ID A0A1S3FFW0_DIPOR Unreviewed; 676 AA.
AC A0A1S3FFW0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Forkhead box protein P2 {ECO:0000256|ARBA:ARBA00040052};
GN Name=Foxp2 {ECO:0000313|RefSeq:XP_012875381.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012875381.1};
RN [1] {ECO:0000313|RefSeq:XP_012875381.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012875381.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR RefSeq; XP_012875381.1; XM_013019927.1.
DR AlphaFoldDB; A0A1S3FFW0; -.
DR GeneID; 105988334; -.
DR CTD; 93986; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd20065; FH_FOXP2; 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; IPR047412; FH_FOXP1_P2.
DR InterPro; IPR001766; Fork_head_dom.
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:SF1; FORKHEAD BOX PROTEIN P2; 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|PROSITE-ProRule:PRU00089};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 465..538
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 465..538
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 75218 MW; E6B216F64E7E62A2 CRC64;
MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQQEAL
QAARQLLLQQ QTSGLKSPKS SDKQRPLQVP VSVAMMTPQV ITPQQMQQIL QQQVLSPQQL
QALLQQQQAV MLQQQQLQEF YKKQQEQLHL QLLQQQHFGQ QQQQQQQLAA QQLVFQQQLI
QMQQLQQQQH LLSLQRQGLI SIPPGQAALP VQSLPQGKYP AEIQQLWKEV TGVHSMEDNG
IKHGGLDLTT NSSSTTSSTT SKASPPITHH SMVNGQSSVL NTRRDSSSHE ETGASHTLYG
HGVCKWPGCE SICEDFGQFL KHLNNEHALD DRSTAQCRVQ MQVVQQLEIQ LSKERERLQA
MMTHLHMRPS EPKPSPKPLN LVSSVTMSKN MLETSPQSLP QTPTTPTAPV TPITQGPSVI
TPASVPNVGA IRRRHSDKYN IPMSSAFIFI EIAPNYEFYK NADVRPPFTY ATLIRQAIME
SSDRQLTLNE IYSWFTRTFA YFRRNAATWK NAVRHNLSLH KCFVRVENVK GAVWTVDEVE
YQKRRSQKIT GSPTLVKNIP TSLGYGAALN ASLQAALAES SLPLLSNPGL INNASSGLLQ
AVHEDLNGSL DHIDSNGNSS PGCSPQPHIH SIHVKEEPVI AEDEDCPMSL VTTANHSPEL
EDDREIEEEP LSEELE
//
