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ASZ1_ORNAN
ID   ASZ1_ORNAN              Reviewed;         474 AA.
AC   Q07DZ7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
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   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258;
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; DP000185; ABI93679.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07DZ7; -.
DR   SMR; Q07DZ7; -.
DR   STRING; 9258.ENSOANP00000030233; -.
DR   Ensembl; ENSOANT00000039557; ENSOANP00000030318; ENSOANG00000031342.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00880000138051; -.
DR   InParanoid; Q07DZ7; -.
DR   Proteomes; UP000002279; Chromosome 10.
DR   Bgee; ENSOANG00000031342; Expressed in testis and 5 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; PF00536; SAM_1; 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.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
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..474
FT                   /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT                   containing protein 1"
FT                   /id="PRO_0000260395"
FT   REPEAT          43..72
FT                   /note="ANK 1"
FT   REPEAT          76..105
FT                   /note="ANK 2"
FT   REPEAT          108..142
FT                   /note="ANK 3"
FT   REPEAT          146..175
FT                   /note="ANK 4"
FT   REPEAT          179..208
FT                   /note="ANK 5"
FT   REPEAT          212..241
FT                   /note="ANK 6"
FT   DOMAIN          270..333
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          1..31
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   474 AA;  53019 MW;  E1FBF2AC2F0700AC CRC64;
     MAGRLRGPAV PGGGESSDSD EDGWDIGYTE RPDKLKDSLL SEEKDEVLKR ALTTGDGSLL
     EELLNSGMQV DSSFRFGWTP LMYAASIANV DLVRILLDRG ANASFSKDQH TVLMAACSAR
     VPEERILKTA ELLLSRNASP NATCRKRMSP LMYAAREGHS QLVALLVGHG AEINAQDDNG
     YTALAWAARH GHKTTVLKLL ELGADKTLQT QDGKTPAEIA KRNKHPELFS MLSLTLNPLH
     GKFQNITKEE NICKFLITDS EKSRDHGFSS YSAFGDLEIF LHGLQLEHLT ELLKERDITL
     RQLLTLRKDD FTKIGITNVR DQKKIMDAVE ELQVEEIKFE ELPEVMKLEF SGDEFLNFLL
     KLSKQCGHLT TAVQDIISQF PVHSHKIVLE WGSPECFTSV CEDLVHNAQN LGEEVGKLKH
     LIQKLHNDQK NDSCRIPPME NVSTGKKRLW KRAAVTVCGF GLLFIVCKLT FLRK
 
 
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