ID G1LS48_AILME Unreviewed; 1251 AA.
AC G1LS48;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=CASK interacting protein 2 {ECO:0000313|Ensembl:ENSAMEP00000009885.2};
GN Name=CASKIN2 {ECO:0000313|Ensembl:ENSAMEP00000009885.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000009885.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000009885.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000009885.2}
RP IDENTIFICATION.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; G1LS48; -.
DR STRING; 9646.ENSAMEP00000009885; -.
DR Ensembl; ENSAMET00000010316.2; ENSAMEP00000009885.2; ENSAMEG00000009400.2.
DR eggNOG; KOG0507; Eukaryota.
DR eggNOG; KOG4384; Eukaryota.
DR GeneTree; ENSGT00940000158256; -.
DR HOGENOM; CLU_003619_2_0_1; -.
DR InParanoid; G1LS48; -.
DR TreeFam; TF320582; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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; cd12063; SH3_Caskin2; 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; IPR035499; Caskin2_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:SF18; CASKIN-2; 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 PRINTS; PR01217; PRICHEXTENSN.
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; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT REPEAT 97..129
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 130..162
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 163..195
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 237..269
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 269..301
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 330..396
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 538..601
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 607..671
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1251 AA; 131392 MW; 69DC50F93942BE6A CRC64;
MGAGPHTLTD SPTARPGQSL CSRSGGREGG GAGFPAGGAE PVLEKEEKEE KRAKGGGESH
RPECQGPRRA SQTPSGAAGR ELLGSTKRLN VNYQDADGFS ALHHAALGGS LELIALLLEA
QATVDIKDSN GMRPLHYAAW QGRLEPVRLL LRASAAVNAA SLDGQIPLHL AAQYGHYEVS
EMLLQHQSNP CLVNKAKKTP LDLACEFGRL KVAQLLLNSH LCVALLEGEA KDPCDPNYTT
PLHLAAKNGH REVIRQLLRA GIEINRQTKT GTALHEAALY GKTEVVRLLL EGGVDVNIRN
TYNQTALDIV NQFTTSQASR EIKQLLREAS GILKVRALKD FWNLHDPTAL NIRAGDVITV
LEQHPDGRWK GHIHESQRGT DRVGYFPPGI VEVVSKRVGV LAPRLPSAPT PLRAGFSRTP
QLPAEDPLHP LTYGQVPRVG LSPDSPAGDR NSVGSEGSVG SIRSAGSGQS SEGTNGHGTG
LLIENAQPLP SPGEDQVLPG LHPPSLADNL SHRPLVNYRS GEQLFTQDVR PEQLLEGKDA
QAIHNWLSEF QLEGYTTHFL QAGYDVPTIS RMTPEDLTAI GVTKPGHRKK IASEIAQLSI
AEWLPNYIPA DLREWLCALG LPQYHKQLVS SGYDSMGLVA DLTWEELQEI GVNKLGHQKK
LMLGVKRLAE LRRGLLQGEA PAEGGRRLAR GPELMAIEGL ENGDGPAAAG PRLLTFQGSE
LSPELQAAMA GGGPEPLPLP PARSPSQESI GARSRGSGHS QEQPAPPSSG GDSSTPQERN
LPEGTERPPK LCSPLPGQGP PPYVFMYPQG PPSSPAPGPP PGAPRAFSYL AGPAATPPDP
PRPKRRSHSL SRPGPAEGEA EGEAEGPAGS ALGSYATLTR RPGRSALART SPSPTPARGA
PRSQSFALRA RRKGPPPPPP KRLSSVSGPT TEPPPVDGSP GPKEGASVPR RRTLSEPAGP
SEPSGPTAPT GPVSDTEEEE PGPEGTPPSR GSSGEGLPFA EEGNLTIKQR PKPAGPPPRE
APLPAGLDFN LTESDTVKRR PKCREREPLQ TALLAFGVAS ATPSPSAPLP SQTPSEPSSS
AAPSPPRPDP SSLPTQGAPA PLSPNPPSQP PAPPGPGPAL ENVAGSRRPG ETEPPASPAA
LIKVPGAGTA PKPVSVACTQ LAFSGPKLAP RLGPRPVPPP RPESTGAMGS GRAQQRLEQT
SSSLAAALRA AEKSIGAEER EGPPGTSTKH ILDDISTMFD ALADQLDAML D
//
