API5_MOUSE
ID API5_MOUSE Reviewed; 504 AA.
AC O35841; Q3U517; Q922L2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Apoptosis inhibitor 5;
DE Short=API-5;
DE AltName: Full=AAC-11;
GN Name=Api5;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=9307294;
RA Tewari M., Yu M., Ross B., Dean C., Giordano A., Rubin R.;
RT "AAC-11, a novel cDNA that inhibits apoptosis after growth factor
RT withdrawal.";
RL Cancer Res. 57:4063-4069(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Placenta, and Thymus;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INDUCTION BY BAP.
RX PubMed=9918813; DOI=10.1006/bbrc.1998.9866;
RA Lu K.P., Ramos K.S.;
RT "Identification of genes differentially expressed in vascular smooth muscle
RT cells following benzo[a]pyrene challenge: implications for chemical
RT atherogenesis.";
RL Biochem. Biophys. Res. Commun. 253:828-833(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-469, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Antiapoptotic factor that may have a role in protein
CC assembly. Negatively regulates ACIN1. By binding to ACIN1, it
CC suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA
CC fragmentation. Also known to efficiently suppress E2F1-induced
CC apoptosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with FGF2 and ACIN1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Mainly nuclear.
CC -!- INDUCTION: Down-regulated in vascular smooth muscle cells (vSMCs)
CC treated with benzo[a]pyrene (BaP). {ECO:0000269|PubMed:9918813}.
CC -!- PTM: Acetylation at Lys-251 impairs antiapoptotic function.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the API5 family. {ECO:0000305}.
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DR EMBL; U35846; AAB86526.1; -; mRNA.
DR EMBL; AK137466; BAE23364.1; -; mRNA.
DR EMBL; AK153934; BAE32263.1; -; mRNA.
DR EMBL; AK167375; BAE39470.1; -; mRNA.
DR EMBL; AL672251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL27645.1; -; Genomic_DNA.
DR EMBL; BC007133; AAH07133.1; -; mRNA.
DR CCDS; CCDS16459.1; -.
DR RefSeq; NP_031492.2; NM_007466.3.
DR AlphaFoldDB; O35841; -.
DR SMR; O35841; -.
DR BioGRID; 198151; 13.
DR STRING; 10090.ENSMUSP00000028617; -.
DR GlyConnect; 2132; 1 N-Linked glycan (1 site).
DR GlyGen; O35841; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; O35841; -.
DR PhosphoSitePlus; O35841; -.
DR SwissPalm; O35841; -.
DR EPD; O35841; -.
DR jPOST; O35841; -.
DR MaxQB; O35841; -.
DR PaxDb; O35841; -.
DR PeptideAtlas; O35841; -.
DR PRIDE; O35841; -.
DR ProteomicsDB; 296373; -.
DR Antibodypedia; 13145; 292 antibodies from 33 providers.
DR DNASU; 11800; -.
DR Ensembl; ENSMUST00000028617; ENSMUSP00000028617; ENSMUSG00000027193.
DR GeneID; 11800; -.
DR KEGG; mmu:11800; -.
DR UCSC; uc008lgx.2; mouse.
DR CTD; 8539; -.
DR MGI; MGI:1888993; Api5.
DR VEuPathDB; HostDB:ENSMUSG00000027193; -.
DR eggNOG; KOG2213; Eukaryota.
DR GeneTree; ENSGT00390000010991; -.
DR HOGENOM; CLU_037809_1_0_1; -.
DR InParanoid; O35841; -.
DR OMA; FIQCATA; -.
DR PhylomeDB; O35841; -.
DR TreeFam; TF324283; -.
DR BioGRID-ORCS; 11800; 14 hits in 61 CRISPR screens.
DR ChiTaRS; Api5; mouse.
DR PRO; PR:O35841; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O35841; protein.
DR Bgee; ENSMUSG00000027193; Expressed in optic fissure and 254 other tissues.
DR Genevisible; O35841; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0044346; P:fibroblast apoptotic process; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IDA:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR008383; API5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR PANTHER; PTHR12758; PTHR12758; 1.
DR Pfam; PF05918; API5; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..504
FT /note="Apoptosis inhibitor 5"
FT /id="PRO_0000064635"
FT REGION 1..360
FT /note="ARM-like and Heat-like helical repeats"
FT /evidence="ECO:0000250"
FT REGION 370..391
FT /note="Leucine-zipper"
FT REGION 451..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 454..475
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 483..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZZ5"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZZ5"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZZ5"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 288
FT /note="K -> N (in Ref. 1; AAB86526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56785 MW; 11E4CC89509487B9 CRC64;
MPTVEELYRN YGILADATEQ VGQHKDAYQV ILDGVKGGTK EKRLAAQFIP KFFKHFPELA
DSAINAQLDL CEDEDVSIRR QAIKELPQFA TGENLPRVAD ILTQLLQTDD SAEFNLVNNA
LLSIFKMDAK GTLGGLFSQI LQGEDIVRER AIKFLSTKLK TLPDEVLTKE VEELILTESK
KVLEDVTGEE FVLFMKILSG LKSLQTVSGR QQLVELVAEQ ADLEQAFSPS DPDCVDRLLQ
CTRQAVPLFS KNVHSTRFVT YFCEQVLPNL STLTTPVEGL DIQLEVLKLL AEMSSFCGDM
EKLETNLRKL FDKLLEYMPL PPEEAENGEN AGNEEPKLQF SYVECLLYSF HQLGRKLPDF
LTAKLNAEKL KDFKIRLQYF ARGLQVYIRQ LRLALQGKTG EALKTEENKI KVVALKITNN
INVLIKDLFH IPPSYKSTVT LSWKPVQKVE IGQKRTSEDT SSGSPPKKSP GGPKRDARQI
YNPPSGKYSS NLSNFNYERS LQGK
