ID E1BMF4_BOVIN Unreviewed; 1781 AA.
AC E1BMF4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Kinase D interacting substrate 220 {ECO:0000313|Ensembl:ENSBTAP00000053227.3};
GN Name=KIDINS220 {ECO:0000313|Ensembl:ENSBTAP00000053227.3,
GN ECO:0000313|VGNC:VGNC:30579};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000053227.3, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000053227.3, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053227.3,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000053227.3}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053227.3};
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 SMR; E1BMF4; -.
DR STRING; 9913.ENSBTAP00000053227; -.
DR PaxDb; 9913-ENSBTAP00000053227; -.
DR Ensembl; ENSBTAT00000061437.3; ENSBTAP00000053227.3; ENSBTAG00000007963.7.
DR VEuPathDB; HostDB:ENSBTAG00000007963; -.
DR VGNC; VGNC:30579; KIDINS220.
DR eggNOG; KOG0502; Eukaryota.
DR GeneTree; ENSGT00940000156714; -.
DR HOGENOM; CLU_001438_2_0_1; -.
DR InParanoid; E1BMF4; -.
DR OMA; TGHDYLK; -.
DR TreeFam; TF344032; -.
DR Reactome; R-BTA-170984; ARMS-mediated activation.
DR Reactome; R-BTA-9696270; RND2 GTPase cycle.
DR Reactome; R-BTA-9696273; RND1 GTPase cycle.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000007963; Expressed in occipital lobe and 109 other cell types or tissues.
DR ExpressionAtlas; E1BMF4; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IBA:GO_Central.
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:UP000009136};
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 692..712
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 1184..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1781 AA; 197399 MW; F6528E2F37DA3C49 CRC64;
MSVLISQSVI NYVEEENIPA LKALLEKCKD VDERNECGQT PLMIAAEQGN LEIVKELIKN
GANCNLEDLD NWTALISASK EGHLHVVDEL LKCGASLEHR DMGGWTALMW ACYKGRTEVV
ELLLSHGANP SVTGLYSVYP IIWAAGRGHA DIVQLLLQNG AKVNCSDKYG TTPLVWAARK
GHLECVKHLL AMGADVDQEG ANSMTALIVA VKGGYTQSVK EILKRNPNVN LTDKDGNTAL
MIASKEGHTE IVQDLLDAGT YVNIPDRSGD TVLIGAVRGG HVEIVRALLQ KYADIDIRGQ
DSKTALYWAV EKGNATMVRD ILQCNPDTEI CTKDGETPLI KATKMRNIEV VELLLDKGAK
VSAVDKKGDT PLHIAIRGRS RKLAELLLRN PKDGRLLYRP NKAGETPYNI DCSHQKSILT
QIFGARHLSP TETDGDMLGY DLYSSALADI LSEPTMQPPI CVGLYAQWGS GKSFLLKKLE
DEMKTFAGQQ IEPLFQFSWL VVFLTLLLCG GLGLLFAFTV DLNLGIAVSL SFLAVLYIFF
IVIYFGGRRE GESWNWAWVL STRLARHIGY LELLLKLMFV NPPELPEQTT KALPVRFLFT
DYNRLSSVGG ETSMAEMIAT LSDACEREFG FLATRLFRVF KTEDTQGKKK WKKTCCLPSF
VIFLFIFGCI IAAITLLAIF RVDPKHMTVN AVLISIASIV GLAFVLNCRT WWQVLDSLLN
SQRKRLHNAA SKLHKLKSEG FMKVLKCEVE LMARMAKTID SFTQNQTRLV VIIDGLDACE
QDKVLQMLDT VRVLFSKGPF IAIFASDPHI IIKAINQNLN SVLRDSNING HDYMRNIVHL
PVFLNSRGLS SARKFLVTST TNGDVPCSDN TGMQEDADRR VSQNSLGEMT KLGSKTALNR
RDTYRRRQMQ RTITRQMSFD LTKLLVTEDW FSDISPQTMR RLLNIVSVTG RLLRANQISF
NWDRLASWIN LTEQWPYRTS WLILYLEETE GIPDQMTLKT IYERISKNIP TTKDVEPLLE
IDGDIRNFEV FLSSRTPVLV ARDVKTFLPC TVNLDPKLRE IIADVRAARD QINIGGLAYP
PLPLHEPPPR PPSGYSQPAS VCSSSTSFNG PFGGGVVSPQ PHSSYYSGMT GPQHPFYNRP
FFAPYLYTPR YCPGGSHHLI SRPSVKTNLP RDQSNGLEVI KEDAAEGLSS PTDSSRPCDS
GFNKQRQGSG PASGTIPLNS MNVDAVCEKL KQIEGLDQSM LPQYCATIKK ANINGRVLAQ
CNIDELKKEM NMNFGDWHLF RSTILEMRNA ENQVVPEDPR LLSENSSSVP HGEPARRSAH
SELPHTELSS QAPYTLNFSF EELNTLGLDE GAPRHSNLSW QSQTRRTPSL SSLTSQDSSI
EISKLTDKVQ AEYRDAYREY IAQMSQLEGG TGSTTMSGRS SPHSTYYMGQ SSSGGSIHSS
LEPEKGKDSE PKQDDTRKSF LMKRGDVIDY SSSGVSTNDA SPLDPITEED EKSDQSGSKL
LPGKKSSERS SLFQTDLKLK GGGLRYQKLP SDEDESGTEE SDNTPLLKDD KDKKAEGKAE
RALKSPEHSA EPIRTFIKAK EYLSDALLDK KDSSDSGVRS NESSPNHSLH NEAADDSQLE
KANLIELEDD PHSGRRGVPH SLSGLPDPLV ARMSICSEDK KSPSECSLIA SSPEENWPAC
HKSYNLNRTP STVTLNNNSA PANRANQNSD ETEGLRETPQ VLLRSGSSSH STALQNENLK
SMAHKRGQRS SYTRLSKDSS ELHAVASSDS TGFGEERESI L
//
