ID A0A6I8P3D7_ORNAN Unreviewed; 2988 AA.
AC A0A6I8P3D7;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Centromere protein F {ECO:0000313|Ensembl:ENSOANP00000047483.1};
GN Name=CENPF {ECO:0000313|Ensembl:ENSOANP00000047483.1};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000047483.1, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000047483.1}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000047483.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSOANT00000064803.1; ENSOANP00000047483.1; ENSOANG00000008524.3.
DR GeneTree; ENSGT00730000111187; -.
DR InParanoid; A0A6I8P3D7; -.
DR OMA; EQPNEQH; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000008524; Expressed in fibroblast and 7 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: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 Gene3D; 1.10.287.1490; -; 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.
DR SUPFAM; SSF57997; Tropomyosin; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279}.
FT DOMAIN 1..303
FT /note="Centromere protein Cenp-F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10481"
FT DOMAIN 1939..2058
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2177..2322
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2838..2882
FT /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT /evidence="ECO:0000259|Pfam:PF10490"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1749..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2766..2849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2877..2988
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 269..434
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 503..623
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 652..774
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 845..900
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 926..1016
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1049..1136
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1173..1371
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1598..1695
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1877..1911
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1943..2033
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2062..2480
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2534..2579
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2623..2732
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 133..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1767..1788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2817..2841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2877..2924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2939..2954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2966..2988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2988 AA; 342492 MW; 4AD06DCE9A3EB32D CRC64;
MSWAVEEWKE GLSTRALQKI QELESQLDKL KKERQQRQFQ LESLEAALQK QKQKVENEKT
EAATLKRENQ SLMEMCDNLE KTRQKISHDL QVKESQVNYQ EGQLNSSKRQ IEKLELELKR
CKSELERGQQ ALLPGDSSLS VSSTPQKSFT APLTPSQYHN DAKYKELQEK YNKEVEERKR
