ID   ASZ1_BOVIN              Reviewed;         475 AA.
AC   Q8WMX8; A4D7S1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12040005; DOI=10.1210/mend.16.6.0864;
RA   Yan W., Rajkovic A., Viveiros M.M., Burns K.H., Eppig J.J., Matzuk M.M.;
RT   "Identification of Gasz, an evolutionarily conserved gene expressed
RT   exclusively in germ cells and encoding a protein with four ankyrin repeats,
RT   a sterile-alpha motif, and a basic leucine zipper.";
RL   Mol. Endocrinol. 16:1168-1184(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12917688; DOI=10.1038/nature01858;
RA   Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA   Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA   Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA   Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA   Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA   Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA   Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA   Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA   Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA   Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA   Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA   Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA   Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA   Haussler D., Green P., Miller W., Green E.D.;
RT   "Comparative analyses of multi-species sequences from targeted genomic
RT   regions.";
RL   Nature 424:788-793(2003).
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; AF461261; AAL68817.1; -; mRNA.
DR   EMBL; DP000008; AAR16262.1; -; Genomic_DNA.
DR   RefSeq; NP_776488.1; NM_174063.2.
DR   AlphaFoldDB; Q8WMX8; -.
DR   SMR; Q8WMX8; -.
DR   STRING; 9913.ENSBTAP00000000194; -.
DR   PaxDb; Q8WMX8; -.
DR   PRIDE; Q8WMX8; -.
DR   Ensembl; ENSBTAT00000000194; ENSBTAP00000000194; ENSBTAG00000000169.
DR   GeneID; 281184; -.
DR   KEGG; bta:281184; -.
DR   CTD; 136991; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000169; -.
DR   VGNC; VGNC:26231; ASZ1.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00880000138051; -.
DR   HOGENOM; CLU_053259_0_0_1; -.
DR   InParanoid; Q8WMX8; -.
DR   OMA; RHLLTMK; -.
DR   OrthoDB; 1428188at2759; -.
DR   TreeFam; TF352216; -.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000000169; Expressed in oocyte and 59 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; PF13606; Ank_3; 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   2: Evidence at transcript level;
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_0000226359"
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..25
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;  53184 MW;  EEEF157DA828F2A7 CRC64;
     MAAGPLRGLA VAGGGESSDS EDDGWEIGYL DRKSQKLKGP LPVEERQETF KKALTTGNIS
     LVEELLDSGI SVDTSFQYGW TSLMYAASVS NVELVRVLLD RGANASFDKD KQTVLITACS
     ARGSEEKILK CIELLLSRNA DPNVACRRLM TPIMYAARDG HPQVVALLVA HGAEVNTQDE
     NGYTALTWAA RQGHKNVVLK LLELGANKMI QTKDGKTPSE IAKRNKHLEI FNFLSLTLNP
     LEGKLHQLTK EESICKLLRT DSDKEKDHIF SSYTAFGDLE IFLHGLGLEH MTDLLKEREI
     TLRHLLTMRK DELAKNGITS RDQQKIMAAL KELEVEEIKF GELPEVAKLE ISGDEFLNFL
     LKLNKQCGHL ITAVQNIITE LPVNSHKIVL EWASPRNFTS VCEELVSNVE DLSEEVCKLK
     DLIQKLQNER ENDPTHIPLM EEVSTWNSRI LKRTAITVCG FGFLLFICKL AFQRK