ASZ1_MUNMU
ID ASZ1_MUNMU Reviewed; 474 AA.
AC Q09YJ5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 50.
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 Muntiacus muntjak (Barking deer) (Indian muntjac).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Muntiacinae; Muntiacus.
OX NCBI_TaxID=9888;
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; DP000178; ABI75285.1; -; Genomic_DNA.
DR AlphaFoldDB; Q09YJ5; -.
DR SMR; Q09YJ5; -.
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 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..474
FT /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT containing protein 1"
FT /id="PRO_0000260392"
FT REPEAT 44..73
FT /note="ANK 1"
FT REPEAT 77..106
FT /note="ANK 2"
FT REPEAT 109..143
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 271..333
FT /note="SAM"
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 474 AA; 53059 MW; FF7479380B6FD432 CRC64;
MAAPLRALAV AGGGESSESE DDGWEIGYLD RTAQKLKGPL PVEERQETFK KALTTGNISL
VEELLDSGIS VNTSFQYGWT SLMYAASVSN VQLVRVLLDR GANASFDKDK QTVLITACSA
RGSEEKILKC VELLLSRNAD PNVACRRLMT PIMYAARDGH PQVVALLVAH GAEVNTQDEN
GYTALTWAAR QGHKNVVLKL LELGANKMIQ TKDGKTPSEI AKRNKHLEIF SLLSLTLNSL
EGKFHQLTKE ESICKLLRTD SDKEKDHLFS SYTAFGDLEL FLHGLGLEHM TDLLKEREIT
LRHLLTMRKD ELAKNGITSR DQQKIMAALK ELEVEEIKFG ELPEVAKLEI SGDEFLNFLL
KLNKQCGHLI AAVQNIITEL PVNSHKIVLE WASPRNFTSV CEELVSNVED LSEEVCKLKD
LIQKLQNERE NDPTHIPLME EVSTWNSRIL KRTAITVCGF GFLLFICKLT FQRK
