ID A0A452F1Z5_CAPHI Unreviewed; 412 AA.
AC A0A452F1Z5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ankyrin repeat and sterile alpha motif domain containing 4B {ECO:0000313|Ensembl:ENSCHIP00000018401.1};
GN Name=ANKS4B {ECO:0000313|Ensembl:ENSCHIP00000018401.1};
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:ENSCHIP00000018401.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000018401.1, 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:ENSCHIP00000018401.1}
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}.
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DR EMBL; LWLT01000031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005697644.2; XM_005697587.3.
DR RefSeq; XP_005697645.2; XM_005697588.3.
DR AlphaFoldDB; A0A452F1Z5; -.
DR STRING; 9925.ENSCHIP00000018401; -.
DR Ensembl; ENSCHIT00000026216.1; ENSCHIP00000018401.1; ENSCHIG00000017844.1.
DR GeneID; 100861335; -.
DR KEGG; chx:100861335; -.
DR CTD; 257629; -.
DR GeneTree; ENSGT00390000017548; -.
DR OMA; DLQSIHM; -.
DR Proteomes; UP000291000; Chromosome 25.
DR Bgee; ENSCHIG00000017844; Expressed in adult mammalian kidney and 16 other cell types or tissues.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:1904970; P:brush border assembly; IEA:Ensembl.
DR GO; GO:1904106; P:protein localization to microvillus; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR CDD; cd09587; SAM_HARP; 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; IPR037601; ANKS4B_SAM.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24161:SF20; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 4B; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 31..63
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 64..96
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 335..400
FT /note="SAM"
FT /evidence="ECO:0000259|SMART:SM00454"
FT REGION 297..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 136..163
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 310..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46310 MW; EE6F1339E697C5F2 CRC64;
MSTRYHQAAS DSYLELLKEA TKRDLNLSDE DGMTPTLLAA YHGNLEALEI ICSRGGDPNR
CDIWGNTPLH YAASNGHAHC VSFLINFGAN IFALDNDLQS PLDAAASREQ NECVALLDKA
ATAQNIMNPK KVTRQKEQAQ KNVKKQIKEC ERLQEKHQNK MARTYSKEES GTLSSAKGTF
TRSLLSNASA SNTFGSLSKG IKDTLKLKFK KNKDTAEQLG NESRSGQKNV MEVFREDEED
EFSGDFIEKL QLSAKGDSCM QHESILNRPG LGNVVFGRNR IFSPEDISDS RRELGLTMPS
ELFQRPGEAE ADEEGEENNH EGDLPWDEDE VEWEEDVVDA TALEVFLQSH YLEEFLPIFM
REQIDLEALL LCSDEDLQSI HMQLGPRKKV LNAINRRKQV LQQPGQLVDT NL
//
