ID W5NJ32_LEPOC Unreviewed; 2869 AA.
AC W5NJ32;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Centromere protein F {ECO:0000313|Ensembl:ENSLOCP00000020641.1};
GN Name=CENPF {ECO:0000313|Ensembl:ENSLOCP00000020641.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020641.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020641.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01027781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015207576.1; XM_015352090.1.
DR Ensembl; ENSLOCT00000020677.1; ENSLOCP00000020641.1; ENSLOCG00000016707.1.
DR GeneID; 102695567; -.
DR KEGG; loc:102695567; -.
DR CTD; 1063; -.
DR GeneTree; ENSGT00730000111187; -.
DR OrthoDB; 5363462at2759; -.
DR Proteomes; UP000018468; Linkage group LG1.
DR Bgee; ENSLOCG00000016707; Expressed in embryo and 11 other cell types or tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:InterPro.
DR GO; GO:0070840; F:dynein complex binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR Gene3D; 1.10.287.1490; -; 2.
DR InterPro; IPR043513; Cenp-F.
DR InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd.
DR InterPro; IPR019513; Centromere_CenpF_leu-rich_rpt.
DR InterPro; IPR018463; Centromere_CenpF_N.
DR PANTHER; PTHR18874:SF10; CENTROMERE PROTEIN F; 1.
DR PANTHER; PTHR18874; CMF/LEK/CENP CELL DIVISION-RELATED; 1.
DR Pfam; PF10490; CENP-F_C_Rb_bdg; 1.
DR Pfam; PF10473; CENP-F_leu_zip; 2.
DR Pfam; PF10481; CENP-F_N; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 1..294
FT /note="Centromere protein Cenp-F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10481"
FT DOMAIN 1828..1968
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2066..2201
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2713..2758
FT /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT /evidence="ECO:0000259|Pfam:PF10490"
FT REGION 125..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2638..2723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2758..2801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2815..2869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 309..446
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 475..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 542..674
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 707..734
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 763..794
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 820..983
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1090..1292
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1504..1599
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1748..2633
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 127..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2638..2654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2655..2669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2679..2696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2815..2836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2837..2858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2869 AA; 329438 MW; 129113DEB8BD3956 CRC64;
MSWAVEEWKD GLPGKALQKI QEIESQLDKL KKERQQKQFQ LETLEAALQK QKQKMEVEKN