LEAEVKVMQV QKMNQALPQS TVNHREIARH QTSSSVFSWQ QEKTPNRFSA NIQETPLKRG
FSACHFPWEQ EETPNKPERK EANTSICDNS CNSQLMDQLK AQNQELRSEV SELERLLQGQ
EKDMKGHMNK LQEIQIQLEK TRLELMEKDK TLSKSRDELT RTAAQLDQAL DKGTMLEQKM
KKMSEELSCQ RQNAESARCS LEQKIKEKEK EYQEELSRQQ RSLQGLDQEL TQIKAKLSQE
LQQAKNAHNA LQAEFDKMVS VKLQLEKSSD ELTQKLYRTE QALQASQTQE NDLRRNFEPS
GSTCSSSVKQ PKVREDIEFF ACLEGMKQEK DILRNQTDQK EREVRHLEEE LKETKKCLKQ
SQNFAEEMKD QNASREAMLK TLQEKLTQQE NSLTLEKLKL AVADLEKQRE FSQDLLKKRE
HHIEQLNNKL SRVERESETI MSALGLKEKE CEELKRETVL FSQWKSENEQ LLNQLGADKE
RLQSTINNLE VRLQNQQLKN HEEKERIKIM ENEKESFSVE MKNLQKKMEG KSAELEAQKL
AYAELQQKAE CSDRKYKKEI ENMSWKIAQL TGQVEELEEK LQSESNEALE RAQRYHELQA
DYEKISKLVK FKDDSALMTA DDCRPLLVFE QQSMMNNSPT DVVIGEKQSF FLGETGQSTD
LSLGVGKYEK NVALLQEKVS SLEISLETQK QLNIDLQTQC EELVKIKAEI EENLIKAEQM
HQSFVAETNQ RVSKLQEDTS AQQNVVNEAL VALEDREKQL QTLNEKLETG QVEIQDLKTN
NKLLEDSIKQ LHLVSETLSS EKKEMSGILT LKEEEIEDLT KENGNLKQLN ATLHQEKINL
VQENLTISNC VAEREKNISE LSKSYNEQRL ALCQRCEEAE KDLRIIQEKY KSLEERNMNL
ECVANEHSSN LEVRKYELEQ LESALAKERK EYQCRLVSSE EKNRNLIQEL DRVQGAFKAE
IEEIQNVSQV EISSLRQDIS DFKALQSTMQ EKHDALLREN EKLMEANQIK DEEQRRELTL
VENLTAEQIK ESVEEKEKEL NQFQVQLEVL QQDLKARDIA VDSYSIKVGV LEAAVKTLEH
RLRESESEKE TLQQEMQLIK GELKASDSKF QEVQLKDQSL DLSAYEDSKR EMDEKYASIL
QELSSSQNDN EQLLASLQAT KSKLSKLEKM YEMLQIEKLE LTSALNESKS ECIMAEEVEK
MVNDVKTPIK ENIVCQDDCM EQSGKDDVGE PTGEPELESL KLQGSDVEGS AADYENLKLS
NQKVQMHFVE LQDKFSTLQS EHKILYDQHC TMSSKMSELQ SYINTLKAEN SVLSANLKNI
NPDLVSQVSP TKGDFELGES EPLFSTPSVK EIPSLTSCVE SSFYKNLFDQ TGESSLLTSL
AENSLENQVR ADIELAHCSP GTDNRTKKDI ETDLEMKIKE LETLCQVHQQ SMKKLQDKLE
NQEMMKNDEI QTLKQLLCSE RKELDCLRKQ CSSENEQWQQ KLTSLTLEME SKLAAEKKQT
EHLSLELEVA RLQLQGLDLS SRSLLCARIE DTTLAENESS GLGDSEENIL GPEEEIQKDG
DLQTKIPCDV KQEGSPKNEA GTVLPGIGSG EQTSEIKGGT SPVRNSEPSE CYSELSFCSQ
ETSLAPMDFL ENQVSIQNMQ VKHIPNENLN LLQDAEESDK KEDKLLSEIK ELDPKMDLQK
QELTAKSGSH RELAKLVLLL EREKSGLNEK VESLSCENQQ LSHKVAVLEK LNSELEICEV
RVADVTAIND DIAVAERVWK EKCLEIEKEL KRVKSEKANV ENHALTMESD FEELQTQRRN
LENDNENKRE TITSLQEQLS VITSERNQLT EELNALSEEK AIVGQDCEKL KEKIKDFETS
EEESIRHIQR VESEVKEKTV LVQALSSDIN HLSRDKDCLQ SQLQNLDKTM QAFILEKEEL
QKQTKQLNEE KELLLQELET VQTKLSSSEG EIVKLSTSLK GSQIEKGEIA ARLNSTQEEV
HQMRNGIEKL KMHIEADEKE KQHITGKLKE SERKADSLQD KIEALERQLQ MAEENQEAMI
LDAETAKMEA ETLKTKIEEL TGRLQGLELE FGALRLEKEN VIEEKETIAK DLQEKQDRMS
ELESCNSSFE KLLENKEQEI VRMEEESKNA IELLQVQLKD LKDKIETLLS EHKAYKVTEH
DLISQVDDLE RDKVQLLQQL EETQSNNASL DLSLKDLIQE LEGHKQKLGE KMAENEVLLI
QVKDAEQLSL KLSQIENERD LWEKERVDLQ NRTMELEHKN QVLSKNETLR DTLEALQSSY
KNLENVLELT KAEKLALLEK VNAMTENNTI LQRKMSDTIQ NMTVLQEEFT GEKNGLIEKV
MVMEKQAEMN KVQIDKITLE NSNLKKSLDC VQKELKEKEV KMAEEITEYQ SRLNEADKKH
QAILMDANEQ HKIEIQAYQD KLNSTDQCLN LQRLEMNILR TSKEELTHSL KTTNQVLEEL
QKTKVDNLKY VAQLKKENDS IRGKLQMLLK SCKQLEKEKG ALQKEMTERE ALQKQKQSPA
ASVRLEELMA QLKDLKEAFE EKSKEADENL DKYCSLIVNY NKLEEANEML KTQVFLLNSQ
LSQPVKRTLR SSPSQCAGHA AKSPVHLDGE KTTPKGGNKL SGKRSRPHGT KDSFGGSEPC
TPETSSKRLR KGMTPSLRSS DHSDCELPGL PEIVQKGFAD IPTGKTSPYV LRRTTLPTRT
SPRLAAQKLS PSTQCSQKSP LKNLVETSKP TAGGSRSQKV TEAQAHTAGL LAARMGSTGR
SPLSVNNLSK KISAGSPRET LKAKKGRPAT NQQLSSEPNQ QDENCRVQ
//
