ID W5PN70_SHEEP Unreviewed; 1094 AA.
AC W5PN70;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000011896.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000011896.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000011896.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000011896.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000011896.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; AMGL01058322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01058323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01058324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01058325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01058326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01058327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5PN70; -.
DR SMR; W5PN70; -.
DR STRING; 9940.ENSOARP00000011896; -.
DR PaxDb; 9940-ENSOARP00000011896; -.
DR Ensembl; ENSOART00000012070.1; ENSOARP00000011896.1; ENSOARG00000011089.1.
DR eggNOG; KOG0507; Eukaryota.
DR HOGENOM; CLU_010379_0_0_1; -.
DR OMA; REGWSEC; -.
DR Proteomes; UP000002356; Chromosome 20.
DR Bgee; ENSOARG00000011089; Expressed in heart right ventricle and 52 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR CDD; cd01274; PTB_Anks; 1.
DR CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1.
DR CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR InterPro; IPR033635; ANKS1/Caskin.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041880; SAM_ANKS1_repeat1.
DR InterPro; IPR041882; SAM_ANKS1_repeat2.
DR PANTHER; PTHR24174:SF4; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 1A; 1.
DR PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00454; SAM; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 14..46
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 47..79
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 104..136
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 137..169
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 170..202
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 202..234
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 654..720
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 728..787
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 901..1033
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 276..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 120180 MW; D53930148F4B55D3 CRC64;
SIWRGPNVNC VDSTGYTPLH HAALNGHKDV VEVLLRNDAL TNVADSKGCY PLHLAAWKGD
AQIVRLLIHQ GPSHTKVNEQ NALEIKELKK YGPFDPYINA KNNDNETALH CAAQYGHTEV
VKVLLEELTD PTMRNNKFET PLDLAALYGR LEVVKMLLNA HPNLLSCNTK KHTPLHLAAR
NGHKAVVQVL LDAGMDSSYQ TEKGSALHEA ALFGKTDVVQ ILLAAGIDVN IKDNRGLTAL
DTVRELPSQK SQQIAALIED HMTGKRSAKE VDKTLAPQPP LISNPDSISQ KSQGDLEKAV
TELIIDFNTN REEEGPYEAL YNAVSCQSLD STASGRSSDR DSVSREAEAA GGKAAGVRPR
ERPPPPAKPP PDEEEEDHID KKYFPLTASE VLAMRPWIQG SAAKEEDEHP YELLLTAETK
KLVSVDGKTK VQDHRRSSGG RSQDSAEGQD GQVPEQFSGL LHGSSPVCEA GQDPLQLLPA
PGQNHREGSP AQGACPEEMQ LEQTGRRASG ASLPRVLDQS RRVGHPASLP PAHSQTHPKT
VMRTAFPRPG GAEEEGDLSG ARSRAPPTSR PKAELKLSRS LSKSDSDLLT CSPTEDATMG
SRSESLSNCS IGKKRLEKSP SFASEWDEIE KIMSSIGEGI DFSQEQQRIS GARPREQSVG
EWLEARGLQQ YESRLLLNGF DDVRFLGPNV MEDQDLREIG ISDAQHRRKL LQAARSLPKV
KALGYDGNSP ASVPSWLDSL GLQDYVHSFL SSGYSSIDTV KNLWELELVN VLKVHLLGHR
KRIIASLADR PYEEPPQKPP RFSQLRQCQD LFSQTSSPLS QSDSCAARSA DLLLPPGEPG
RRLRDSLHEP AASSRAERFR TQEEHREAKL TLRPPSLAAP YAPVQSWQHQ PEKLIFESCG
YEANVISGSM LIKDLRGTES TQDACAKMRK STEHMRKIPT IVLSITYKGV KFIDASNKNV
IAEHEIRNIS CAAQDPEDLC AFAYVTKDLQ TGHHYCHVFR QVDVNLTYEI ILTLGQAFEV
AYQLALQAQK SRPMGASAAE VIETRSSKPV PKPRVGVRKS ALEPPDTDPD AQSHASVSWV
VDPKPDSKRS LSTK
//
