ASZ1_HORSE
ID ASZ1_HORSE Reviewed; 475 AA.
AC Q2QLA4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
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 (NOV-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; DP000020; ABB89805.1; -; Genomic_DNA.
DR RefSeq; NP_001107613.1; NM_001114141.1.
DR AlphaFoldDB; Q2QLA4; -.
DR SMR; Q2QLA4; -.
DR STRING; 9796.ENSECAP00000009625; -.
DR PaxDb; Q2QLA4; -.
DR Ensembl; ENSECAT00000012205; ENSECAP00000009625; ENSECAG00000011002.
DR GeneID; 100071245; -.
DR KEGG; ecb:100071245; -.
DR CTD; 136991; -.
DR VGNC; VGNC:15601; ASZ1.
DR GeneTree; ENSGT00880000138051; -.
DR HOGENOM; CLU_053259_0_0_1; -.
DR InParanoid; Q2QLA4; -.
DR OrthoDB; 1428188at2759; -.
DR Proteomes; UP000002281; Chromosome 4.
DR Bgee; ENSECAG00000011002; Expressed in testis and 9 other tissues.
DR GO; GO:0033391; C:chromatoid body; IDA:MGI.
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; Reference proteome; Repeat; RNA-mediated gene silencing;
KW Spermatogenesis.
FT CHAIN 1..475
FT /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT containing protein 1"
FT /id="PRO_0000226353"
FT REPEAT 45..74
FT /note="ANK 1"
FT REPEAT 78..107
FT /note="ANK 2"
FT REPEAT 110..144
FT /note="ANK 3"
FT REPEAT 148..177
FT /note="ANK 4"
FT REPEAT 181..210
FT /note="ANK 5"
FT REPEAT 214..243
FT /note="ANK 6"
FT DOMAIN 272..334
FT /note="SAM"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
SQ SEQUENCE 475 AA; 53292 MW; 97A99AEC7C706BA7 CRC64;
MAAARFRGLA VAGGGESSES EDDGWEIGYL DRAAQKLKEP LPIEEKNETF KRALTAGDVA
LVEELLDSGI SVDSSFRYGW TPLMYAASVS NVDLVRVLLD RGAKASFDKD KQTILITACS
ARGSEEQILK CVELLLSRNA DPNVACRRLM TPIMYAARDG HPQVVALLVA HGAEVNTQDE
NGYTALTWAA RQGHKNVVLK LLELGANKML QTKDGKTPSE IAKRNKHLEI FNFLSLTLNP
LEGKLQQLTK EETICKLLTT KSDKEKDHIF SSYTAFGDLE IFLHGLGLEH MTDLLKERDI
TLRHLLTMRK DEFTKNGITN KDQQKILAAL KELEVEEIKF GELPEMAKLE ISGDEFLNFL
LKLNKQCGHL ITAVQNIINE LPVNSHKIVL EWASPRNFTS VCEELVGKVE DLSEEVCKLK
DLIQKLQNER ENDPAHIPLM EEVSTWNSRI LKRTAITVCG FGFLLFICKL TFQRQ
