ID A0A452FA63_CAPHI Unreviewed; 493 AA.
AC A0A452FA63;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 {ECO:0000256|ARBA:ARBA00020117};
DE AltName: Full=Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein {ECO:0000256|ARBA:ARBA00030354};
GN Name=ASZ1 {ECO:0000313|Ensembl:ENSCHIP00000021149.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000021149.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000021149.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000021149.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025297}.
CC -!- SUBUNIT: Interacts with DDX4, PIWIL1, RANBP9 and TDRD1.
CC {ECO:0000256|ARBA:ARBA00011479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; LWLT01000003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452FA63; -.
DR STRING; 9925.ENSCHIP00000021149; -.
DR Ensembl; ENSCHIT00000028991.1; ENSCHIP00000021149.1; ENSCHIG00000019569.1.
DR GeneTree; ENSGT00880000138051; -.
DR OMA; SFQYGWT; -.
DR Proteomes; UP000291000; Chromosome 4.
DR Bgee; ENSCHIG00000019569; Expressed in testis and 10 other cell types or tissues.
DR GO; GO:0071546; C:pi-body; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0010526; P:retrotransposon silencing; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF140860; Pseudo ankyrin repeat-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT REPEAT 96..128
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 166..198
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 199..231
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 290..352
FT /note="SAM"
FT /evidence="ECO:0000259|Pfam:PF07647"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 54974 MW; 734E90EE03195CCD CRC64;
MEPVGRQAAS TVRRGPGGMA ASPLRGLAVA GGGESSESED DGWEIGYLDR TAQKLKGPLP
VEERQETFKK ALTSGNISLV EELLDSGISV DTSFQYGWTS LMYAASVSNV ELVRVLLDRG
ANASFDKDKQ TVLITACSAR GSEEKILKCI ELLLSRNADP NVACRRLMTP IMYAARDGHP
QVVALLVAHG AEVNTQDENG YTALTWAARQ GHKNVVLKLL ELGANKMIQT KDGKTPSEIA
KRNKHLEIFN FLSLTLNPLE GKLHQLTKEE SISKLLRTDS DKEKDHIFSS YTAFGDLEIF
LHGLGLEHMT DLLKEREITL RHLLTMRKDE LSKNGITSRD QQKIMAALKE LEVEEIKFGE
LPEVAKLEIS GDEFLNFLLK LNKQCGHLIK AVQNIITELP VNSHKIVLEW ASPRNFTSVC
EELVSNVEDL SEEVCKLKDL IQKLQNEREN DPTHIPLMEE VSTWNTRILK RTAITVCGFG
VLLFICKLTF QKK
//
