MOAP1_MOUSE
ID MOAP1_MOUSE Reviewed; 352 AA.
AC Q9ERH6;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Modulator of apoptosis 1 {ECO:0000303|PubMed:11060313};
DE Short=MAP-1 {ECO:0000303|PubMed:11060313};
DE Short=MmMOAP1 {ECO:0000303|PubMed:34413232};
GN Name=Moap1 {ECO:0000303|PubMed:34413232, ECO:0000312|MGI:MGI:1915555};
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 TISSUE=Brain;
RX PubMed=11060313; DOI=10.1074/jbc.m008955200;
RA Tan K.O., Tan K.M.L., Chan S.-L., Yee K.S.Y., Bevort M., Ang K.C., Yu V.C.;
RT "MAP-1, a novel proapoptotic protein containing a BH3-like motif that
RT associates with Bax through its Bcl-2 homology domains.";
RL J. Biol. Chem. 276:2802-2807(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic, and Kidney;
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 [4]
RP INTERACTION WITH RASSF6.
RX PubMed=17404571; DOI=10.1038/sj.onc.1210440;
RA Allen N.P., Donninger H., Vos M.D., Eckfeld K., Hesson L., Gordon L.,
RA Birrer M.J., Latif F., Clark G.J.;
RT "RASSF6 is a novel member of the RASSF family of tumor suppressors.";
RL Oncogene 26:6203-6211(2007).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=19366867; DOI=10.1093/cercor/bhp062;
RA Takaji M., Komatsu Y., Watakabe A., Hashikawa T., Yamamori T.;
RT "Paraneoplastic antigen-like 5 gene (PNMA5) is preferentially expressed in
RT the association areas in a primate specific manner.";
RL Cereb. Cortex 19:2865-2879(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [7]
RP FUNCTION.
RX PubMed=33783314; DOI=10.1080/15548627.2021.1896157;
RA Chang H.C., Tao R.N., Tan C.T., Wu Y.J., Bay B.H., Yu V.C.;
RT "The BAX-binding protein MOAP1 associates with LC3 and promotes closure of
RT the phagophore.";
RL Autophagy 17:3725-3739(2021).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=34413232; DOI=10.1126/science.abg6155;
RA Segel M., Lash B., Song J., Ladha A., Liu C.C., Jin X., Mekhedov S.L.,
RA Macrae R.K., Koonin E.V., Zhang F.;
RT "Mammalian retrovirus-like protein PEG10 packages its own mRNA and can be
RT pseudotyped for mRNA delivery.";
RL Science 373:882-889(2021).
CC -!- FUNCTION: Retrotransposon-derived protein that forms virion-like
CC capsids (PubMed:34413232). Acts as an effector of BAX during apoptosis:
CC enriched at outer mitochondria membrane and associates with BAX upon
CC induction of apoptosis, facilitating BAX-dependent mitochondrial outer
CC membrane permeabilization and apoptosis (By similarity). Required for
CC death receptor-dependent apoptosis (By similarity). When associated
CC with RASSF1, promotes BAX conformational change and translocation to
CC mitochondrial membranes in response to TNF and TNFSF10 stimulation (By
CC similarity). Also promotes autophagy: promotes phagophore closure via
CC association with ATG8 proteins (PubMed:33783314). Acts as an inhibitor
CC of the NFE2L2/NRF2 pathway via interaction with SQSTM1: interaction
CC promotes dissociation of SQSTM1 inclusion bodies that sequester KEAP1,
CC relieving inactivation of the BCR(KEAP1) complex (By similarity).
CC {ECO:0000250|UniProtKB:Q96BY2, ECO:0000269|PubMed:33783314,
CC ECO:0000269|PubMed:34413232}.
CC -!- SUBUNIT: Homodimer. Under normal circumstances, held in an inactive
CC conformation by an intramolecular interaction. Interacts with BAX.
CC Binding to RASSF1 isoform A (RASSF1A) relieves this inhibitory
CC interaction and allows further binding to BAX. Binds also to BCL2 and
CC BCLX. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to
CC their respective cognate ligand, after internalization. Interacts with
CC TRIM39 (By similarity). Interacts with RASSF6 (PubMed:17404571).
CC Interacts with ATG8 proteins MAP1LC3A, MAP1LC3B and MAP1LC3C (By
CC similarity). Does not interact with ATG8 proteins GABARAPL1, GABARAPL2
CC and GABARAP (By similarity). Interacts with SQSTM1; promoting
CC dissociation of SQSTM1 inclusion bodies that sequester KEAP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q96BY2,
CC ECO:0000269|PubMed:17404571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96BY2}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96BY2}. Extracellular vesicle membrane
CC {ECO:0000269|PubMed:34413232}. Note=Forms virion-like extracellular
CC vesicles that are released from cells. {ECO:0000269|PubMed:34413232}.
