ID F1Q7X5_DANRE Unreviewed; 2708 AA.
AC F1Q7X5; A0A8M1RE46;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Centromere protein F {ECO:0000313|Ensembl:ENSDARP00000115642, ECO:0000313|RefSeq:XP_002665261.2};
GN Name=cenpf {ECO:0000313|Ensembl:ENSDARP00000115642,
GN ECO:0000313|RefSeq:XP_002665261.2,
GN ECO:0000313|ZFIN:ZDB-GENE-041111-205};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000115642};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000115642}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000115642};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000115642, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000115642};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_002665261.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_002665261.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; BX936381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002665261.2; XM_002665215.6.
DR STRING; 7955.ENSDARP00000115642; -.
DR Ensembl; ENSDART00000135517; ENSDARP00000115642; ENSDARG00000055133.
DR Ensembl; ENSDART00000135517.3; ENSDARP00000115642.2; ENSDARG00000055133.10.
DR GeneID; 497403; -.
DR KEGG; dre:497403; -.
DR AGR; ZFIN:ZDB-GENE-041111-205; -.
DR CTD; 1063; -.
DR ZFIN; ZDB-GENE-041111-205; cenpf.
DR eggNOG; ENOG502QVMD; Eukaryota.
DR HOGENOM; CLU_000551_0_0_1; -.
DR OMA; EQPNEQH; -.
DR OrthoDB; 5363462at2759; -.
DR Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000000437; Chromosome 17.
DR Bgee; ENSDARG00000055133; Expressed in proliferative region and 20 other cell types or tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:GO_Central.
DR GO; GO:0001822; P:kidney development; IMP:GO_Central.
DR GO; GO:0051310; P:metaphase chromosome alignment; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0021591; P:ventricular system development; IMP:GO_Central.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
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.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1Q7X5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 1..295
FT /note="Centromere protein Cenp-F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10481"
FT DOMAIN 1707..1845
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 1945..2083
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2562..2606
FT /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT /evidence="ECO:0000259|Pfam:PF10490"
FT REGION 47..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2435..2573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2615..2660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2674..2708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 268..330
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 708..742
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 792..882
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 918..976
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1015..1109
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1145..1277
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1306..1392
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1499..1537
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1655..1759
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1788..1878
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1921..2060
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2103..2232
