ID M4AL14_XIPMA Unreviewed; 2702 AA.
AC M4AL14;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 18-JUN-2025, entry version 59.
DE SubName: Full=Centromere protein F {ECO:0000313|Ensembl:ENSXMAP00000015158.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000015158.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000015158.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000015158.2};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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DR FunCoup; M4AL14; 1339.
DR STRING; 8083.ENSXMAP00000015158; -.
DR Ensembl; ENSXMAT00000015178.2; ENSXMAP00000015158.2; ENSXMAG00000015125.2.
DR eggNOG; ENOG502QVMD; Eukaryota.
DR GeneTree; ENSGT00730000111187; -.
DR HOGENOM; CLU_236004_0_0_1; -.
DR InParanoid; M4AL14; -.
DR OMA; EQPNEQH; -.
DR Proteomes; UP000002852; 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:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
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 GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
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:UP000002852}.
FT DOMAIN 1..304
FT /note="Centromere protein Cenp-F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10481"
FT DOMAIN 1773..1912
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2010..2150
FT /note="Centromere protein Cenp-F leucine-rich repeat-
FT containing"
FT /evidence="ECO:0000259|Pfam:PF10473"
FT DOMAIN 2621..2665
FT /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT /evidence="ECO:0000259|Pfam:PF10490"
FT REGION 123..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1612..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2442..2463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2529..2637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2656..2702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..196
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 865..966
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1012..1127
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1156..1190
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1493..1527
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1671..1824
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1895..1943
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1986..2388
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 133..146
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2568..2583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2692..2702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2702 AA; 309552 MW; 631728B8C96F99C0 CRC64;
MSWAVEEWKD GLPGKALQKI QEMEVQLDKL KKERTQKQFQ LDSLEAALQK QKQKVDSERT
EISALKRENQ SMIESCDALE KTRQKVVHDL GVKEQQVSYL EGQLNSCRKT IDRLEQELKK
YKTELDRSQP AGSSLLSTSS SDLQTFSTPQ KTFATPAPVA AHRQPDSKLD ELQEKYNHEV
