ID A0A2Y9KZ88_ENHLU Unreviewed; 1198 AA.
AC A0A2Y9KZ88;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Caskin-2 isoform X2 {ECO:0000313|RefSeq:XP_022378976.1};
GN Name=LOC111160299 {ECO:0000313|RefSeq:XP_022378976.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022378976.1};
RN [1] {ECO:0000313|RefSeq:XP_022378976.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022378976.1};
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_022378976.1; XM_022523268.1.
DR AlphaFoldDB; A0A2Y9KZ88; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR032232; Caskin1-CID.
DR InterPro; IPR035497; Caskin1/2_SAM_1.
DR InterPro; IPR035498; Caskin1/2_SAM_2.
DR InterPro; IPR032117; Caskin_C.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR24174:SF18; CASKIN-2; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF16907; Caskin-Pro-rich; 1.
DR Pfam; PF16632; Caskin-tail; 1.
DR Pfam; PF16600; Caskin1-CID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 48..80
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 81..113
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 114..146
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 188..220
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 220..252
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 485..548
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 554..618
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 351..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..787
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1064
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 125771 MW; 8F994D0659D1CF79 CRC64;
MGREQDLILA VKNGDVTGVQ KLVAKVKAAK TKLLGSTKRL NVNYQDADGF SALHHAALGG
SLELIALLLE AQATVDIKDS NGMRPLHYAA WQGRLEPVRL LLRASAAVNA ASLDGQIPLH
LAAQYGHYEV SEMLLQHQSN PCLVNKAKKT PLDLACEFGR LKVAQLLLNS HLCVALLEGE
AKDPCDPNYT TPLHLAAKNG HREVIRQLLR AGIEVNRQTK TGTALHEAAL YGKTEVVRLL
LEGGVDVNIR NTYNQTALDI VNQFTTSQAS REIKQLLREA SGILKVRALK DFWNLHDPTA
LNVRAGDVIT HPDGRWKGHI HESQRGTDRV GYFPPGIVEV VSKRVGVLAP RLPSAPTPLR
PGFSRTPQPP AEDPLHPLTY GQLPRGGLSP DSPAGDRSSV GSEGSVGSIR SAGSGQSSEG
ANGHGTGLLI ENAQPLPSTG EDQVLLGLHP PSLADNLSHR PLANYRSGEQ LFTQDVRPEQ
LLEGKDAQAI HNWLSEFQLE GYTAHFLQAG YDVPTISRMT PEDLTAIGVT KPGHRKKIAS
EIAQLSIAEW LPNYIPVDLR EWLCALGLPQ YHKHLVSSGY DSMGLVADLT WEELQEIGVN
KLGHQKKLML GVKRLAELRR GLLQGEAPAE GGRRLARGPE LMAIEGLENG DGPAAAGPRL
LTFQGSELSP ELQAAMAGGG PEPLPLPPAR SPSQESIGAR SQGSGHSQEQ PASQPGGGDP
GTPQERNLPE GTERPPKLCS PLPGQGAPPY VFMYPQGSPS SPAPGPPPGA PRAFSYLAGP
PATPPDPPRP KRRSHSLSRP GPEDGEAEGE AEGPVGSALG SYATLTRRPG RSALARTSPS
PTPARGAPRS QSFALRARRK GPPPPPPKRL SSVSGPTTEP PPVDGSPGPK EGASVPRRRT
LSEPAGPLEP PSPPAPAGPV SDTEEEEPGP EGTPPSRGSS GEGLPFAEEG NLTIKQRPKP
AGPPSREAPV PAGLDFNLTE SDTVKRRPKC RGREPLQTAL LAFGVAGATP SASASLPSQP
PGEPSSSAAP SPPRPDPSSL PTQGAPVPLS PGLPAQPPVA PSPGPALENS AGGGQPGEME
PPASPAALIK VPSAGTAPKP VSVACTQLAF SGPKLAPRLG PRPVPPPRPE STGAAGSGRA
QQRLEQTSSS LAAALRVAEK SIGVEEQEGP PGTSTKHILD DISTMFDALA NQLDAMLD
//
