ID A0A3Q7RL84_VULVU Unreviewed; 1142 AA.
AC A0A3Q7RL84;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ankyrin repeat and SAM domain-containing protein 1A isoform X4 {ECO:0000313|RefSeq:XP_025846567.1};
GN Name=ANKS1A {ECO:0000313|RefSeq:XP_025846567.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025846567.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025846567.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025846567.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025846567.1};
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_025846567.1; XM_025990782.1.
DR AlphaFoldDB; A0A3Q7RL84; -.
DR STRING; 9627.ENSVVUP00000036485; -.
DR Proteomes; UP000286640; 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: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:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 78..110
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 111..143
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 147..179
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 180..212
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 213..245
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 245..277
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 701..764
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 772..831
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 944..1075
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 33..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 124095 MW; F831D5EBC3573145 CRC64;
MGKEQELLEA ARTGHLPAVE KLLSGKRLSS GFGGGGGGSG SSGSGGGGGG GGLGSSSHPL
SSLLSIWRGP NVNCVDSTGY TPLHHAALNG HKDVVEVLLR NDALTNVADS KGCYPLHLAA
WKGDAQIVRL LIHQGPSHTR VNEQNNDNET ALHCAAQYGH TEVVKVLLEE LTDPTMRNNK
FETPLDLAAL YGRLEVVKML LNAHPNLLSC NTKKHTPLHL AARNGHKAVV QVLLDAGMDS
NYQTEKGSAL HEAALFGKTD VVQILLAAGI DVNIKDNRGL TALDTVRELP SQKSQQIAAL
IEDHMTGKRS AKEVDKTLRS QGPLISNMDS ISQKSQGDVE KAVTELIIDF DTNAEEEGPY
EALYNAVSCH SLDSMASGRS SDRDSVNKET EAAGVKAAGV RPRERPPPPA KPPPDEEEEE
RIDKKYFPLT ASEVLAMRPW IQGSAAREED EHPYELLLTA ETKKLGSMDG DGKPKDHRRS
SSSRSQDSAE GQDGQVPEQF SGLLHGSSPV CEVGQDPFQL LSATGQSHPE GSPAQGACHE
ASMQLEETGV HAPGASPPSV LDQGKRVGYP AGLPTTTSQS HPETLTHTAS QHPGGAEEEK
DRSGTRSRAP PTSKPKAELK LSRSLSKSDS DLLTCSPTED TTMGSRSESL SNCSIGKKRL
EKSPSFASEW DEIEKIMSSI GEGIDFSQEQ QKISGSRTLE QSVGEWLEAV GLQQYESKLL
LNGFDDVRFL GSNVMEEQDL RDIGITDPQH RRKLLQAAKS LPKVKALGYD GNSPPSVPSW
LDSLGLQDYV HSFLSSGYSS IDTVKNLWEL ELVNVLKVHL LGHRKRIIAS LADRPYEEPP
QKPPRFSQLR CQDLLSQASS PLSQNDSCTG RSADLLLPPG DTGKRRHDSL HDPAAPSRAE
RFRVQEEQRE AKLTLRPPSL AAPYAPVQSW QHQPEKLIFE SCGYEANYLG SMLIKDLRGT
ESTQDACAKM RKSTEHMKKI PTIILSITYK GVKFIDASNK NVIAEHEIRN ISCAAQDPED
LCTFAYITKD LQTSHHYCHV FSTVDVNLTY EIILTLGQAF EVAYQLALQA QKSRPLGASA
AETIETKSSK PVPKPRVGTR KSALEPPDLD PDTQSHASVS WVVDPKPDSK RSLSTKYETT
IF
//
