ASZ1_MOUSE
ID ASZ1_MOUSE Reviewed; 475 AA.
AC Q8VD46; G3X8S0; Q6PD92; Q9JKQ7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1;
DE AltName: Full=Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein;
GN Name=Asz1 {ECO:0000312|MGI:MGI:1921318};
GN Synonyms=Gasz {ECO:0000312|EMBL:AAL67487.1};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv {ECO:0000269|PubMed:12040005};
RC TISSUE=Ovary {ECO:0000269|PubMed:12040005}, and
RC Testis {ECO:0000269|PubMed:12040005};
RX PubMed=12040005; DOI=10.1210/mend.16.6.0864;
RA Yan W., Rajkovic A., Viveiros M.M., Burns K.H., Eppig J.J., Matzuk M.M.;
RT "Identification of Gasz, an evolutionarily conserved gene expressed
RT exclusively in germ cells and encoding a protein with four ankyrin repeats,
RT a sterile-alpha motif, and a basic leucine zipper.";
RL Mol. Endocrinol. 16:1168-1184(2002).
RN [2] {ECO:0000312|EMBL:AAF30297.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10655503; DOI=10.1073/pnas.97.3.1172;
RA Ellsworth R.E., Jamison D.C., Touchman J.W., Chissoe S.L.,
RA Braden Maduro V.V., Bouffard G.G., Dietrich N.L., Beckstrom-Sternberg S.M.,
RA Iyer L.M., Weintraub L.A., Cotton M., Courtney L., Edwards J., Maupin R.,
RA Ozersky P., Rohlfing T., Wohldmann P., Miner T., Kemp K., Kramer J.,
RA Korf I., Pepin K., Antonacci-Fulton L., Fulton R.S., Minx P., Hillier L.W.,
RA Wilson R.K., Waterston R.H., Miller W., Green E.D.;
RT "Comparative genomic sequence analysis of the human and mouse cystic
RT fibrosis transmembrane conductance regulator genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1172-1177(2000).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP DDX4; PIWIL1; RANBP9 AND TDRD1.
RX PubMed=19730684; DOI=10.1371/journal.pgen.1000635;
RA Ma L., Buchold G.M., Greenbaum M.P., Roy A., Burns K.H., Zhu H., Han D.Y.,
RA Harris R.A., Coarfa C., Gunaratne P.H., Yan W., Matzuk M.M.;
RT "GASZ is essential for male meiosis and suppression of retrotransposon
RT expression in the male germline.";
RL PLoS Genet. 5:E1000635-E1000635(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-18 AND SER-20, AND
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).
CC -!- FUNCTION: Plays a central role during spermatogenesis by repressing
CC transposable elements and preventing their mobilization, which is
CC essential for the germline integrity. Acts via the piRNA metabolic
CC process, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC governs the methylation and subsequent repression of transposons. Its
CC association with pi-bodies suggests a participation in the primary
CC piRNAs metabolic process. Required prior to the pachytene stage to
CC facilitate the production of multiple types of piRNAs, including those
CC associated with repeats involved in regulation of retrotransposons. May
CC act by mediating protein-protein interactions during germ cell
CC maturation. {ECO:0000269|PubMed:19730684}.
CC -!- SUBUNIT: Interacts with DDX4, PIWIL1, RANBP9 and TDRD1.
CC {ECO:0000269|PubMed:19730684}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12040005,
CC ECO:0000269|PubMed:19730684}. Note=Component of the meiotic nuage, also
CC named P granule, a germ-cell-specific organelle required to repress
CC transposon activity during meiosis. Specifically localizes to pi-
CC bodies, a subset of the nuage which contains primary piRNAs.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in testis and ovary with
CC higher levels in testis. {ECO:0000269|PubMed:12040005}.
CC -!- DEVELOPMENTAL STAGE: Expressed in pachytene spermatocytes and early
CC spermatids in the developing and adult testes and in oocytes in all
CC stages of oogenesis in the ovary. Also expressed in preimplantive
CC embryos. {ECO:0000269|PubMed:12040005}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but show profound defect in male
CC meiosis leading to male sterility. Testes display increased
CC hypomethylation of retrotransposons and their subsequent expression as
CC well as piRNAs suppression. {ECO:0000269|PubMed:19730684}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF30297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF459789; AAL67487.1; -; mRNA.
