ID A0A2K5IGS2_COLAP Unreviewed; 3114 AA.
AC A0A2K5IGS2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 18-JUN-2025, entry version 35.
DE RecName: Full=Centromere protein F {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000015859.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000015859.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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DR RefSeq; XP_011784804.1; XM_011929414.1.
DR RefSeq; XP_011784805.1; XM_011929415.1.
DR STRING; 336983.ENSCANP00000015859; -.
DR Ensembl; ENSCANT00000038795.1; ENSCANP00000015859.1; ENSCANG00000031380.1.
DR GeneID; 105502776; -.
DR KEGG; cang:105502776; -.
DR CTD; 1063; -.
DR OMA; EQPNEQH; -.
DR OrthoDB; 13233at314294; -.
DR Proteomes; UP000233080; Unassembled WGS sequence.
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 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:UP000233080}.
FT DOMAIN 1..307
FT /note="Centromere protein Cenp-F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10481"
FT DOMAIN 1893..2035
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2131..2270
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2313..2452
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2970..3013
FT /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT /evidence="ECO:0000259|Pfam:PF10490"
FT REGION 208..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2889..3114
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..501
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 546..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 1196..1244
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1286..1313
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1549..1646
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1790..1873
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1904..2078
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2107..2544
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 211..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2970..2980
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3033..3057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3079..3089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3114 AA; 357799 MW; 8E622DFAC5852E3B 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
FSASYFSGEQ GVTPSRSTLQ IGKRDANSSF FDNSSSPHLL EQLKVQNQEL RSKINELELH
LQGQEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRATAQY DQASTKCTAL
EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL SRQQRSFQTL DQECIQVKAR
LTQELQQAKN MHNVLQAELD KVTAVKQQLE KNLEEFKQKL CRAEQASQAS QIKEDELRRS
VEEMKKENNL LKSQSEQKTR EVCHLEAELK NVKQCLNQSQ NFAEEMKVKN TSQETMLRDL
HEKINQQENS LTLEKLKLAV AELEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS
ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC LKTQQIKSHE
YNERVRTLEM DRENLSVEIR NLHNVIDSKS VEVETQKLAY VELQQKAEFS DQKHQKEIEN
MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD RCYQDLHAEY ESLRDLLKSR DVSLATNEDH
QRSLLAFDEQ PAMHNSFANI IEDQGSMPSE RSECHLEADQ SPKNSAILQN RVDSLEFSLE
SQKQMNSDLQ KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA
ETLSALENKE KELQLLNGKL ETEQAEIQEL KQSNHLLEDS LKELQLLSET LSLEKKEMSS
IISLNKREIE QLTQENETLK EINASLNQEK MNLIQKSESF ANYIDEREKS ISELSDQYKQ
EKLILLQRCE ETGNAYEALS QKYKAAQEKN SKLECLLNEC TSLCENRKNE LEQLKEAFAK
EHQEFLTKLA FAEERNQNLM LELETVQQDL RSEMTDTQNN SKSETDGLKQ EIMTLKEEQN
KMQKEVNDLL QENEQLMKVM KTKHECQNPE SEPIRNSVKE RESERNQCNF KPQMDLEVKE
ISLDSYNAQL VQLEAMLRNM ELKLQESEKE KECLQHELQI IRGDLETKNL QDMQSQEISG
LKDCEVDAEE RYIPVLHELS TSQNDNAHLE CSLQTAMNKL NELEKICEIL QAEKCELVTE
LNDSRSECIT ATRKMAEEVG KLVNEVKILN EDSGLLHGEL VEDLPGGEFG EQPNEQHPMC
LAPLDESNSY EHLTLSNKEV QIHFAELQEK FSSLQSEHKI LYDQHCQMSS KMSELQTYID
SLKAENLVLS TNLRNFQGDL VKEMQPGLEE GLVPSLSSSC VPDSPGLSSL GDSSFYKALL
EQTGEMSLLN NLEGTVSANQ CSVDEVFCSS LEEENLTKKE TPSAPAKGVE ELESLCEAYR
QSLEKLEEKM ESQGIMKNKE IQELEQLLSS ERQELDCLRK QYLSENEQWQ QKLTSVTLEM
ESKLAAEKKQ TEQLSLELEV ARLQLQGLDL SSRSLLGIDT EDAIQGRNES CDVSKEHTSE
TTERTPKHDV HQICDKDVQQ DLHLDIEKIT ETGAVKLTGE CSGEQYPDTN YETPGEDKTQ
GSSECISELS FSGANASIPM DFPGNQENIQ NLQLRVKETS NENLRLLHVI EERDRKVESL
LNEMKELDSK LHLQEVQLMT KIEACIELEK IVGELKKENS ELSEKLEYFS CDNQELLQRV
ESSEGLNSNL EMRADKSSHE DIDDNVAKVN DSWKERFLVV ENELSRIRSE KANIEHQALS
LEADLEIVQT ERLCLEKDNE NKQKVIVCLE EELSVVTSER NQLRGELDTM SKKNTELDQL
SEKMKEKTQE LESHRSEYLH CIQVAEAEVK EKTELLQTLS SDVSELLKDK THLQEKLQSL
EKDSQALSLT KCELENQIAQ LNKEKELLIK ESESLQTRLN ESDYEKLNIS KALEAALVEK
GEFVLRLSST QEEVHQLRRG IEKLRVRIEA DERKQLHIAE KLKEREREND SLKDKVENLE
RELQMSEENQ ELVILDAENS KAEVETLKTQ IEEMARNLKV FELDLVTLRS EKENLTKQIQ
EKQGQVSELD KLLSSFKSLL EEKEQAEIQI KEESKTAVEM LQNQLKELNE AVAALCGDQE
TMKATEQSLD PPVEEAHQLR NSIEKLRSRL ETDEKKQLCV LEQLKESEHH ADLLKSRVEN
LERELEIARK NQEHAALEAE SSKGEVETLK AKIEGMTQSL RELELDLATI RSEKENLTNK
LQKEQERISE LEIINSSFEN ILREKEQEKV EMKEKSNTAM EMLQAQLKEL NERVTALHND
QEACKAKEQN LSSQVDCLEL EKAQLLQGLD EAKNNNIVLQ SSVNGLIQEV EDGKQKLGKK
DEEISRLKNQ IQDQEQLISK LSQVEGEHQL WKKQNLELGN LTVELEQKIQ VLHSKNASLQ
DTLEVLQGSY KNLENELELT KMDKMSFVEK VNTMTAKETE LQREMHEMAQ KTTELQEELS
GETNRLTGEL QLLLEEIKSS KDQLKELTLE NSELKKSLDC MHKDQVEKEG KVREEIAEYQ
LRLHETEKKH QALLLDTNKQ YEIEIHTYRE KLTSKEECLN SQKLEMDLLK SSKEELNNSL
KATTQVLEEL KKTKMDNLKY VNQLKKENEH AQGKIKLLIK SCKQLEEEKE ILQKELSKLQ
AAQEKQKTGT VVDTKVDELT TEIKKLKEAL EEKTKEADEY LDKYCSLLIS HEKLEKAKEM
LETQVAHLCS QQSKPDSRGS PLLDPVVPGP SPILSAAEKR LSSGQKKASG KRQRSSGIWE
NGRGPTPSTP ETFSKKSKKA VMSGIHPAED TEGTEFEPEG LPEVVKKGFA DIPTGKTSPY
ILRRTTMATR TSPRLAAQKL ALSPLSLGKE NLAESSKPTA GGSRSQKVKV AQQNPVDSDT
ILREPTTKSL PVNNLPERSP TDSPREGLRV KRGRLAPNPK AGLEPKGSEN CKVQ
//