EERRKLESEL KMLQVKLLNQ SSVSHKDIAA RQAGSSIFPW QQQDQVHSLR GQDAMETPLK
RRGASLWDTH EETPIKPNQR MSSSRTVQSP SGSTQQTEQL KSLNQELRGR VSELERNLAA
QEKEIRNQTS KLQELQTHLN QTRKELAERD RELAKAGHEL SQAADRHQQL EAKCSLVEQK
LKQVSEEMSC QRHNAESCRR ALEQKLKDQE RNSQKELAQL QSSHQALDQQ LNQTRTKLTQ
EIQQAKKDHN VLQADMEKTR LQKSQMEREM EEQKQKLLRS EQGLQATQTK EQDLRKKMEE
LQKEKNGVTI QLDRCSRSLT QLEEEKRISE QSLKRTQGLL EDLKAKSEGQ AEELKRLQSK
FEQQTQTAAR ELEHVKKTLS DAEARNDKSQ NELQKQKQES EKLSNKLTVI EQESEELKSN
LRQSRDECQA VKQEHQALLE WKKNKENLIN QTEAAQQELT DKIITLEGKA SRMHEANNEL
QDKISSTEAD KASLSAHIDA LKGELLMRST ELEEKEHQYQ QLQLHVSEAA QKHGKDLENA
GKQLAQLQGQ VKELESRLQR EASRAELAEK TNCELQEEHQ AACDLLRSKD QLLELGRAEV
SQLKDSLAQS AAQQEAQSDS FVKQKAVLLK RCEESISAQA EETERVKLQA EEVQQELLLS
RHKITSMEQI LKVQEQLGAE LQKQIKTTSD KEEELTKTCE EKSEELKRLE EELKDQRSLT
EETEQQIRAA EARIHSVENQ KAELENRLQE MKTEAEILQF SHTERMNALQ EQIVCLEKQV
AANQEEAEEV PVLKNKLDVV NQSLAHLNKS LEASEKSLSC ANEIKADLEV TLSEKVKLIT
ALEDQINNLT EKLRKESESH SSEVEDFINK ERSLKEQLEA TRKSVAAAKE ESSSRRENIR
EMKMTLSAAS RGLEERDNTI KSLKEKLNKA EAEQAKASEL LKEKTVAMSK IKVQLEMLQM
DLEDNELAMT SVGSQAEELK GTIASLEAML EESKAQVSVL ETRLDEVQYQ NSLLETKYVT
AKDELLERSC EITRLEEDAV RRQQLEENVS ALEAKLSQIT EENSKAETEL RQIIQEKESH
LEQVNEERNS LQATLTQSVD EQKRAESEIT QVKAVKAELE ERMSNLSKEI QQLHADVREL
SEQKQEAEGT IDQMAAETQQ TESALRRISE EKAQLDVALS SVSEEKVELQ ERISTLTSEN
GELVCKVKQV EEEKLQLESK FSQISEENVK QQSDMNRLTA EKQQLQSSAE RLQEEMASLR
EESERVQSSL LSAEEERQML REQLNTRDET NHTESRARNQ QFEAEQTALH QKLSILQTEL
AVLQQQYDLL LQQVDQQQRI IQQLTESQKY QNPTGNIPRL EPKDAEDGAE AAEQTKPNPE
LGANVGTSAE SDPLNEQEEA SEKSPDQAAS EAELIVREDA SDQEMINEEE AHKHDAQEIQ
LRQQVSEENC SSSGDLENEK YDASSFQHEI RGMKFSGDES WPVKDVDTEM ISEQQSELKT
LRSEFDLLTS ELQLRAELTS ELEVQVQKLE EKVQAAEEQL STALEEKKSL SDQVTQLLEE
RESLSLQLET SKCQLTDFME MLEGLEMAKG GLDEKFLQQE SELKRVRSEK ANLEQHILGM
ESELESMQAE TSRLTEELEI QRKTCSGREQ QIETLLTETT QLRAELVSCS EDRDELSQSL
GQWRDKVHGL EKTNLETRNL ISILEEDIRV GRKEYEGLQS GMERVKAERE QFLQQVVVLE
EAISKHNREK EGLLNHLHEM EEDHTSTNQN TESMAGKIQA LEGEVCRLSQ SLESSLLEKG
EIASRLNSTQ DEVRQMRTGI EKLQVRIESD ERKKKKMGEL LKAAQRKSDS LQDRIDALER
EKDEFEQNLE EAVLQAEVAK AELEEERTKV EEEKKELNEK LTELSAALDT LTSQKAHLER
ELDMKNVEIE ELKAAKDKLE QGLEKAEVDR REEDRQRQRL EELEKWTREE AERQSVRVGD
LQGQLTELER ENNDLRATFE SLGEEIKDLK TLAQAKEEEI LALEKDKENK AESISLIVAE
KKRLEERNEQ LEKERDDLQS ALVSVNQEKA KADQEKTELD EGRVKLQSKI SLVETEKQNL
QQTVSLLEQE KLRSEAETEE LQSSLLMMEE EKNNLSSALS LLEEEKQQAT EEKERLTQEH
EVLQKTVASM EEELETHKRS MTQLSEQVSE LTSSLARLTK ERDSALSKMN LWMKTCKQLE
QEKQNILNSS GRSSEEFQAE AAQLRAQAEV RKKEVQELKT ALEKKTTEAE ERRQELKQKE
EEVKERAAAL EGVRAEKERE LEEIRKELDE VNALLEEKST EADESIEKYC SLLVKVHKLE
ESNDALKTRL EHLTASQPVN EAKVPPETRR RSVRKSSSKH QEEKMSENTE NLVPTTTPSS
PQGGSPGKRG HKEISDRDSA QEALHNLTKK LKANTATPRG RGEQDDEEFR PEGLPDLVQK
GFADIPLGEA SPYIIRRTTG RRCSPRLAAR QTKPDIKVSS SSSSPTQRCF PLSQSDLSVL
IR
//
