ID G3U5Q1_LOXAF Unreviewed; 492 AA.
AC G3U5Q1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=POU domain protein {ECO:0000256|RuleBase:RU361194};
GN Name=POU2F2 {ECO:0000313|Ensembl:ENSLAFP00000023159.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000023159.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000023159.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023159.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000023159.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023159.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000256|ARBA:ARBA00008879}.
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DR AlphaFoldDB; G3U5Q1; -.
DR Ensembl; ENSLAFT00000029846.1; ENSLAFP00000023159.1; ENSLAFG00000009508.3.
DR GeneTree; ENSGT00940000160115; -.
DR OMA; PMKISPF; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR000972; TF_octamer.
DR PANTHER; PTHR11636; POU DOMAIN; 1.
DR PANTHER; PTHR11636:SF46; POU DOMAIN, CLASS 2, TRANSCRIPTION FACTOR 2; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PRINTS; PR00029; OCTAMER.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU361194};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 208..282
FT /note="POU-specific"
FT /evidence="ECO:0000259|PROSITE:PS51179"
FT DOMAIN 310..370
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 312..371
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 52808 MW; 33A49A34A23FDD44 CRC64;
QDSRGSPEIR MSKPLEAEKQ GLDSPSEHTD TERNGPDTNH QNPQNKTSPF SVSPTGPSTK
IKAEDPSGDS APAAPPPPQP AQPHLPQAQL MLTGSQLAGD IQQLLQLQQL VLVPGHHLQP
PAQFLLPQTQ QSQPGLLPTP NLFQLPQQTQ GALLTSQPRA GLPTQNPGPP SCIPPTPPHQ
AVTRPTLPDP HLSHPQPPKC LEPPSHPEEP SDLEELEQFA RTFKQRRIKL GFTQGDVGLA
MGKLYGNDFS QTTISRFEAL NLSFKNMCKL KPLLEKWLND AGTETMSVDS SLPSPNQLSS
PSLGFDGLPG RRRKKRTSIE TNVRFALEKS FLANQKPTSE EILLIAEQLH MEKEVIRVWF
CNRRQKEKRI NPCSAAPMLP SPGKPASYSP HLVTPQGAAG TLPLSQASSS LSTTVTTLSS
AVGTLHPSRT AGAPPLNSIP SVTPPPPATT NSTNPSPQGS HSAIGLSGLN PSTGVDLMLS
PWLWGSPPAL PP
//
