ASZ1_NOTEU
ID ASZ1_NOTEU Reviewed; 475 AA.
AC A4D7T3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 48.
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 Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX NCBI_TaxID=9315;
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 (AUG-2005) 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; DP000012; ABA02587.1; -; Genomic_DNA.
DR AlphaFoldDB; A4D7T3; -.
DR SMR; A4D7T3; -.
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; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07647; SAM_2; 1.
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.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ANK repeat; Cytoplasm; Developmental protein; Differentiation; Meiosis;
KW Phosphoprotein; Repeat; RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..475
FT /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT containing protein 1"
FT /id="PRO_0000295861"
FT REPEAT 44..73
FT /note="ANK 1"
FT REPEAT 77..106
FT /note="ANK 2"
FT REPEAT 109..146
FT /note="ANK 3"
FT REPEAT 147..176
FT /note="ANK 4"
FT REPEAT 180..209
FT /note="ANK 5"
FT REPEAT 213..242
FT /note="ANK 6"
FT DOMAIN 273..336
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
SQ SEQUENCE 475 AA; 52936 MW; AAD60024A92A74C5 CRC64;
MAGSLGNLVV AGGGESSDSE EDYWDIGYMD RPPQTTKGSL ATEERDETFK KALTSGDVSL
VEELLNSGMS VESSFQFGWT PLMCAVNIAN VELVRILLDR GANASFDKDQ YTILMAACAA
HASESQILKT VELLLSRNAN PNVACRKCMT PVMYAAREGH AQVVALLVAH GAEINAQDEN
GYTALTWAAR HGHKSVVLKL LELGANKTIQ TKDGKTAGEI AKRNKHPELF TLLSLTVNPL
QGKLQHLTKE EAICRLLTTD GDAGKEHKFS SYTAFGDLEV FLHGLGLEHM TELLKERDIT
LRQLLTMRKE DFTENGITNI RDQQKILDAV KELQVEEIKF GELTEVINLE ISSDEFLNFL
LKLNKQCGHL TTAVQNIINQ LPVNSHKIVL EWGSSQRFTS VCENLVCNVE DLGEEVCKLK
DLIQKLQNDQ KNDPCRVLPM ETYSTWNSRF LKRATFTVCG FGFLLFIFKL TFRKS
