   Pfam; PF18608; XAF1_C; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Metal-binding; Mitochondrion;
KW   Nucleus; Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT   CHAIN           1..297
FT                   /note="XIAP-associated factor 1"
FT                   /id="PRO_0000329027"
FT   ZN_FING         22..99
FT                   /note="TRAF-type"
FT   REGION          178..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         284..297
FT                   /note="EKCRRLASSKGKQV -> RCWFAQELQLNQEEKRTPTLLPENSDQASRPNPA
FT                   WTPWEIQLYL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16305752"
FT                   /id="VSP_032917"
FT   CONFLICT        26
FT                   /note="H -> Y (in Ref. 2; AAI22802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="D -> E (in Ref. 2; AAI22802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="E -> K (in Ref. 2; AAI22802)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   297 AA;  33687 MW;  ED4CE8AFB28A22E5 CRC64;
     MEGALQVCRN CKRRVASNHL GLHEAHCLMY LVLCPECKEP VLQHEMEEHC QGGHQQVGCA
     MCQQSVPKHS LDSHEAQECQ ERPVECQFCQ LAVRLNKVDL HEHHCGQQTE LCPDCGQHVM
     LRVLARHREE CQREQLRLQK GKSIPVPESN ICCHYCNQMI PGNKYFHHLD RCRRVSGAVT
     PSPVGKPEIP PSSPLSWAAE DQTSKAEKDV RPKLKNRHRA PFLSEKSTRQ APRGTNKTTN
     LSLKSNGKLR ASSPVEDETA YDILRRCSQC DILLPLPTLN HHQEKCRRLA SSKGKQV