ID   ASZ1_RABIT              Reviewed;         475 AA.
AC   Q09YN0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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; Synonyms=GASZ;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA   Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA   Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA   Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA   Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA   Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA   Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA   Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA   Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA   Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 the regulation of retrotransposons.
CC       May act by mediating protein-protein interactions during germ cell
CC       maturation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DDX4, PIWIL1, RANBP9 and TDRD1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC       meiotic nuage, also named P granule, a germ-cell-specific organelle
CC       required to repress transposon activity during meiosis. Specifically
CC       localizes to pi-bodies, a subset of the nuage which contains primary
CC       piRNAs (By similarity). {ECO:0000250}.
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DR   EMBL; DP000006; AAY89017.1; -; Genomic_DNA.
DR   RefSeq; NP_001164490.1; NM_001171019.1.
DR   AlphaFoldDB; Q09YN0; -.
DR   SMR; Q09YN0; -.
DR   STRING; 9986.ENSOCUP00000013721; -.
DR   PRIDE; Q09YN0; -.
DR   Ensembl; ENSOCUT00000015964; ENSOCUP00000013721; ENSOCUG00000015962.
DR   GeneID; 100126561; -.
DR   KEGG; ocu:100126561; -.
DR   CTD; 136991; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00880000138051; -.
DR   HOGENOM; CLU_053259_0_0_1; -.
DR   InParanoid; Q09YN0; -.
DR   OMA; RHLLTMK; -.
DR   OrthoDB; 1428188at2759; -.
DR   TreeFam; TF352216; -.
DR   Proteomes; UP000001811; Chromosome 7.
DR   Bgee; ENSOCUG00000015962; Expressed in upper lobe of left lung and 3 other tissues.
DR   GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS: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   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   3: Inferred from homology;
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_0000260396"
FT   REPEAT          45..74
FT                   /note="ANK 1"
FT   REPEAT          78..107
FT                   /note="ANK 2"
FT   REPEAT          110..144
FT                   /note="ANK 3"
FT   REPEAT          148..177
FT                   /note="ANK 4"
FT   REPEAT          181..210
FT                   /note="ANK 5"
FT   REPEAT          214..243
FT                   /note="ANK 6"
FT   DOMAIN          272..334
FT                   /note="SAM"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VD46"
SQ   SEQUENCE   475 AA;  53041 MW;  C8DF35294E9A6C9C CRC64;
     MATGSLRGLA VAGGGESSDS EDDGWEIGYL DRPPQKLKGP LPIEEKNETF KKALTTGDTS
     LVKELLDSGI SVDSSFRYGW TPLMYAASVA NVELVRVLLD RGANASFDKD KQTILITACS
     ARGSEEQILK CVELLLSRNA DPNVACRRLM TPIMYAARDG HPQVVALLVA HGAEVNIQDE
     NGYTALTWAA RQGHKSVVLK LLELGANKTL QTKDGKTPSE IAKRNKHLEI FNLLSLTLNP
     LEGKLQQLTK EETICKLLTT DSDKEKDHIF SSYTAFGDLE IFLHGLGLEH MTDLLKERDI
     TLRHLLTMRK DEFTQNGITS KDQQKILAAL KELEVEEIKF GELPEVAKLE ISGDEFLNFL
     LKLNKQCGHL ITAVQNIITE LPVNSHKIVL EWASPRNFTS VCEELVSNVE DLNEEVCKLK
     DLIQKLQNER ENDPTHIPLM EEVSTWNSKI LKRTAVTVCG FGFLLFICKL TFQRK