ID A0A3Q1MKP8_BOVIN Unreviewed; 1171 AA.
AC A0A3Q1MKP8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ankyrin repeat and sterile alpha motif domain containing 1A {ECO:0000313|Ensembl:ENSBTAP00000071484.1};
GN Name=ANKS1A {ECO:0000313|Ensembl:ENSBTAP00000071484.1,
GN ECO:0000313|VGNC:VGNC:25944};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000071484.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000071484.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000071484.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000071484.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000071484.1};
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 AlphaFoldDB; A0A3Q1MKP8; -.
DR Ensembl; ENSBTAT00000068504.1; ENSBTAP00000071484.1; ENSBTAG00000016890.6.
DR VEuPathDB; HostDB:ENSBTAG00000016890; -.
DR VGNC; VGNC:25944; ANKS1A.
DR GeneTree; ENSGT00940000155806; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000016890; Expressed in trachea and 107 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1MKP8; baseline.
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; 3.
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:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 83..115
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 116..148
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 152..184
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 185..217
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 218..250
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 250..282
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 703..766
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 774..833
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 946..1077
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 33..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 126654 MW; FF0E5B7282570AEB CRC64;
MGKEQELLEA ARTGHLPAVE KLLSGKRLSS GFGGGGGGGG SGGGSGGGSG SGGGGGGLGS
SSHALSSLLS IWRGPNVNCV DSTGYTPLHH AALNGHKDVV EVLLRNDALT NVADSKGCYP
LHLAAWKGDA QIVRLLIHQG PSHTKVNEQN NDNETALHCA AQYGHTEVVK VLLEELTDPT
MRNNKFETPL DLAALYGRLE VVKMLLNAHP NLLSCNTKKH TPLHLAARNG HKAVVQVLLD
AGMDSSYQTE KGSALHEAAL FGKTDVVQIL LAAGIDVNIK DNRGLTALDT VRELPSQKSQ
QIAALIEDHM TGKRSAKEVD KTLTPQPPLI SNLDSISQKS QGDLEKAVTE LIIDFNTSTE
EEGPYEALYN AVSCQSLDST ASGRSSDRDS VSREAEAAGG KAAGVRPRER PPPPAKPPPD
EEEEDHIDKK YFPLTASEVL AMRPWVQGSP AKEEDEHPYE LLLTAETKKL VSVDGKTKDH
RQSSGGRSQD SAEGQDGQVP EQFSGLLHGS SPVCEAGQDP LQLLPAPGQN HREGSPAQGA
CPEEMQLEQT GRRASGASPP RVLDQSRRVG HPASLPPAHS QTHPKTSMRT AFPRPGGAEE
EGDPSGARSR APPTSRPKAE LKLSRSLSKS DSDLLTCSPT EDATMGSRSE SLSNCSIGKK
RLEKSPSFAS EWDEIEKIMS SIGEGIDFSQ EQQRISGARP LEQSVGEWLE AVGLQQYESR
LLLNGFDDVR FLGPNVMEDQ DLREIGISDA QHRRKLLQAA RSLPKVKALG YDGNSPLSVP
SWLDSLGLQD YVHSFLSSGY SSIDTVKNLW ELELVNVLKV HLLGHRKRII ASLADRPYEE
PPQKPPRFSQ LRCQDLFSQT SSPLSQNDSC AGRSADLLLP PGDAGRRPHD SLHEPAAPSR
AERFRTQEEH REAKLTLRPP SLAAPYAPVQ SWQHQPEKLI FESCGYEANY LGSMLIKDLR
GTESTQDACA KMRKSTEHMR KIPTIILSIT YKGVKFIDAS NKNVIAEHEI RNISCAAQDP
EDLCAFAYVT KDLQTGHHYC HVFSTVDVNL TYEIILTLGQ AFEVAYQLAL QAQKSRPVGA
SAAEVIETRS SKPVPKPRVG VRKSAVPPPP GSRCCHCHTR PAHRPSYLPL PSVSPGAKLE
PPDTDPDAQS HASVSWVVDP KPDSKRSLST N
//
