ID D2HLL0_AILME Unreviewed; 1772 AA.
AC D2HLL0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Kinase D interacting substrate 220 {ECO:0000313|Ensembl:ENSAMEP00000008798.1};
DE Flags: Fragment;
GN Name=KIDINS220 {ECO:0000313|Ensembl:ENSAMEP00000008798.1};
GN ORFNames=PANDA_012393 {ECO:0000313|EMBL:EFB27451.1};
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|EMBL:EFB27451.1};
RN [1] {ECO:0000313|EMBL:EFB27451.1, 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:ENSAMEP00000008798.1}
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL193012; EFB27451.1; -; Genomic_DNA.
DR STRING; 9646.ENSAMEP00000008798; -.
DR Ensembl; ENSAMET00000009174.2; ENSAMEP00000008798.1; ENSAMEG00000008328.2.
DR eggNOG; KOG0502; Eukaryota.
DR GeneTree; ENSGT00940000156714; -.
DR HOGENOM; CLU_001438_2_0_1; -.
DR OMA; TGHDYLK; -.
DR TreeFam; TF344032; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
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; IPR011646; KAP_P-loop.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR24116; KINASE D-INTERACTING SUBSTRATE OF 220 KDA; 1.
DR PANTHER; PTHR24116:SF0; KINASE D-INTERACTING SUBSTRATE OF 220 KDA; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07693; KAP_NTPase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 10.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 37..69
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 70..102
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 103..135
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 136..168
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 169..201
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 202..234
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 235..267
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 268..300
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 334..366
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 367..390
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 440..952
FT /note="KAP NTPase"
FT /evidence="ECO:0000259|Pfam:PF07693"
FT REGION 1285..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1580..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1714..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1589..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1772
FT /evidence="ECO:0000313|EMBL:EFB27451.1"
SQ SEQUENCE 1772 AA; 196671 MW; 61F9C8D849CCB591 CRC64;
MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMIAAEQGN LEIVKELIKN
GANCNLEDLD NWTALISASK EGHMHIVEEL LKCGVNLEHR DMGGWTALMW ACYKGRTEVV
ELLLSHGANP SVTGLYSVYP IIWAAGRGHA DIVHLLLQNG AKVNCSDKYG TTPLVWAARK
GHLECVKHLL AMGADVDQEG ANSMTALIVA VKGGYTQSVK EILKRNPNVN LTDKDGNTAL
MIASKEGHTE IVQDLLDAGT YVNIPDRSGD TVLIGAVRGG HVEIVRALLQ KYADIDIRGQ
DNKTALYWAV EKGNATMVRD ILQCNPDTEI CTKDGETPLI KATKMRSIEV VELLLDKGAK
VSAVDKKGDT PLHIAIRGRS RKLAELLLRN PKDGRLLYRP NKAGETPYNI DCSHQKSILT
QIFGARHLSP TETDGDMLGY DLYSSALADI LSEPTMQPPI CVGLYAQWGS GKSFLLKKLE
DEMKTFAGQQ IEPLFQFSWL IVFLTLLLCG GLGLLFAFTV DLNLGIAVSL SLLALLYIFF
IVIYFGGRRE GESWNWAWVL STRLARHIGY LELLLKLMFV NPPELPEQTT KALPVRFLFT
DYNRLSSVGG ETSMAEMIAT LSDACEREFG FLATRLFRVF KTEDTQGKKK WKKTCCLPSF
VIFLFIFGCI IAGITLLAIF RVDPKHLTVN AVLISIASIV GLAFVLNCRT WWQVLDSLLN
SQRKRLHNAA SKLHKLKSEG FMKVLKCEVE LMARMAKTID SFTQNQTRLV VIIDGLDACE
QDKVLQMLDT VRVLFSKGPF IAIFASDPHI IIKAINQNLN SVLRDSNING HDYMRNIVHL
PVFLNSRGLS NARKFLVTST TNGDIPCTDT AGVQEDADRR VSQNSLGEMT KLGSKTALNR
RDTYRRRQMQ RTITRQMSFD LTKLLVTEDW FSDISPQTMR RLLNIVSVTG RLLRANQISF
NWDRLASWIN LTEQWPYRTS WLILYLEETE GIPDQMTLKT IYERISKNIP TTKDVEPLLE
IDGDIRNFEV FLSSRTPVLV ARDVKTFLPC TVNLDPKLRE IIADVRAARD QINIGGLAYP
ALPLHEAPPR PPSGYSQPPS VCSSSTSFNG PFGGGVVSPQ PHSSYYSGMT GPQHPFYNRP
FFAPYLYTPR YYPGGSQHLI SRPSVKTNLP RDQSNGLEVI KEDAAEGLPS PTDSLRGSGP
ASGAMISLNS MNVDAVCEKL KQIEGLDQSM LPQYCATIKK ANINGRVLAQ CNIDELKKEM
SMNFGDWHLF RSTVLEMRNA ENQVVPEDPR LLSENNSGPV PHGESARRPS HNELPHTELS
NQTPYTLNFS FEELNTLGLD EGAPRHSNLS WQSQTRRTPS LSSLNSQDSS IEISKLTDKV
QAEYRDAYRE YIAQMSQLEG GTGSTTISGR SSPHSTYYMG QSSSGGSIHS NLEPEKGKDS
EPKQDDGRKS FLMKRGDVID YSSSGVSTND ASPLDPITEE DEKSDQSGSK LLPGKKSSER
SSLFQTDLKL KGGGLRYQKL PSDEDESGTE ESDNTPLLKD DKDKKVEGKV ERISKSPEHS
AEPIRTFIKA KEYLSDALLD KKDSSDSGVR SSESSPNHSL HNEGADDSQL EKANLIELED
DSHSGKRGIP HSLSGLQDPI IARMSICSED KKSPSECSLI ASSPEENWPA CQKAYNLNRT
PSTVTLNNNS APANRSNQNF DEMEGMRETS QVILRPGSSS NPTAIQNENL KSMTHKRSQR
SSYTRLSKDS SELHAVASSD STGFGEERES IL
//
