ID A0A5F5XQN5_FELCA Unreviewed; 1456 AA.
AC A0A5F5XQN5;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=Caskin-1 {ECO:0000256|ARBA:ARBA00073386};
DE AltName: Full=CASK-interacting protein 1 {ECO:0000256|ARBA:ARBA00082418};
GN Name=CASKIN1 {ECO:0000313|Ensembl:ENSFCAP00000056342.1,
GN ECO:0000313|VGNC:VGNC:82359};
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:ENSFCAP00000056342.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000056342.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000056342.1,
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:ENSFCAP00000056342.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000056342.1,
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:ENSFCAP00000056342.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000056342.1};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: May link the scaffolding protein CASK to downstream
CC intracellular effectors. {ECO:0000256|ARBA:ARBA00055074}.
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 EMBL; AANG04001668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSFCAT00000007681.6; ENSFCAP00000056342.1; ENSFCAG00000007678.6.
DR VGNC; VGNC:82359; CASKIN1.
DR GeneTree; ENSGT00940000158025; -.
DR Proteomes; UP000011712; Chromosome E3.
DR Bgee; ENSFCAG00000007678; Expressed in prefrontal cortex and 7 other cell types or tissues.
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 CDD; cd12062; SH3_Caskin1; 1.
DR FunFam; 1.10.150.50:FF:000032; caskin-1 isoform X1; 1.
DR FunFam; 1.25.40.20:FF:000225; caskin-1 isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000062; caskin-2 isoform X1; 1.
DR FunFam; 1.10.150.50:FF:000028; caskin-2 isoform X2; 1.
DR FunFam; 1.25.40.20:FF:000042; caskin-2 isoform X2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; IPR035495; Caskin1_SH3.
DR InterPro; IPR032117; Caskin_C.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR24174:SF11; CASKIN-1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
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 Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00326; SH3; 1.
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; 6.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
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 147..171
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 281..347
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 472..535
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 541..605
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 348..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..367
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..684
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..817
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1317
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1345
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1392
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 151904 MW; 6F7DF38FEFBAE07E CRC64;
MGKEQELVQA VKAEDVGTAQ RLLQRPRPGK AKLLGSTKKI NVNFQDPDGF SALHHAALNG
NTELITLLLE AQAAVDIKDN KGMRPLHYAA WQGRKEPMKL VLKAGSAVNI PSDEGHIPLH
LAAQHGHYDV SEMLLQHQSN PCMVDNSGKT PLDLACEFGR VGVVQLLLNS NMCAALLEPR
PGDTTDPNGT SPLHLAAKNG HIDIIRLLLQ AGIDINRQTK SGTALHEAAL CGKTEVVRLL
LDNGINAHVR NTYSQTALDI VHQFTTSQAS KEIKQLLREA SAALQVRATK DYCNNYDLTS
LNVKAGDIIT VLEQHPDGRW KGCIHDNRTG NDRVGYFPSS LGEAIVKRAG SRAGTEPSPS
QAGSSPGPSA PPEEIWVLRK PFAGGDRSGS LGSVAGGRSS GGHTLHAGSE GVKLLATVLS
QKSVSESSPG DGPAKPPEGS TGAARSQLPA AHAGQVYGEQ PPRKLEPASE GKSAEAVGQW
LATFQLQLYA PNFISAGYDL PTISRMTPED LTAIGVTKPG HRKKITAEIS GLSIPDWLPE
HKPANLAVWL SMIGLAQYYK VLVDNGYENI DFITDITWED LQEIGITKLG HQKKLMLAVR
KLAELQKAEY AKFEGGPLRR KAPQSLEVMA IESPPPPEPA PADCQSPKMT TFQDSELSGE
LQAAMTGPAE GGAAAAAATT ATTAEKPSNH LPPTPRASVR QEPSLGGQAR HMSSSQELLG
DGPPGPGSPM SRSQEYLLDE GPAPGTPPKE TRPSRHGHSV KRASVPPVPG KPRQVLPPGA
SHFTPPQTPT KAQPGSPQAL GGPHGPAPAT AKVKPTPQLL PPTERPMSPR SLPQSPTHRG
FAYVLPQPVE SDAGPAAPGP GPVPVPAAAP PPVPTLCLPP EADAEPGRPK KRAHSLNRYA
ASDSEPERDE LLVPAAAGPY ATVQRRVGRS HSVRAPAGTD KNVNRSQSFA VRPRKKGPPP
PPPKRSSSAM ASANLADESA PDAETEGAGT EDGRLGVRAQ RRRASDLAGS VDTGSAGSVK
SIAAMLELSS IGGGGRAARR PPEGHPTPRP ASPEPGRVAT VLASVKHKEA IGPDGEVVNR
RRTLSGPVTG LLATARRAPG ESGGPADHGH FVEDGSARQR SRGPAKGEAS GEGPPLARVE
ASATLKRRIR AKQSQQESVK FILTESDTVK RRPKAKEREA GPEPPPLSVY QNGTGTVRRR
PTSEQTGPPE LPPPPPPAEP PPSDLMHLPP LPPPDTDSRK PAKPPVSPKP MLAQPVPKIQ
GSPTPASKKV PLPGPGSPEV KRAHGTPPPV SPKPPPPPTA PKPAKAAAGL QSGSASPSPA
PSPARQPPAA LAKPASTPPS LSASPAKPPS PGASALHVPA KPPRAAAAAA AAATTATAGP
PAAPDGASPG DSARQKLEET SACLAAALQA VEEKIRQEDA QGARPSSAEE KSTGSILDDI
GSMFDDLADQ LDAMLE
//
