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Database: UniProt
Entry: H3AGZ6_LATCH
LinkDB: H3AGZ6_LATCH
Original site: H3AGZ6_LATCH 
ID   H3AGZ6_LATCH            Unreviewed;      2955 AA.
AC   H3AGZ6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   18-JUN-2025, entry version 59.
DE   SubName: Full=Centromere protein F {ECO:0000313|Ensembl:ENSLACP00000008917.1};
GN   Name=CENPF {ECO:0000313|Ensembl:ENSLACP00000008917.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000008917.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000008917.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
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DR   EMBL; AFYH01094288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01094289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01094290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01094291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01094292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01094293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01094294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01094295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSLACT00000008986.1; ENSLACP00000008917.1; ENSLACG00000007875.2.
DR   GeneTree; ENSGT00730000111187; -.
DR   HOGENOM; CLU_000551_0_0_1; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000007875; Expressed in pelvic fin and 1 other cell type or tissue.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0000922; C:spindle pole; IEA:TreeGrafter.
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   GO; GO:0051310; P:metaphase chromosome alignment; IEA:TreeGrafter.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:TreeGrafter.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:TreeGrafter.
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; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT   DOMAIN          1..305
FT                   /note="Centromere protein Cenp-F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10481"
FT   DOMAIN          1901..2042
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          2137..2276
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          2807..2849
FT                   /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT                   /evidence="ECO:0000259|Pfam:PF10490"
FT   REGION          205..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1697..1716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2663..2688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2722..2776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2897..2955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..131
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          162..189
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          285..625
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          654..741
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          781..1270
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1298..1395
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1436..1463
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1487..1620
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1849..2051
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        206..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..274
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1697..1706
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2675..2688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2722..2755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2902..2917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2945..2955
