ID A0A1S2ZNI7_ERIEU Unreviewed; 1261 AA.
AC A0A1S2ZNI7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Ankyrin repeat and sterile alpha motif domain-containing protein 1B isoform X1 {ECO:0000313|RefSeq:XP_007522108.1};
GN Name=ANKS1B {ECO:0000313|RefSeq:XP_007522108.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007522108.1};
RN [1] {ECO:0000313|RefSeq:XP_007522108.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007522108.1; XM_007522046.2.
DR AlphaFoldDB; A0A1S2ZNI7; -.
DR STRING; 9365.ENSEEUP00000005405; -.
DR GeneID; 103112599; -.
DR CTD; 56899; -.
DR eggNOG; KOG0507; Eukaryota.
DR InParanoid; A0A1S2ZNI7; -.
DR OrthoDB; 25046at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR24174:SF3; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1B; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00536; SAM_1; 2.
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; 5.
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:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 58..90
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 91..123
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 127..159
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 193..225
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 225..257
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 814..877
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 885..950
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1060..1193
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 298..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1261 AA; 139087 MW; 512E229389B5C2BA CRC64;
MGKDQELLDA ARTGNAAQVE KLLSGRRGGI LGGGSAPLPL SSLLSIWRGP NVNCTDSSGY
TALHHAALNG HKDIVLKLLQ YEASTNVADN KGYFPIHLAA WKGDVEIVKI LIHHGPSHSR
VNEQNNENET ALHCAAQYGH SEVVAVLLEE LTDPAIRNSK LETPLDLAAL YGRLRVVKMI
VSAHPHLMSC NTRKHTPLHL AARNGHKAVV QVLLEAGMDV SCQTEKGSAL HEAALFGKVD
VVRVLLETGI DANIKDSLGR TVLDILKEHP SQKSLQIATL LQEYLEGLGR STVLEEHAQE
DTAQETNNSS SPVASPLQKT KSDTVTGELS KLLDEIKLCQ EKDYSFEDLC HTISDHYLDN
LSKISEEELG KNGSQSVRTS STINLSPGEV EDDYDNENTC GPTGLWEALT PCNGCRNLGF
TMLAQESYPK KRNYTMEMVP SASVDTFPSE NENFLCDLTD TAVTKKPCSL EIARAPSPRT
ENASEVAITA PGTSNHRNSS TGPTPDCSPP SPDTALKNIV KVIRPQPKQR TSIVSALDFQ
RMNHSQEYFE IVTATECAAL TPSPPASPPT SSVGTTGVKD EGTGHTDDLP QPEDTDPPRE
YDPGQFAGLL HGSSPACESP ENPFHLYGKR DEPGEVQEEM NLASNPLTFK QPPAGKNSEP
LVKKVKPKVV SRTIFHKKSS HLQNHTIVGT KASRSGSRSG EQWMATTGTF VERACTLGRI
RSLPKALIDM HLSKNVSKSD SDLIGYPSTE KAARVNWSET STAEHSSRGN SERTPSFTSE
WEEIDKIMNS IDIGINSELE EMDGENTRPR CPVQTVGQWL ESIGLPQYEN HLMANGFDNV
QFMGSNVMED QDLLEIGILN SGHRQRILQA IQLLPKMRPI GHEGYHPTSV AEWLDSIELG
DYTKAFLING YTSMDLLKKI WEVELINVLK ISLIGHRKRI LASLGDRLQE DPPQKPPRSI
TLREPSGNHT PPQLSPSLSQ STYTTGGSLD VPHIIMQGDA RRRRNENYFD DIPRSKLERQ
MAQTGDWGEP SITLRPPNEA TASTPVQYWQ HHPEKLIFQS CDYKAFYLGS MLIKELRGTE
STQDACAKMR ANCQKSTEQM KKVPTIILSV SYKGVKFIDA ANKNIIAEHE IRNISCAAQD
PEDLSTFAYI TKDLKSNHHY CHVFTAFDVN LAYEIILTLG QAFEVAYQLA LQARKGGHSS
TLPESFENKP SKPIPKPRVS IRKSVQIDPS EQKTLANLPW IVEPGQEAKR SINTKYETTI
F
//