EVTALKRENQ SLVESCDNLE KTRQKVTHEL QVKEQQVNYL EGQLAASKKQ IEKLEQEIKR
NKVELDRSQQ SVAAGDQQSY GTPQKSFATP ATPSQKLHDS KLEEIQEKYY KEVEERQKLE
AELKVMQIKL LNQSSVSHKD IARQQTQSSI FPWQQDQTPS RQSHSFLETP LKRGIGASSF
LWDHEETPYK RNSRSTLHDN AGSSQQSEQL KAMNQDLKAK VSEMELCLQA QDKDMKNHVN
KLHEIQISFE KAKMELAEKD KNLNKCRDEL TRVTGQYEQA TSKCAALEQK LKQLSEELNC
QRHNADSSRL ALEQKMKDHE KEYQKELVHQ QNSLRSLDQE FHQMKSKMSQ ELQLAKSDYN
ALQAEMDKIV QQKHHLEKCV EDLKQKLCRT EQILQTSQTK ENEMRKNFEG IQKEKNSLSC
QFEQSSRRMT QVEEELKAAK QNLKQSHSLM EDFKAKTLAQ SEELKCLQVK MENQDQSSAL
ELENMKKVVS DLEKIKEMAQ NQIKKQEQDL EQMKSKQTVM EKEQQALQIA LDSKQNECTE
LKKENDFLSK WKTEKEDLVN SVEIEREHML NKIGDLEKNI EMIQNVSCGL NEKVNSLKSE
KEDLTEQTDS LKGELLKKCM ELEEKSKVYE ELQKSSEEDN LKYTKDLENG NLQITELQAK
ASNLEMKLQL ETCRADKMEQ SYNEFILQYE SACNLAKSKE SVIDLKEEEI LHLKNTISQA
LSQHEQQLEK LSTERCSLLK AHEESLYEKE QAFQQASLNF EKSQQEAALL KDQVSSLESS
LKLQKNLNVE LQSKCEELSK VKGELQIKFS QAEESQKELL QELSLLSEQA SSSVSLQEQC
NLFSEAAKEK EASLQNLTKE LESKVTQLQV FKASVEELKN SVEETGLKSS RLEDENAQLK
ARLQTLEEEI GQVTVRSRSL EDSHNILCQE KDSLLKEIYR LNDLVGEKED ASAEMIQSYK
NELGVANELC AQLKSSLEDL QGKYTSVMEL NSTLEICLRE ESYKKFSQDK ELVELQKKYR
DESEEHAAML KGYEDKQMQL LQEKDALQSQ LQNKSNEVEN TMEKLEMAEN EISQLKKNNV
ICNEELKKMQ DCYRMITQEK ETLKQQVSTH QSDLESLKSV LLISENCIVE RNLKIEMLEA
KLSAAELKQI EISDRLKEKE VQLNKINVQL EMLQMDLEDN QKNCVCEGSE FEQLKNSLGI
LEGKLKENEL QKSSLQKTLH SAREELAEKE REALLTKAVL EDAQKSSKSM NESYIALAAK
VEMLQATNEK AQFSLDEEVK RYTVLENSYS NWVAEKTELK TKLTESQHQC LNALEENKIL
IKNSSFSFEE TLLRLQEENQ TLKSMLDRQN DKSKCSEELK MQNKDLESCQ ISSECQYDSL
SNLSKQQCFI DQLQAEKALL TQETIHKKLK ADTSELQTCV HDDGPLCRTH NDLCPLESEL
LKKSEELKML SQTYEDSLKT LKEQMDRQKE VSKEEIEELK AALSRVQHEL DQLQQHHLDE
VKVWQQKLVD LNAEMETRLA EEKQNCEFLS SELETARLQM QCLDLSSRSL LCSENDEEFH
QANTEKGGIK CLSPEKDPEE LKTEILESTE QQYNPNVNEE VEHSVAGSNT AINDTFDGLL
SGVEILTLEN DSSVVEDDLH TTKTSTENVQ VSVLQECLKD LEENNEKGNL ENDVQTLCSQ
LDLNKVEIIS KTDLFAEMEE KFQKLEKENS NLIQKLSVSV MENQKLDEHV RELDEELNSL
NLQLKTSKLQ LSDVTNLLES LEMAKGGWDE KLLQIESDLK RTQSEKANLE KHILSLEAEF
EEIQQKNEKL QKELDLSKKA IESLEQQLKG AVDERNQLHQ DLSLCTEEKE EVERDFQRWK
GKAEQLEKDN VDAKEFIKIL EKDITNQKCQ RELANSSLDN LQSEKDKLLQ QLQNMEQTVV
LLKEENQELL RVLNEVKEEK TSVSTECEVL ESKVQELGNE NSKLSQLLES SLCEKGEIAS
KLNSTQEEVT QMRAGIEKLR VRIEADEKKK RHVGEQLKAS QRKADVLVDK IEKLEREREM
TETSLEDAIL QAESAKAELE ILAPEKKELT KSIECKVQEI NDLKAVKEKL EKELLCKNEQ
VVQLQISSSA ASERLEVLEK EVKVAKTNQE NAAKTCESKV KEISNELQLS KDEVMSMQLK
ENDLNSQLSC FKNENIMLSQ KLQEAEKTLA DVKSLNQVLS QDCEAKQLKL IESTGVNDQL
QQEVVDLQVL RQTAEEKLTS LKVEKEELEK EKVCLQTIVT EWEQRSQIMS TKAEVMQNTI
NSLEDDLKQH KHNLESVKVI NLELTEKVSM LQENCFKLQN EINDCLKKAE RMQKDFELER
NSLSVELQSS RQEVESYKLS LEISASEKED LKKNLALSQD NIALYEQKIK EMEGACQEKL
ALAQERYEGE KQALKRELTG AEQKNIDCFT EINDLKSSKE ELNLALKESE IKLEQCTKIK
GDLNSTIMRL TKEKDSALNK LQLWMKSCKQ LEQEKEALLK ENQQQELLAK RNASLEEVGA
LQSEIQELKE ALDEKSKEAD ESMEKYCNIM ISLHKLEEAN EILENKLALM SSQVLPLKGS
KTAGSTPKTS DSPTEKNPKS AERRRASPRG QSRLSAKRQR ASGAEEETDP AKAQEHLSSS
KRVCGQVNPQ TAQRTEEEDE EFRLEGLPEV VKKGFADIPS GEMSPYIIRR TTVQRCSPRL
AAKRSPTLQT AQKGLENAVP GQKPTAEGSK NKKQMHKVES LPAPVVISAG KLLSTITNSP
TKQGFESPVS NMEARRSKRS LSSKKSPEQM EKRRQIVASE NSSENCQVQ
//
