ID A0A3Q2H077_HORSE Unreviewed; 1775 AA.
AC A0A3Q2H077;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Kinase D interacting substrate 220 {ECO:0000313|Ensembl:ENSECAP00000026274.2};
GN Name=KIDINS220 {ECO:0000313|Ensembl:ENSECAP00000026274.2,
GN ECO:0000313|VGNC:VGNC:19391};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000026274.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000026274.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000026274.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000026274.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000026274.2};
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 Ensembl; ENSECAT00000054298.2; ENSECAP00000026274.2; ENSECAG00000019263.4.
DR VGNC; VGNC:19391; KIDINS220.
DR GeneTree; ENSGT00940000156714; -.
DR Proteomes; UP000002281; Chromosome 15.
DR Bgee; ENSECAG00000019263; Expressed in brainstem and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2H077; baseline.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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:UP000002281};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 525..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..707
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 137..169
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 170..202
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 203..235
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 236..268
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 REPEAT 335..367
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 368..391
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 441..953
FT /note="KAP NTPase"
FT /evidence="ECO:0000259|Pfam:PF07693"
FT REGION 1086..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1582..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1718..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1775 AA; 196891 MW; 0963ABA4D8F9B710 CRC64;
MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMIAAEQGN LEIVKELIKN
GANCNLEDLD NWTALISASK EGHVHVVEEL LKYGASVEHR DMGGWTALMW ACYKGRTEVV
ELLLSHGANP SVTGLQYSVY PIIWAAGRGH ADIVHLLLQN GAKVNCSDKY GTTPLVWAAR
KGHLECVKHL LAMGADVDQE GANSMTALIV AVKGGYTQSV KEILKRNPNV NLTDKDGNTA
LMIASKEGHT EIVQDLLDAG TYVNIPDRSG DTVLIGAVRG GHVEIVRALL QKYADIDIRG
QDNKTALYWA VEKGNATMVR DILQCNPDTE ICTKDGETPL IKATKMRNIE VVELLLDKGA
KVSAVDKKGD TPLHIAIRGR SRRLAELLLR NPKDGRLLYR PNKAGETPYN IDCSHQKSIL
TQIFGARHLS PTETDGDMLG YDLYSSALAD ILSEPTMQPP ICVGLYAQWG SGKSFLLKKL
EDEMKTFAGQ QIEPLFQFSW LIVFLTLLLC GGLGLLFAFT VDLTLGIAVS LSFLALLYIF
FIVIYFGGRR EGESWNWAWV LSTRLARHIG YLELLLKLMF VNPPELPEQT TKALPVRFLF
TDYNRLSSVG GETSMAEMIA TLSDACEREF GFLATRLFRV FKTEDTQGKK KWKKTCCLPS
FVIFLFIFGC IIAGITLLAI FRVDPKHLTV NAVLISIASV VGLAFLLNCR TWWQVLDSLL
NSQRKRLHNA ASKLHKLKSE GFMKVLKCEV ELMARMAKTI DSFTQNQTRL VVIIDGLDAC
EQDKVLQMLD TVRVLFSKGP FIAIFASDPH IIIKAINQNL NSVLRDSNIN GHDYMRNIVH
LPVFLNSRGL SNARKFLVTS TTNGDIPCSD TAGIQEDADR RVSQNSLGEM TKLGSKTALN
RRDTYRRRQM QRTVTRQMSF DLTKLLVTED WFSDISPQTM RRLLNIVSVT GRLLRANQIS
FNWDRLASWI NLTEQWPYRT SWLILYLEET EGIPDQMTLK TIYERISKNI PTTKDVEPLL
EIDGDIRNFE VFLSSRTPVL VARDVKTFLP CTVNLDPKLR EIIADVRAAR DQINIGGLAY
PPLPPLPLHD SHPRPPSGYS QPPSVCSSST SFNGPFGGGV VSPQPHSSYY SGMTGPQHPF
YNRPFFAPYL YTPRYYPGGS QHLISRPSVK TSLPRDQSNG LEVIKEDAAE GLSSPTDSSR
GSGPASGTVS LNSMSVDAVC EKLKQVEGLD QSMLPQYCTT IKKANINGRV LAQCNIDELK
KEMNMNFGDW HLFRSTVLEM RNAENQVVPE DPRLLSESTS GPVPHGEAAR RSSHNELPHT
ELSSQAPYTL NFSFEELNTL GLDEGAPRHS NLSWQSQTRR TPSLSSLNSQ DSSIEISKLT
DKVQAEYRDA YREYIAQMSQ LEGGTGSATI SGRSSPHSTY YMGQSSSGGS IHSNLEPEKG
KDSEPKQDDG RKSFLMKRGD VIDYSSSGVS TNDASPLDPI TEEDEKSDQS GSKLLPVKKS
SERSSLFQTD LKLKGSGLRY QKLPSDEDES GTEESDNTPL LKDDKDKKAE GKVERVSKSP
EHSAEPIRTF IKAKEYLSDA LLDKKDSSDS GVRSNESSPN HSLHNEAADD SQLEKANLIE
LEDDSHGGKR GMPHSLSGLQ DPIIARMSIC SEDKKSPSEC SLIASSPEEN WPACQKAYNL
NRTPSTVTLN NNSAPANRAN QNFDEMEGIR ETSQVILRPG SSSNPTAIQN ENLKSMTHKR
SQRSSYTRLS KDSSELHAVA SSDSTGFGEE RESIL
//
