ID A0A2I2UA92_FELCA Unreviewed; 553 AA.
AC A0A2I2UA92;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ankyrin repeat and sterile alpha motif domain containing 3 {ECO:0000313|Ensembl:ENSFCAP00000029369.2};
GN Name=ANKS3 {ECO:0000313|Ensembl:ENSFCAP00000029369.2,
GN ECO:0000313|VGNC:VGNC:59821};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000029369.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000029369.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000029369.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000029369.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000029369.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000029369.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000029369.2};
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; AANG04001668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2UA92; -.
DR PaxDb; 9685-ENSFCAP00000004216; -.
DR Ensembl; ENSFCAT00000043592.3; ENSFCAP00000029369.2; ENSFCAG00000004565.6.
DR VGNC; VGNC:59821; ANKS3.
DR GeneTree; ENSGT00940000156610; -.
DR Proteomes; UP000011712; Chromosome E3.
DR Bgee; ENSFCAG00000004565; Expressed in adult mammalian kidney and 10 other cell types or tissues.
DR CDD; cd09519; SAM_ANKS3; 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; IPR047238; ANKS3_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; PTHR24184:SF6; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR24184; SI:CH211-189E2.2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 61..93
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 321..384
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 245..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 60561 MW; 6079D190AC84F834 CRC64;
MSELSDEASE PELLNCSLSM WHGLGAQVGR EELAVPLDLH TAASIGQYEV VKECVQREPV
YGFTPLMEAA ASGHEIIVQY FLNHGVRVDT RDHSGATARM LAKQYGHMKI VGLIDAHSPT
LPKNLYRSPE KFEDLSSSDE SCPVPQRQRP CRKKGLSIHE GPRALARITA IGLGGKMQQA
CCEQVPPRGY VTFNSSDENP LEAGGLCYRD VTSPINDRDV ESSSSSSREE HAFCANLGVA
RRSSSSEGLA RAPGVSSEAS LESNEDSDHA CQSSVRKQTK SYMKTKNRYS NSDGQWPAST
GPAGAACSPA SVSQTERSLC SGPQDLATLL EQIGCLKYLQ VFEEQDVDLR IFLTLTESDL
KEIGITLFGP KRKMTSAIAR WHSSARPPSD ALELAYADRL EAEMQELAIQ LHKRCEEVEA
MRGQVSQEQE LRAVVESCLL EQDGARKDVH AQLQETWALA RDAALVLDQL RACQAELSAR
VKQEESTRGL PQGPALPTAD SKGWQASLQA LSLPELSGAL EDRVQEMGRV LCSVTQSLEK
LQVLNGKENW REP
//
