XAF1_MOUSE
ID XAF1_MOUSE Reviewed; 273 AA.
AC Q5NBU8; B7ZD14; Q3USK3; Q5NBU6; Q5NBU7; Q5NBU9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=XIAP-associated factor 1;
DE AltName: Full=BIRC4-binding protein;
GN Name=Xaf1; Synonyms=Birc4bp, Xiapaf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-205 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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=Q5NBU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5NBU8-3; Sequence=VSP_039715;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE24328.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=CAI36034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL929071; CAI36033.2; -; Genomic_DNA.
DR EMBL; AL929071; CAI36034.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL929071; CAX15644.1; -; Genomic_DNA.
DR EMBL; AK140315; BAE24328.1; ALT_SEQ; mRNA.
DR CCDS; CCDS24984.2; -. [Q5NBU8-1]
DR CCDS; CCDS70236.1; -. [Q5NBU8-3]
DR RefSeq; NP_001032802.2; NM_001037713.4. [Q5NBU8-1]
DR RefSeq; NP_001278082.1; NM_001291153.1. [Q5NBU8-3]
DR AlphaFoldDB; Q5NBU8; -.
DR STRING; 10090.ENSMUSP00000123011; -.
DR iPTMnet; Q5NBU8; -.
DR PhosphoSitePlus; Q5NBU8; -.
DR EPD; Q5NBU8; -.
DR MaxQB; Q5NBU8; -.
DR PaxDb; Q5NBU8; -.
DR PeptideAtlas; Q5NBU8; -.
DR PRIDE; Q5NBU8; -.
DR ProteomicsDB; 297861; -. [Q5NBU8-1]
DR ProteomicsDB; 297862; -. [Q5NBU8-3]
DR Antibodypedia; 23838; 252 antibodies from 31 providers.
DR DNASU; 327959; -.
DR Ensembl; ENSMUST00000140842; ENSMUSP00000121472; ENSMUSG00000040483. [Q5NBU8-3]
DR Ensembl; ENSMUST00000146233; ENSMUSP00000123011; ENSMUSG00000040483. [Q5NBU8-1]
DR GeneID; 327959; -.
DR KEGG; mmu:327959; -.
DR UCSC; uc007jyr.2; mouse. [Q5NBU8-1]
DR UCSC; uc056ymf.1; mouse. [Q5NBU8-3]
DR CTD; 54739; -.
DR MGI; MGI:3772572; Xaf1.
DR VEuPathDB; HostDB:ENSMUSG00000040483; -.
DR eggNOG; ENOG502QQRU; Eukaryota.
DR GeneTree; ENSGT00530000063869; -.
DR HOGENOM; CLU_066148_0_0_1; -.
DR InParanoid; Q5NBU8; -.
DR OMA; AQHREVC; -.
DR OrthoDB; 1113262at2759; -.
DR PhylomeDB; Q5NBU8; -.
DR TreeFam; TF331416; -.
DR BioGRID-ORCS; 327959; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q5NBU8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NBU8; protein.
DR Bgee; ENSMUSG00000040483; Expressed in small intestine Peyer's patch and 161 other tissues.
DR ExpressionAtlas; Q5NBU8; baseline and differential.
DR Genevisible; Q5NBU8; MM.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0035456; P:response to interferon-beta; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 2.
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 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Metal-binding; Mitochondrion;
KW Nucleus; Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..273
FT /note="XIAP-associated factor 1"
FT /id="PRO_0000329029"
FT ZN_FING 22..80
FT /note="TRAF-type"
FT REGION 181..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 57..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039715"
SQ SEQUENCE 273 AA; 31117 MW; 89D504585DACEFCA CRC64;
MEADFQVCRN CKRNVASLHF MLHEAHCLRF IVLCPECEEP IPESKMKEHM EVVHQQTKES
QQHPAKCKFC ELAVQLSNLD VHESHCGSRT EHCPHCNQPI TLQVLSQHKA MCLSAKGRPE
EGKRIVSSPG RKTRCDLCKQ MIPENTYASH MKQCSAPNTV TRIRDESIIV IPSTLAFMDS
GNRRSTVSKD VRPKTKNRNS STKRETKKQN GTVALPLKSG LQQRADLPTG DETAYDTLQN
CCQCRILLPL PILNEHQEKC QRLAHQKKLQ WGW
