ID G1LD29_AILME Unreviewed; 587 AA.
AC G1LD29;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Ankyrin repeat and sterile alpha motif domain containing 6 {ECO:0000313|Ensembl:ENSAMEP00000004810.2};
GN Name=ANKS6 {ECO:0000313|Ensembl:ENSAMEP00000004810.2};
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:ENSAMEP00000004810.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000004810.2, 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:ENSAMEP00000004810.2}
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}.
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DR AlphaFoldDB; G1LD29; -.
DR STRING; 9646.ENSAMEP00000004810; -.
DR Ensembl; ENSAMET00000005003.2; ENSAMEP00000004810.2; ENSAMEG00000004563.2.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000157664; -.
DR HOGENOM; CLU_018325_0_0_1; -.
DR InParanoid; G1LD29; -.
DR TreeFam; TF329520; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0097543; C:ciliary inversin compartment; IEA:Ensembl.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR CDD; cd09518; SAM_ANKS6; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR10627:SF70; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 6; 1.
DR PANTHER; PTHR10627; SCP160; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 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}.
FT REPEAT 24..56
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 58..90
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 475..538
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 121..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 62294 MW; A3EB4FD62331BB25 CRC64;
MGNCQLVKEI ADEDPNYVNL VNGDGATPLM LAAVMGQLPL VQLLVERHAD IDKQDSVHGW
TALMQATYHG NKEIVKYLLN QGADVTLRAK NGYTAFDLVM LLSDPDTELV RLLASVCMQV
NKDKGRPSHP PPPPHSKVRQ PWSVPVLPDD KGGLKSWWNR MSNRFRKLKL MQTLPRGLSS
NQPLPFCDEP ESALDSTMRA APQDKTSRPG LRDVAPTTKE NGPGSTRGNK EDVLLTTMLR
NGAPFPRLPS DKLKAVIPPF LPPSSFELWS SDRSRTCHSG KAEPVKTVLS QRAGRGAPMG
AAGGSTDATP VRPVKFPSLS RSPASPVNSG NFNHSPHSSG GSSGVGGSSR HGGELHNRSG
GSIDSVLSQI AAQRRKAAGL SEQKPGHQSS PVGPAPGSSS SELPVAPAGS GGPGGKKLET
SKRPPSGTST TSKSTSPTLT PSPSPKGHTA ESSVSSSSSH RQSKSSGGSS SGTITDEDEL
TGILKKLSLE KYQPIFEEQE VDMEAFLTLT DGDLKELGIK TDGSRQQILA AISELNAGKG
RERQILQETI HNFHSSFESS ASNTRAPGNP SIAGGVRPEE GASRQRE
//
