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Database: UniProt
Entry: A0A2K5WNM4_MACFA
LinkDB: A0A2K5WNM4_MACFA
Original site: A0A2K5WNM4_MACFA 
ID   A0A2K5WNM4_MACFA        Unreviewed;      3113 AA.
AC   A0A2K5WNM4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   18-JUN-2025, entry version 31.
DE   SubName: Full=Centromere protein F {ECO:0000313|Ensembl:ENSMFAP00000038721.2};
GN   Name=CENPF {ECO:0000313|Ensembl:ENSMFAP00000038721.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000038721.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000038721.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000038721.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
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DR   STRING; 9541.ENSMFAP00000038721; -.
DR   Ensembl; ENSMFAT00000012978.2; ENSMFAP00000038721.2; ENSMFAG00000038702.2.
DR   VEuPathDB; HostDB:ENSMFAG00000038702; -.
DR   GeneTree; ENSGT00730000111187; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000038702; Expressed in bone marrow and 7 other cell types or tissues.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0097539; C:ciliary transition fiber; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0000940; C:outer kinetochore; IEA:Ensembl.
DR   GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR   GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0051310; P:metaphase chromosome alignment; IEA:Ensembl.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0016202; P:regulation of striated muscle tissue development; IEA:Ensembl.
DR   GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
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; 3.
DR   Pfam; PF10481; CENP-F_N; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT   DOMAIN          1..307
FT                   /note="Centromere protein Cenp-F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10481"
FT   DOMAIN          1892..2034
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          2130..2269
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          2312..2451
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          2968..3012
FT                   /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT                   /evidence="ECO:0000259|Pfam:PF10490"
FT   REGION          208..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1719..1742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2888..3113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          13..131
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          164..191
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          280..685
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          832..873
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          899..996
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1029..1159
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1203..1244
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1286..1313
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1548..1645
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1761..1844
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1910..2077
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        211..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1722..1731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3032..3056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3078..3113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3113 AA;  357597 MW;  FCF23E34A225EDC5 CRC64;
     MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK QKQKVENEKT
     EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ EGQLNSGKKQ IEKLEQELKR
