GenomeNet

Database: UniProt
Entry: F1Q7X5_DANRE
LinkDB: F1Q7X5_DANRE
Original site: F1Q7X5_DANRE 
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
//
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