CC -!- TISSUE SPECIFICITY: Widely expressed, including in the brain. High
CC expression levels in testis. {ECO:0000269|PubMed:19366867}.
CC -!- DOMAIN: The protein is evolutionarily related to retrotransposon Gag
CC proteins: it contains the capsid (CA)subdomain of gag.
CC {ECO:0000269|PubMed:34413232}.
CC -!- DOMAIN: The BH3-like domain is required for association with BAX and
CC for mediating apoptosis. The three BH domains (BH1, BH2, and BH3) of
CC BAX are all required for mediating protein-protein interaction.
CC {ECO:0000250|UniProtKB:Q96BY2}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with the ATG8 family proteins MAP1LC3A, MAP1LC3B and
CC MAP1LC3C. {ECO:0000250|UniProtKB:Q96BY2}.
CC -!- PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this
CC modification is inhibited by TRIM39. {ECO:0000250|UniProtKB:Q96BY2}.
CC -!- SIMILARITY: Belongs to the PNMA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF305551; AAG31787.1; -; mRNA.
DR EMBL; AK019599; BAB31810.1; -; mRNA.
DR EMBL; BC014715; AAH14715.1; -; mRNA.
DR EMBL; BC055374; AAH55374.1; -; mRNA.
DR CCDS; CCDS26122.1; -.
DR RefSeq; NP_001136409.1; NM_001142937.2.
DR RefSeq; NP_071718.1; NM_022323.7.
DR AlphaFoldDB; Q9ERH6; -.
DR SMR; Q9ERH6; -.
DR STRING; 10090.ENSMUSP00000133459; -.
DR iPTMnet; Q9ERH6; -.
DR PhosphoSitePlus; Q9ERH6; -.
DR MaxQB; Q9ERH6; -.
DR PaxDb; Q9ERH6; -.
DR PeptideAtlas; Q9ERH6; -.
DR PRIDE; Q9ERH6; -.
DR ProteomicsDB; 295574; -.
DR Antibodypedia; 22; 319 antibodies from 32 providers.
DR DNASU; 64113; -.
DR Ensembl; ENSMUST00000173760; ENSMUSP00000133459; ENSMUSG00000096458.
DR Ensembl; ENSMUST00000178384; ENSMUSP00000137010; ENSMUSG00000096458.
DR GeneID; 64113; -.
DR KEGG; mmu:64113; -.
DR UCSC; uc011yqo.2; mouse.
DR CTD; 64112; -.
DR MGI; MGI:1915555; Moap1.
DR VEuPathDB; HostDB:ENSMUSG00000096458; -.
DR eggNOG; ENOG502SAVD; Eukaryota.
DR GeneTree; ENSGT01030000234522; -.
DR HOGENOM; CLU_014694_0_0_1; -.
DR InParanoid; Q9ERH6; -.
DR OMA; GMIPEIR; -.
DR OrthoDB; 820525at2759; -.
DR PhylomeDB; Q9ERH6; -.
DR TreeFam; TF335054; -.
DR BioGRID-ORCS; 64113; 2 hits in 37 CRISPR screens.
DR ChiTaRS; Gm20604; mouse.
DR PRO; PR:Q9ERH6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9ERH6; protein.
DR Bgee; ENSMUSG00000096458; Expressed in spermatocyte and 73 other tissues.
DR Genevisible; Q9ERH6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR InterPro; IPR026523; PNMA.
DR PANTHER; PTHR23095; PTHR23095; 1.
DR Pfam; PF14893; PNMA; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Autophagy; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..352
FT /note="Modulator of apoptosis 1"
FT /id="PRO_0000155207"
FT REGION 120..127
FT /note="BH3-like"
FT /evidence="ECO:0000303|PubMed:11060313"
FT REGION 204..207
FT /note="RASSF1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q96BY2"
FT MOTIF 49..52
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:Q96BY2"
FT CONFLICT 57
FT /note="R -> K (in Ref. 3; AAH55374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39404 MW; 8F4630D080495D98 CRC64;
MTLRLLEDWC RGMDMNPRKA LLVAGIPPTC GVADIEEALQ AGLAPLGEHR LLGRMFRRDE
NKNVALIGLT VETGSALVPK EIPAKGGVWR VIFKPPDTDS DFLCRLNEFL KGEGMTMGEL
TRVLGNRNDP LGLDPGIMIP EIRAPMLAQA LNEALKPTLQ YLRYKKLSVF SGRDPPGPGE
EEFESWMFHT SQVMKTWQVS DVEKRRRLIE SLRGPAFEII RVLKINNPFI TVAECLKTLE
TIFGIIDNPR ALQVKYLTTY QKTDEKLSAY VLRLEPLLQK LVQKGAIEKE VVNQARLDQV
IAGAVHKSVR RELGLPEGSP APGLLQLLTL IKDKEAEEEE VLLQAELEGY CT
