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FOXQ1_RAT
ID   FOXQ1_RAT               Reviewed;         399 AA.
AC   Q63244;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   25-MAY-2022, entry version 150.
DE   RecName: Full=Forkhead box protein Q1;
DE   AltName: Full=HNF-3/forkhead-like protein 1;
DE            Short=HFH-1;
DE   AltName: Full=Hepatocyte nuclear factor 3 forkhead homolog 1;
GN   Name=Foxq1; Synonyms=Hfh1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-65.
RC   STRAIN=Wistar;
RX   PubMed=15326124; DOI=10.1167/iovs.04-0302;
RA   Ahmed F., Torrado M., Zinovieva R.D., Senatorov V.V., Wistow G.,
RA   Tomarev S.I.;
RT   "Gene expression profile of the rat eye iridocorneal angle: NEIBank
RT   expressed sequence tag analysis.";
RL   Invest. Ophthalmol. Vis. Sci. 45:3081-3090(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-399.
RC   STRAIN=Sprague-Dawley; TISSUE=Lung;
RX   PubMed=7683413; DOI=10.1073/pnas.90.9.3948;
RA   Clevidence D.E., Overdier D.G., Tao W., Qian X., Pani L., Lai E.,
RA   Costa R.H.;
RT   "Identification of nine tissue-specific transcription factors of the
RT   hepatocyte nuclear factor 3/forkhead DNA-binding-domain family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:3948-3952(1993).
CC   -!- FUNCTION: Plays a role in hair follicle differentiation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA74561.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; DV214562; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L13201; AAA74561.1; ALT_FRAME; mRNA.
DR   PIR; I60916; I60916.
DR   PDB; 1KQ8; NMR; -; A=114-213.
DR   PDBsum; 1KQ8; -.
DR   AlphaFoldDB; Q63244; -.
DR   SMR; Q63244; -.
DR   UCSC; RGD:621572; rat.
DR   RGD; 621572; Foxq1.
DR   InParanoid; Q63244; -.
DR   PhylomeDB; Q63244; -.
DR   EvolutionaryTrace; Q63244; -.
DR   PRO; PR:Q63244; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR018122; TF_fork_head_CS_1.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..399
FT                   /note="Forkhead box protein Q1"
FT                   /id="PRO_0000091892"
FT   DNA_BIND        114..205
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        41
FT                   /note="G -> S (in Ref. 1; DV214562)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55..58
FT                   /note="SGAG -> RSAV (in Ref. 1; DV214562)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="G -> S (in Ref. 1; DV214562)"
FT                   /evidence="ECO:0000305"
FT   HELIX           121..128
FT                   /evidence="ECO:0007829|PDB:1KQ8"
FT   STRAND          131..134
FT                   /evidence="ECO:0007829|PDB:1KQ8"
FT   HELIX           138..148
FT                   /evidence="ECO:0007829|PDB:1KQ8"
FT   HELIX           152..154
FT                   /evidence="ECO:0007829|PDB:1KQ8"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:1KQ8"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:1KQ8"
SQ   SEQUENCE   399 AA;  41079 MW;  DFFFDBBA7B04F780 CRC64;
     MKLEVFAPRA AHGDKMGSDL EGAGSSDVPS PLSAAGDDSL GSDGDCAANS PAAGSGAGDL
     EGGGGERNSS GGASTQDDPE VTDGSRTQAS PVGPCAGSVG GGEGARSKPY TRRPKPPYSY
     IALIAMAIRD SAGGRLTLAE INEYLMGKFP FFRGSYTGWR NSVRHNLSLN DCFVKVLRDP
     SRPWGKDNYW MLNPNSEYTF ADGVFRRRRK RLSHRTTVSA SGYGGGSPPG PAGTPQPAPT
     AGSSPIARSP ARQEEGSSPA SKFSSSFAID SILSKPFRSR RDGTPALGVQ LPWSAAPCPP
     LRAYPALLPA SSGGALLPLC AYGAAEPTLL ASRGAEVQPA APLFVAPLST AAPAKPFRGP
     ETAGAAHLYC PLRLPTALQA AAACGPGPHL SYRVETLLA
 
 
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