ASZ1_RHIFE
ID ASZ1_RHIFE Reviewed; 479 AA.
AC Q2IBB4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 57.
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 Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479;
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 (JAN-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; DP000028; ABC87479.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2IBB4; -.
DR SMR; Q2IBB4; -.
DR Proteomes; UP000472240; Unplaced.
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; 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..479
FT /note="Ankyrin repeat, SAM and basic leucine zipper domain-
FT containing protein 1"
FT /id="PRO_0000260398"
FT REPEAT 49..78
FT /note="ANK 1"
FT REPEAT 82..111
FT /note="ANK 2"
FT REPEAT 114..148
FT /note="ANK 3"
FT REPEAT 152..181
FT /note="ANK 4"
FT REPEAT 185..214
FT /note="ANK 5"
FT REPEAT 218..247
FT /note="ANK 6"
FT DOMAIN 276..338
FT /note="SAM"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD46"
SQ SEQUENCE 479 AA; 53504 MW; B91A3EC2DCF073FF CRC64;
MAAGVAARTL RGLAVAGGGE TSDSEDDGWE IGYLDRAAQK LKGPLPTEEK NETFKKALTT
GDILLVKELL NSGISVDSSF RYGWTPLMYA ASVSNVELVR VLLDRGANAS FDKDKQTILI
TACSARGSEE QILKCVELLL SRNADPNVPC RRLMTPIMYA ARDGHTQVVA LLVAHGAEVN
TQDENGYTAL TWAARQGHKN VVLKLLELGA NKMLQTKDGK TPSEIAKRNK HVEIFSFLSL
TLNPLEGKLQ QLTKEETICK LLTTDSDKEK DNIFSSYTAL GDLEIFLHGL GLEHMTDLLK
ERDITLRHLL TMKKDEFTKN GITSRDQQKI LDALKELQVD EIKFGELPEV TKLEISGDEF
LNFLLKLNKQ CRHLITAVQN IITELPVNSH KIVLEWASPR NFTSVCEELI SNVEDLNEEV
CKLKDLIQKL QNERENDPTH IPLIEEVSTW NSGILKRTAL AVCGFGFLLF ICKLTFQRK