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2955 AA;  342120 MW;  A2E473081652BAB6 CRC64;
     MSWAIEEWKE GLPSKALQKI QDFESQLEKL KKERQQKQFQ LESLEAAFQK QKQKVENEKS
     EVTALKRENQ SLVESCDNLE KSKQKISHDL QVKELQVNFL EGQLATCKKQ IEKLEQEMKR
     SKCEIERSQQ PLLLGDLQPC ATPEKNFAVP VAPSRNYNDS KVEELQEKYN KEVEERKRLE
     AELKIMQAKV VNQSQGNVNR RDIARQQASS SVFPWQQEQT PSHAASNSLE TPSRRGCTTS
     HFPWEREETP SMYCQRSAKK TASNSSFNES SSNSPQNDLL KVQNQEELNS KVTELELRLQ
     AQEKEMKTCA NKLQEVQAHF EKAKLELSEK DKALNKYRDE VTKMTTQLDQ SSSKCEVVEQ
     KLKQVSEELI CQRQNTDSAR HTMEQRLKEK EKEYQQELCQ QLHSFQILDQ QFKQMKTELQ
     QAKNDRNTLQ AEIDKLSTMK QRAEKEVEDM KQTLFRTEQT LQAKEKDFKK TVEEVQKEKN
     NLHCQFEQSS RQVHQQEEEL KMTQQHLKQS QSLVEELKSK NIAREVQLLS FKEKLDKQEQ
     SLNTDLENLR QTVADLQKQQ DSAQDILTKR EKEMEEMNNK IITMEKETEE LQNALCLKYN
     ECAELKRETS LLSEWKNKTE NLKNQMLCEK EGMLKEIQEL EKCLESHQYD NERIKVLENE
     KQNLCLQIEN YERLLDCKSA DLESQKQIYE KLRKTAEQAD QKYSKEKENM CLQVIQLTAQ
     ANGLEKKLQL ETNKILKMEQ SYSELCAEYE RATNLAKSKE SVIELKEAEM LNLQNSLSET
     IIDFEKQLAK VNSEKSDLIK EHENAVLGKA VEAENMKLEL EKCQNDIAFS KEQISSLECD
     LKLQKDLNSE LESRCEELMK VKDELEEKLV EVAKNLEIVQ AEAKEERELK ITVSAQQQRV
     DDLLATVQEK EMSIQKLTSE QERKESCLQS LQSSNQLLEV QVQQLNIQSE AQRQEKEDIL
     ASIFSNEKEV ENLAKENEKL KEVIDTLSQE KQVLLEKNSN FANMVKEKEA EVSELSTRRA
     EEHQTILENN VKLESELANL QKKYSCMEET KDELEVQIKE KTEKLEEQER KFNKQCAEYL
     SKMEHYEEAN QSLVKEVEKV QSSLNNKLEE TTQFKERLIV SEKETENLRK KLSDTTEGYK
     ELQEMLRRLQ QENELLNQQN QQLKSSELAK EKTQYGEELR EAMREKESDL SKIQVQLEML
     QMDLEDKEVC IESYSTQIEQ MEATVKKMES ELRESEEQKT IVREEKNSLC KELEATKSKL
     SDALEKEQIL KLCAEHKEQS EKELAAVSQE YKSCQLLKTK LETSLQEVSS KCEELEKMYE
     RMQTEKSELI SELSNLRTQC TTVLDENSGL ADKIKHLENE VNLSKDESTA LHSKLMSLKD
     ENEKLKEWAK QEECEKLKLC NKEIERHLFE VNEKLSCSQK EYDIVQEQYC CAMSKVSELQ
     SLVETLEEEK SVLVAKLEES AEVDKADELQ TQLNMAERKL FDTEIILSKT NVEKAALEAE
     VNILETSLES AQLQLTEQKA QLQHLEQLIL ERETEVMDLK EQLNDFKGNL VSKENNASQT
     EGNLPKEIEE LKILSETYET GIKKLEEQLQ MQKDARNGEI QELSQTLAAT KNELTCLQKQ
     HSSEIDQWQQ KLSSMTLEME TKLAAERQQT EILSTELKGA RIQIQHLDLS SHSLLCAETE
     EDQKEEINEN LQYINSFSKD PQSEPQSNER DGIETENTID ISQENISRLD VETETDSVAD
     NTVECLRATV EFLCLDSNTS THQEDFQETH VVPESCTSQP ENVSSKQEFL SQELEEYKKD
     DILLKEEQHL YSRLDSQQLQ STSQNSACTE LQNVVYKLEE EKSVLSDRIK STNLENQKLS
     ERIKDLEKEL NSMTSEQEVY KARLSDVTEM LHSLEMVKGN WNEKYLEVEN ELKRTRSEKA
     NLEKHILSME ADIEEMQIAK TSLEKEAANS SKCISRLGEQ LSVATADKNQ LSQELESSRE
     IQEELEQISQ NLKEKLEQLA SDKVNYTEFI KVLEAENKKL TKQLEITKFD VEKLSKERNS
     ILEQLDCLEK NVLSDEKGEL QKQFDQRTEE KEVLLNECET LQGKICALEM ENSRLSQSLE
     SSLVEKGEIA SRLNSTQEEV VQMRHGIEKL KVRIESDEKK RHHEAEKLKA SERKADSFQD
     KVEKLQRELQ MSEESLEGMV LEAETVKEEM EKLVTVKQEI SKKLQILETE VNTLSSERDL
     LDKELQQKQL KISELEGSCM DITNLLKKVE EEKLQVMQEH VVSQKALKSE LMELNEKLKI
     CSEELENWRA KEQDWLGQIS GLECEKTELS QQLQQKESSF AELHSANVSL TQDLLASKQE
     LNEQVKANNR LQQEVTDMQQ WKQKISEQLS NVEAEKVSLE KERNQLQTIT TESEQRVQAL
     EAKNFKMQGT IEGLEGSQQL LEDELQSAKL QNSALLEQIQ KITENDSRVR SDLNAANQKI
     EKMQEECNLE RSTLVAQINN AQQQEESYKV QLDLVTSEKE EMKKRLQHLQ NELQISEEKI
     KEERMEYQHQ LQEAEEKQKT LLKEGREKYE AEVHTEREKL ITMRQMLNDH ILEINNLKSA
     KEQLNAALRK AESKLEQLNE KKVEDLKTTI VQLKKEKESA VSKLQLWMRS CKQMEQEKEM
     LLKDIEQQDA LLNKLKKNEK IETDTNADGV SSELEELRET VEEKTREADE SMEKYCNLII
     NYHKLEEANE TLKNRIAFLS SQLKQPGSQD SNSTAKTTPD NPPNSKTGNL KTGKTSPWDR
     SRPCNKRHRT VEPKEDGLEL EKVEATECVS KRIRNGKENG MSRHSAGGDN VEFKPEGLPE
     VVKKGFADIP AGTASPFILR RTTLQRRSPR LAAQKTSPIT QVVQKVALEN QAQNSKTPGG
     SKLQQVKEVS SFSLGSVLGP VASTSGSPLS SVINSPKKTA FQIPSGSAPT RRSRRSPSTR
     KYPEQEEEEE NCNVQ
//
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