DR EMBL; AF162137; AAF30297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC068561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466533; EDL13867.1; -; Genomic_DNA.
DR EMBL; BC058859; AAH58859.1; -; mRNA.
DR CCDS; CCDS19929.1; -.
DR RefSeq; NP_076218.3; NM_023729.3.
DR AlphaFoldDB; Q8VD46; -.
DR SMR; Q8VD46; -.
DR STRING; 10090.ENSMUSP00000010940; -.
DR iPTMnet; Q8VD46; -.
DR PhosphoSitePlus; Q8VD46; -.
DR MaxQB; Q8VD46; -.
DR PaxDb; Q8VD46; -.
DR PRIDE; Q8VD46; -.
DR ProteomicsDB; 281925; -.
DR Antibodypedia; 17481; 154 antibodies from 25 providers.
DR DNASU; 74068; -.
DR Ensembl; ENSMUST00000010940; ENSMUSP00000010940; ENSMUSG00000010796.
DR GeneID; 74068; -.
DR KEGG; mmu:74068; -.
DR UCSC; uc009bah.2; mouse.
DR CTD; 136991; -.
DR MGI; MGI:1921318; Asz1.
DR VEuPathDB; HostDB:ENSMUSG00000010796; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00880000138051; -.
DR HOGENOM; CLU_053259_0_0_1; -.
DR InParanoid; Q8VD46; -.
DR OMA; RHLLTMK; -.
DR OrthoDB; 1428188at2759; -.
DR PhylomeDB; Q8VD46; -.
DR TreeFam; TF352216; -.
DR BioGRID-ORCS; 74068; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Asz1; mouse.
DR PRO; PR:Q8VD46; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VD46; protein.
DR Bgee; ENSMUSG00000010796; Expressed in spermatocyte and 45 other tissues.
DR ExpressionAtlas; Q8VD46; baseline and differential.
DR Genevisible; Q8VD46; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0071546; C:pi-body; IDA:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007281; P:germ cell development; NAS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR CDD; cd09521; SAM_ASZ1; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042650; Asz1_SAM.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Developmental protein; Differentiation; Meiosis;
KW Phosphoprotein; Reference proteome; Repeat; RNA-mediated gene silencing;
KW Spermatogenesis.
FT CHAIN 1..475
FT /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT containing protein 1"
FT /id="PRO_0000066970"
FT REPEAT 45..74
FT /note="ANK 1"
FT /evidence="ECO:0000305"
FT REPEAT 78..107
FT /note="ANK 2"
FT /evidence="ECO:0000305"
FT REPEAT 110..144
FT /note="ANK 3"
FT /evidence="ECO:0000305"
FT REPEAT 148..177
FT /note="ANK 4"
FT /evidence="ECO:0000305"
FT REPEAT 181..210
FT /note="ANK 5"
FT /evidence="ECO:0000305"
FT REPEAT 214..243
FT /note="ANK 6"
FT /evidence="ECO:0000305"
FT DOMAIN 272..334
FT /note="SAM"
FT /evidence="ECO:0000305"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 47
FT /note="N -> T (in Ref. 1; AAL67487)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="T -> A (in Ref. 5; AAH58859)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="S -> R (in Ref. 2; AAF30297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52984 MW; 8B3BA5F357B26732 CRC64;
MAAGTLRGLA VAGGGESSDS EDDGWDIGYL DRSSQKLKRS LPVEEKNETF KKALTTGDIS
LVKELLDSGI NVDSSFRYGW TPLMYAASVA NAELVRFLLD RGANASFDKD KLTILISACS
ARGSEEQVLK CVELLLSRNA DPNTACRRLM TPIMYAARDG HTQVVALLVA HGAEVNAQDE
NGYTALTWAA RQGHKNVILK LLELGANKML QTKDGRTPSE IAKRNKHLEI FNFLSLTLNP
LEGKLQQLTK EETICKLLAT DSDKEKDHIF SPYTAFGDLE IFLHGLGLEH MTDSLKEKDI
TLRHLLTMKK DELTKNGIAS KDQQKILAAL KELEVEEINF GKLPEVTKLE ISGDEFLNFL
LKLNKQCGHL ITAVQNIITE LPVNSHKIVL EWASPRNFTS VCEELVSNVE DLNEEVCRLK
ELIQKMQNER ENDPTHIPLV EEVSTWKTRI LKRSAVTVCG FGLLLFIGKL TLQRK