     CKSELERSQQ AAQSADVSLN PCNTPQKIFT TPLTPSQYYS GSKYEDLKEK YNKEVEERKR
     LEAEVKALQA KKASQTLPQT TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQKTPIRRD
     FCASYFSGEQ EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL EQLKVQNQEL RSKINELELR
     LQGQEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY DQASTKCTAL
     EQKLKKLSED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL SRQQRSFQTL DQECIQVKAR
     LTQELQQAKN MHNVLQAELD KVTAVKQQLE KNLEEFKQKL CRAEQASQAS QIKEDELRRS
     VEEMKKENNL LKSQSEQKAR EVCHLEAELK NVKQYLNQSQ NFAEEMKVKN TSQETMLRDL
     QEKINQQENS LTLEKLKLAV AELEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS
     ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC LKTQQIKSHE
     YNERVRTLEM DRENLSVEIR NLHNVIDSKS VEVETQKLAY VELQQKAEFS DQKHQKEIEN
     MCLKTSQLTG QVEDLEHKLQ LLSDEIMDKD RCYQDLHAEY ESLRDLLKSK DASLVTNEDH
     QRSLLAFDEQ PAMHNSFANI IEEQGSMLSE RSECHLEADQ SPKNSAILQN RVDSLEFSLE
     SQKQMNSDLQ KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA
     ETLSALENKE KELQLLNDKL ATEQAEIQEL KQSNHLLEDS LKELQLLSET LSLEKKEMSS
     IISLNKREIE ELTQENETLK EINASLNQEK MNLIQKSESF ANYIDEREKS ISELSDQYKQ
     ENLILLQRCE ETGNAYEDLS QKYKAAQEKN SKLECLLNEC TSLCENRKNE LEQLKEAFAK
     EHQEFLTKLA FAEERNQNLM LELETVQQDL RSEMTDTRNN SKSETDGLKQ EIMTLKEEQN
     KMQKEVNDLL QENEQLMKVM KTKHECQNLE SEPIRNCVKE RESERNQCNF KPQMDLEVKE
     ISLDSYNVQL VQLEAMLRNM ELKLQESEKE KECLQHELQI IRGDLETRNL QDMQSQEISG
     LKDCEVDAEE RYISVLHGLS TSQNDNEHLE CSLQTAMNKL NELEKICEIL QAEKCELVTE
     LNDSRSECIT ATRKMAEEVG KLVNEVKILN DDSGLLHGEL VEDIPGGELG EQANEQHPMC
     LAPLDESNSY EHLTLSNKEV QMHFAELQEK FSSLQSEHKI LHDQHCQMSS KMSELQTYID
     SLKAENLVLS TNLRNFQGDL VKEMQPGLEE GLVPSLSSCV PDSPSLSSLG DSSFYKALLE
     QTGEMSLLNN LEGTVSANQC SVDEVFCSSL LEENLTKKEM PSAPAKGVEE LESLCEAYRQ
     SLEKLEEKME SQGIMKNKEI QELQQLLSSE RQELDCLRKQ YLSENEQWQQ KLTSVTLEME
     SKLAAEKKQT EQLSLELEVA RLQLQGLDLS SRSLLGIDTE DAIQGRNESC NISKEHTSET
     TERTPKHDVH QICDKDVQQD LRLDIEKITE TGAVKLTGEC SGEQSQDTNC KTPGEDKSQG
     SSECISELSF SGANASVPMD ILGNQENIQN LQLRVKETSN ENLRLLHVIE ERDRKVENLL
     NEMKELDSKL HLQEVQLMTK IEACIELEKL VGELKKENSD LSEKLEYFSC DNQELLQRVE
     SSEGLNSNLE MHADKSSHED IEDNVAKVND SWKERFLDVE NELSSIRSEK ANIEHQALSL
     EADLEIVQTE KLCLEKDNEN NQKVIVCLEE ELSVVTSERN QLRGELDTMS KKIMELDQLS
     EKMKEKTQEL ESHRSEYLHC IQVAEAKVKE KTELLQTLSS DVSELLKDKT HLQEKLQSLE
     KDSQALSLTK CELENQIAQL NKEKELLVKE SESLQARLNE SDYEKLNVSK ALEAALVEKG
     EFALRLSSTQ EEVHQLRRGI EKLRVRIEAD ERKQLHVAEK LKERERENDS LKDKVENLER
     ELQMSEENQE LVILDAENSK AEVETLKTQI EEMARSLKVF ELDLVTLRSE KENLTKQIQD
     KQGQVSELDK LLSSVKSLLE EKEQAEIQIK EESKTAVEML QNQLKELNEA VAALCGDQET
     MKATEQSLDP SVEEAHQLRN SIEKLRARLE TDEKKQLCVL EQLKESEHHA DLLKSRVENL
     ERELEIAGKN QEHAALEAEN SKGEVETLKA KIEGMTQSLR DLELDLATVR SEKENLTNKL
     QKEQERISEL EIINSSFENI LREKEQEKVQ MKEKSNTAME MLQTQLKELH ERVTALHNDQ
     EACKAKEQNL SSQVDCLELE KAQLLQGLDE AKNNNIVLQS SVNGLIQEVE DGKQKLEKKD
     EEISRLKNQI QDQEQLVSKL SQVEGEHQFW KKQNLELGNL TVELEQKIQV LQSKNTSLQD
     TLEVLQSSYK NLENELELTK MDKISFVEKV NTMTAKETEL QREMHEMAQK TVELQEELSG
     EKNRLTGELQ LLLEEIKSSK DQLKELTLEN SELKKSLDCM QKDQVEKEGK VREEIAEYQL
     LLHEAEKKHQ ALLLDTNKQY EIEIHTYREK LTSKEECLTS QKLEMDLLKS SKEELNNSLK
     ATTEALEELK KTKMDNLKYV NQLKKENERA QGKIKLLIKS CKQLEEEKEI LQKELSKLQA
     AQEKQKTGTV MDIKVDELTT EIKELKEALE EKTKEADEYL DKYCSLLISH EKLEKAKEML
     ETQVAHLCSQ QSKPDSRGSP LLDPVVPGPS PILSAAEKRL SSGQKKASGK RQRSSGIWEN
     GRGPTPSTPE TFSKKSKKAV MSGIHPAEET EGTQFEPEGL PEVAKKGFAD IPTGKTSPYI
     LRRTTMATRT SPRLAAQKLA LSPLSLGKEN LAESSKPTAG GSRSQKVKVA QQSPVDSDTI
     LREPTTKSLL VNNLPERSPT DSPREGLRVK RGRLAPDPKV GLEPKGSENC KVQ
//
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