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2435..2451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2452..2491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2492..2507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2559..2573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2683..2708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2708 AA; 311085 MW; 9F62014444EDDBA4 CRC64;
MSWAVEEWKD GLPAKALQKI QEIEAQLDKL KKERQQKQFQ MDSLEATLQK QKQKMDSEKS
EASALKRENQ SLVESCEHLE KARQKLTHDI QTKEQQVNYL EGQLNSFKKQ TDRLEQEVKK
YKHELERSQT SHASEIQQLS TPQKTFATPA TPNHWQQDSK ITDLQEKYNR EVEERKKLEA
EIKVMHVKLL NQSSVSHKDI ARQQTGSSIF PWQQDQKSSH QSLPVMETPS RRRNGASGMP
WSYDDTPIKP HQQFTSGAPS DTVGSQQMEQ LKNINQDLRS KVSELELRLQ AHEKDMKNQI
NKFSEIQSQL EMAKKDVAEK DKLLNKSRDE LTKATGQYEQ SVSKCSAFEI KLKQVTEEMN
CQRHNAESMH RSLEQKIKDQ ERESQKELAQ LQSSYQALDQ QFTQVKNKTS MEIQQAKKDH
NVLQSEMDKV TALKNRLEKE LEELKQKLLR SEQALQASQV KEAETKKKFE EMQREKNTLN
CQLDQGMKRV KQLEDEKQNT EQILAKNRMM VDDLKVKTQT QNEELTELRK KMDHQSVSSA
QELENLKKTL IEAEAKNMKT QAELQKLVHD VELKENKICA VEKENEELKM TSNSCQKELA
EMKKEYDALL QWKTEKEQLI NNAESNRNEL LAKVADLEKD KDNLSNAHGD LQKKMQDLEN
EKIGLSGQID SLKGELLVKC VELEEKGRVY EELQQQFGET KIKHKKEMDN LNQQITLTQG
KVSELEAKLL QETSKLEGME QAHGQLLAEY ESACILAMSK DSIIEMNKTE IVHLQESFTL
RDQELEKFKV EKDILAKECE DRLAQNKELE QQKLNTETSL MEVLAKFTLL ESDLRCQKDL
NAEIQGKYDE LSKIKEDLVE KVSSLEKREK DLINEVESLL QKNKSLCSLE EQFNCLVAEA
EETRSSLEKV KELQVQTTTE LENQKTIAEN LAIDLEEEKK KALSIKQENT QLKVKQEEIE
NKANDLFEKY ESLQKLHDAV CQENANHLKE ISIVTEALAE KDAMAERIAL IKTELETSNN
LSATLKNSLE NLQTQFDSSV ELISSLEKKL HDMSDEKSLL EISIKELTER HNKESEVYVS
ELETHIKKHK SLEEHISVLE TELQNKSLET KTASEKLEVT TQEMIKLKQD FSLSENKLSV
VTDSNKKVAK ELEDMKQNVF LQEQEMEGLR LALSDLKNQE AAKSCEIETL KEKLQKAQSE
HAKTSETLNE KNINMSKIKV QLEMLQMDLE DNENCINAFD AQVEELQGNV SILEAKLSES
EAQRSNLESK LESVKEDYVK SSLEVSQLSA CLEESQKEQQ SRSVLVAELE SLRVIHEQLK
VSLEQENCKQ ANLEAMYTNL MDQKLKLESE IQELKADTQG SQKQIDQLKQ ANDRLASQIA
EQQIHIEQLQ SEKNLADTLN KEQTSGGNDQ DICEMPFANT SLLPFEEDTA ILGMSSPKGK
HDSQEEPKTP LSAEEDYKDF ALQEQMQNKS SDIEDMSHVL KETVRTMEEQ TAIQIEQLKL
QHATELQSME EQMLNIKNEL EAKLKEEKQH TEILSSQLEA TMQQLQELDI ASSSLLAADT
SQNMGKFASG AQDDLIHHTE QSNSTLGIIT ESEHSNLETE TLKEVLRKRE EELLHLQSQF
EVLESEMVIR KDLCLDMEGK ICKMESEKTN GTDKLASIIQ ENEKLNKHIG ELKEEIDSLT
LQLQTSNCQL TDVMEMMESL EMAKGEWNEK FFQIESELKR VRSEKANLEK HILSMEADIE
EMQEQKQKQE AELETARRTN CSLEQQLNIT MAEGGRLKEE LILCTDERES ETHSLMKLKE
KADLLEKRET DTKELIKELE DDIRVGKKQN EVASDQISVL LKEKEQLIQQ SQNLENKIVL
LNEDNERLLS ELNDIKHNDS FTSRETENMS SKIHSLEDEN VRLSQSLEMS LLEKGEIASR
LISTQEEVAQ MRQGIEKLKV RIESDERKKN HMSQLLKAAQ RKADVLQDNI EKLEREKELS
EQNLEDAILQ AETAKAELEE IQAETQDLTK KIEEMTSELK DLKEEKYKLE QELDQKNKLI
EELQLSIQEA SVKLKSAEEA TLNQEQMIKD FQFKVGAMEE ELRLFQTEVE SKEVKALELA
SHLLSLESEN KEFAQRVLEY ERSQEELHSS NQSLLKDFES KQQELSEENT QLRSQIAELQ
ALSLIREEQD EELQKDKVEL QSTIAQLEEK TQMQSTKMEV MQNSISSLEI NIQQLEGQLD
AMKLMNVELT GKLNSLQESS LHLETQHKQE LCEAKEIQNA LEINQNLLTC QLQESQKQIE
EYKFSLEALA AEKDGLQKSI SVIQESHDVQ LKENNMRHEE NLKRTQQQLE VELNALKENI
LVAEKNAAQY QSDLESIKSQ NAEKDSALKE LQNKWENCQK EKAELDSKIT RLSKEKDSAM
SKINLWMKSC KQLENEKQTL QEELQQQGQE IETLKASKEQ AEGSSSSGAL QEELEELKEA
LEEKSREADD SMDRYCSLMV KVHKLEDSNE SLKNQLKQLS TQTKTPKSRR SLRSETSDLE
NSNPEGVTSG KRQRAIDDTP NKAQEALHNI TKRLKAAAAT PKAKQDDEDF RPEGLPELVQ
KGFADIPVGE MSPFIVRRTT AQRCSPRLAA RTTAVLQSSG SAEHPAQISM QTAEGRTPNT
VQKPKATPSR NVPLLSTLTN SPLKNSCERL APVIEQKISR RSRSFKNSPQ TSEQVTASPK
QNDNCQVQ
//