ID A0A7J7YM17_PIPKU Unreviewed; 669 AA.
AC A0A7J7YM17;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE SubName: Full=Forkhead box P4 {ECO:0000313|EMBL:KAF6362849.1};
GN ORFNames=mPipKuh1_005215 {ECO:0000313|EMBL:KAF6362849.1};
OS Pipistrellus kuhlii (Kuhl's pipistrelle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Pipistrellus.
OX NCBI_TaxID=59472 {ECO:0000313|EMBL:KAF6362849.1, ECO:0000313|Proteomes:UP000558488};
RN [1] {ECO:0000313|EMBL:KAF6362849.1, ECO:0000313|Proteomes:UP000558488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPipKuh1 {ECO:0000313|EMBL:KAF6362849.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6362849.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00089}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6362849.1}.
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DR EMBL; JACAGB010000005; KAF6362849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J7YM17; -.
DR Proteomes; UP000558488; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd20067; FH_FOXP4; 1.
DR FunFam; 1.20.5.340:FF:000005; Forkhead box P1, isoform CRA_f; 1.
DR FunFam; 1.10.10.10:FF:000010; Forkhead box P2 isoform B; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR047414; FH_FOXP4.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR050998; FOXP.
DR InterPro; IPR032354; FOXP-CC.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45796; FORKHEAD BOX P, ISOFORM C; 1.
DR PANTHER; PTHR45796:SF7; FORKHEAD BOX PROTEIN P4; 1.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000558488};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 456..529
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 456..529
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..44
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..669
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 72058 MW; 148FE501400829AF CRC64;
MMVESASETI RSAPSGQNGV GSLSGQADGS GGAGAAGAAG GGAGRDAAAG ADSNGEMSPA
DLLHFQQQQA LQVARQFLLQ QASGLSSPGN NDSKQSASAV QVPVSVAMMS PQMLTPQQMQ
QILSPPQLQA LLQQQQALML QQLQEYYKKQ QEQLHLQLLT QQQAGKQQPK EALGNKQLAF
QQQLLQMQQL QQQHLLNLQR QGLVSLQPSQ APGPLQTLPQ AAVCPTDLPQ LWKGEGAPGQ
PAEDSVKQEG LDLTGTATTA TSFAAPPKVS PPLSHHTLPN GQPTVLTPRR DSSSHEETPG
SHPLYGHGEC KWPGCETLCE DLGQFIKHLN TEHALDDRST AQCRVQMQVV QQLEIQLAKE
SERLQAMMAH LHMRPSEPKP FSQPVTVSAA DSFPDGLVHP PTSAAAPVTP LRPPGLGSAS
LHSGGPARRR SSDKFCSPIS SELAQNHEFY KNADVRPPFT YASLIRQAIL ETPDRQLTLN
EIYNWFTRMF AYFRRNTATW KNAVRHNLSL HKCFVRVENV KGAVWTVDER EYQKRRPPKM
TGSPTLVKNM ISGLSYGALN ASYQAALAES SFPLLNSPGM LNPGSASSLL PLSHDDVGAP
GEPLPSNGSS TPPRLSPPQY SHQVQVKEEP AEAEEDRRPG PPLGPPNPGA AGPAEDKDLE
EELPGEELS
//
