ID   ASZ1_DASNO              Reviewed;         476 AA.
AC   Q07E43;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 55.
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   Dasypus novemcinctus (Nine-banded armadillo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus.
OX   NCBI_TaxID=9361;
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}.
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; DP000181; ABI93633.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07E43; -.
DR   SMR; Q07E43; -.
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; -; 2.
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; Repeat; RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN           1..476
FT                   /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT                   containing protein 1"
FT                   /id="PRO_0000260389"
FT   REPEAT          46..75
FT                   /note="ANK 1"
FT   REPEAT          79..108
FT                   /note="ANK 2"
FT   REPEAT          111..145
FT                   /note="ANK 3"
FT   REPEAT          149..178
FT                   /note="ANK 4"
FT   REPEAT          182..211
FT                   /note="ANK 5"
FT   REPEAT          215..244
FT                   /note="ANK 6"
FT   DOMAIN          273..335
FT                   /note="SAM"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VD46"
SQ   SEQUENCE   476 AA;  53158 MW;  6A3E3374D26408E7 CRC64;
     MAAAVGLRGL AVAGGGESTD SEDDGWEIGY LDRASQKLTG LLPTEEKNET FKKALTTGDI
     SLVEELLDSG ISIDSSFRYG WTPLMYAASV ANVELVRVLL DRGANASFDK DKQTILITAC
     SARGSEEQIL KCVELLLSRN ADPNVACRRL MTPVMYAARA GHPQVVAVLV AYGAEVNTQD
     ENGYTALTWA ARQGHKNVIL KLLELGADKM LQTKDGKTPS EIAKRNKHLE IFNFLSLSLN
     PLEGKLQQLT KEETICKLLT TVSDKEKDHI FSSYAAFEDL EIFLHGLGLE HMTDLLKERD
     ITLRHLLTMR KDEFTKNGIT SRDQQKILAA LKELEVEEIK FGELPEVAKL EISGDEFLNF
     LLKLNKQCGH LITAVQNIIT ELPVNSHKIV LEWASPQNFT SVCEELVSNV EDLSEEVCKL
     KDLIQKLQNE RENDPTHIPS MDEVSSWNNR ILKRTAFTVC GFGFLLFICK LTFQRK