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 27-MAR-2024, entry version 66.
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; ENSOANT00000039557.2; ENSOANP00000030318.2; ENSOANG00000031342.2.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00880000138051; -.
DR InParanoid; Q07DZ7; -.
DR OMA; SFQYGWT; -.
DR OrthoDB; 5354112at2759; -.
DR Proteomes; UP000002279; Chromosome 10.
DR Bgee; ENSOANG00000031342; Expressed in testis and 5 other cell types or tissues.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA processing; IBA:GO_Central.
DR GO; GO:0010526; P:retrotransposon silencing; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd09521; SAM_ASZ1; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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 PANTHER; PTHR24157; ANKYRIN REPEAT, SAM AND BASIC LEUCINE ZIPPER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR24157:SF3; ANKYRIN REPEAT, SAM AND BASIC LEUCINE ZIPPER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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
//
