ID A0A498MER0_LABRO Unreviewed; 1631 AA.
AC A0A498MER0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Forkhead box protein N3 {ECO:0000256|ARBA:ARBA00034870};
GN ORFNames=ROHU_007700 {ECO:0000313|EMBL:RXN18640.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN18640.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN18640.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN18640.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN18640.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a transcriptional repressor. May be involved in DNA
CC damage-inducible cell cycle arrests (checkpoints).
CC {ECO:0000256|ARBA:ARBA00034657}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00089}.
CC -!- SIMILARITY: Belongs to the TFIIA subunit 1 family.
CC {ECO:0000256|ARBA:ARBA00010059}.
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:RXN18640.1}.
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DR EMBL; QBIY01012709; RXN18640.1; -; Genomic_DNA.
DR STRING; 84645.A0A498MER0; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005672; C:transcription factor TFIIA complex; IEA:InterPro.
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 GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd20059; FH_FOXN3; 1.
DR CDD; cd07976; TFIIA_alpha_beta_like; 1.
DR Gene3D; 1.10.287.100; -; 1.
DR Gene3D; 2.30.18.10; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR047404; FH_FOXN3.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR047119; FOXN2/3-like.
DR InterPro; IPR027806; HARBI1_dom.
DR InterPro; IPR018122; TF_fork_head_CS_1.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR004855; TFIIA_asu/bsu.
DR InterPro; IPR009088; TFIIA_b-brl.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13962:SF20; FORKHEAD BOX PROTEIN N3; 1.
DR PANTHER; PTHR13962; FORKHEAD BOX PROTEIN N3-LIKE PROTEIN-RELATED; 1.
DR Pfam; PF13359; DDE_Tnp_4; 1.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF03153; TFIIA; 2.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SMART; SM01371; TFIIA; 1.
DR SUPFAM; SSF47396; Transcription factor IIA (TFIIA), alpha-helical domain; 1.
DR SUPFAM; SSF50784; Transcription factor IIA (TFIIA), beta-barrel domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 856..943
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 856..943
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 65..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1365..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..320
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1433
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1631 AA; 178042 MW; 3B7B817E307174F4 CRC64;
MAMSTIPTSF SESAVSSSSE LSDELTTALA AGRWWAIMEV SSPISEEPEY GDLTSVQWWG
TMEAGESSCP TSLAFSDESG KTESPYSGVS DETLNTKDPW RQKKTQSAPM PPRSQKGAPV
PACTEKRDHT SPLVFSNASE KTESLYSGFS DAMLKTTERQ RKWRQKKPQG PRVLARSEKA
ECGDSPFSNA ALKTSKQVRQ KKLQVAPVAA RSPQGAPVPA RSPQGAPVPF RSPQGEPVPA
RSPPGAPVPV RSPLGASVPA RSPQGALVPS RSPQGAPVPN RSPPGAPVPF RSPQGAPVPT
RSPPGAPVPT RSPPGAPVPA RSPLGASVPA RSPQGAPVPN RSPPGAPVPN RSPPGAPVPA
RSPLGAPVPA RSPQGAPVLA RTPKRAPVPS GSPQEPPVHT GSQQRGKLRI PEHLRKHLLR
AAGELGAPVP AKSPQGAPVP TKSLQREPVP APEVQNPEPL RQELQQQKPQ ASSVMGAPMP
NKTPVRQRLK IPEPLRQELL QLSRRASSVR EDLVPNKTPE RQRLKIPEPL RQELLLLSRR
ASSVKGEPML KKTPERQRLK IPQPLRQELL QLSSRASSVK EEPMPKKTAE RQRLKIQEPL
RQELLQLSAR AEKGAAMPKN TVERQRLKIP ERLRKELLQQ KPPATAQGLL MSSNSPREAP
VPDGNPVHAD TPQGAGVFAR SPPAEAVPTG CLKGAVVLTR TMKAGKRRLE GLNPSTQAFS
STRQRGGAGL TSGCVSYDYR AEGCMGPVVM PPGKKAEGPS SGSVARGLSQ LYQDTEAADL
SLALSASLSR AEDEELTSLS WLHESTDLLT SLGHSGLRSV SPLQDANGGR EPSSSPSSSP
EPSEPPYHLS TGPSRKPPYS FSCLIFMAIE DAPSKRLPVK DIYGWILEHF PYFASAPTGW
KNSVRHNLSL NKCFKKVDKD RSQSIGKGSL WSIDPDYRHN LIQALKKTPY HPYSPRLPKP
STSPSASPQQ YHRPTKPQDR QWDNEIRNVM SDFSSVNPNN TPNVKFLSLK KVMPMSSTMA
RESTLQKKWR SALTRSALGD YLTRGKNSLR SDSPPPSDDQ QEDHTYSSSQ SLNTKGDISS
SLSSCSTQGS LSAYSPGQEV TVTEVKEEQK DFPLDATPPP SQLLQRRRLL WTKGHLRTPG
DTLPLKKRRA EKLLVKEEED EEMKEAAGSL LHLAGVRTGV NKNAQRYQIT LPKEETSRKP
INEQICLVLN ISFHSEGLIQ DLLTNRVTFA PNLYKAVMDD VISEVRELFL DEGVDEQVLM
ELKTSAAATA ATLALPAGVA PFQQLITPQG QILQVVRAAN GAQYIIQPQQ QMLLQQQVLP
QMQPGGVQAP VIQQVLTPLQ GGLSQQTGVI IQPQQIVLTG NKVQQNTQAS QQPPMVLQVD
GAGDTSSEED EEEEDEYDED EDEDKEKDGG EDGQVEEEPL NSGDDVSDEE DQELFDTENV
VVCQYDKIHR SKNKWKFHLK DGIMNLNGRD YVFSKAIGDA EWLCYRTSIL VSGIKGLGEA
SLSECNGQYN GYLLGDRGYP CLPYLMTPYP EPDPGPQTRF NLAHSRTRAK VEMTIGILKS
RFQCLRGLRV SPERACDIIV ACVVLHNIAT IRGESHPACI EEDGPEEPLQ IFAHNRDGRL
LRDRICQNYF Y
//