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Database: UniProt
Entry: A7Y7W2
LinkDB: A7Y7W2
Original site: A7Y7W2 
ID   PO5F3_CHICK             Reviewed;         389 AA.
AC   A7Y7W2; A0A0E4BYL6; A0A0E4BZG1; A0A0E9K094; R4GG91;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 2.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=POU domain, class 5, transcription factor 3;
GN   Name=POU5F3; Synonyms=POU2, POUV;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RX   PubMed=17827181; DOI=10.1242/dev.006569;
RA   Lavial F., Acloque H., Bertocchini F., MacLeod D.J., Boast S.,
RA   Bachelard E., Montillet G., Thenot S., Sang H.M., Stern C.D., Samarut J.,
RA   Pain B.;
RT   "The Oct4 homologue PouV and Nanog regulate pluripotency in chicken
RT   embryonic stem cells.";
RL   Development 134:3549-3563(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=25846318; DOI=10.1111/dgd.12205;
RA   Nakanoh S., Fuse N., Takahashi Y., Agata K.;
RT   "Verification of chicken Nanog as an epiblast marker and identification of
RT   chicken PouV as Pou5f3 by newly raised antibodies.";
RL   Dev. Growth Differ. 57:251-263(2015).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
CC   -!- FUNCTION: Required for the maintenance of pluripotency and self-renewal
CC       of embryonic stem cells. Transcriptional activator that binds the DNA
CC       consensus sequence 5'-ATGCAAAT-3'. {ECO:0000269|PubMed:17827181}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25846318}.
CC   -!- DEVELOPMENTAL STAGE: Widely expressed during embryonic development (at
CC       protein level). In pre-primitive streak stage embryos, expressed in the
CC       epiblast and in a salt-and-pepper fashion in the forming hypoblast
CC       (stages XI and XIII) (at protein level). As the primitive streak starts
CC       to form, strongly expressed in the epiblast of the streak itself (stage
CC       XIV) and in the mesoderm emerging from it, whereas expression in the
CC       lower layer tends to decrease (stages 2 through 4+). Expression in the
CC       area opaca is lost by stage 3+. At later stages, continues to be
CC       expressed in the mesoderm, but not detected in the endoderm (stages 5
CC       through 8). At stage 5, expressed in all cells of the germinal
CC       crescent. At stage 8 and subsequently, strongly expressed in the neural
CC       plate and neural tube with particularly strong expression in the
CC       anterior hindbrain/posterior midbrain. At stage 9 and subsequently,
CC       still expressed in neural tissue and in primordial germ cells (at
CC       protein level). At stage 33, still expressed in germ cells. At stages
CC       42-43, expressed in male and female gonads, as well as in spleen and
CC       brain, but at much lower levels than in proliferating embryonic stem
CC       cells. {ECO:0000269|PubMed:17827181, ECO:0000269|PubMed:25846318}.
CC   -!- INDUCTION: Strongly down-regulated during embryonic stem cell
CC       differentiation induced either by retinoic acid treatment, or by cell
CC       adhesion prevention leading to embryoid body formation.
CC       {ECO:0000269|PubMed:17827181}.
CC   -!- SIMILARITY: Belongs to the POU transcription factor family.
CC       {ECO:0000255|RuleBase:RU361194}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK27428.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AADN03007288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ867024; ABK27428.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; LC016616; BAR64207.1; -; Genomic_DNA.
DR   EMBL; LC016620; BAR64208.1; -; mRNA.
DR   EMBL; BR001258; FAA01189.1; -; mRNA.
DR   RefSeq; NP_001103648.1; NM_001110178.1.
DR   RefSeq; NP_001296301.1; NM_001309372.1.
DR   AlphaFoldDB; A7Y7W2; -.
DR   SMR; A7Y7W2; -.
DR   STRING; 9031.ENSGALP00000070462; -.
DR   PaxDb; 9031-ENSGALP00000041055; -.
DR   Ensembl; ENSGALT00015068316; ENSGALP00015041956; ENSGALG00015028097.
DR   GeneID; 427781; -.
DR   KEGG; gga:427781; -.
DR   CTD; 30333; -.
DR   VEuPathDB; HostDB:geneid_427781; -.
DR   eggNOG; KOG3802; Eukaryota.
DR   InParanoid; A7Y7W2; -.
DR   PRO; PR:A7Y7W2; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:1902459; P:positive regulation of stem cell population maintenance; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   PANTHER; PTHR11636:SF137; NETRIN-1-RELATED; 1.
DR   PANTHER; PTHR11636; POU DOMAIN; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF00157; Pou; 1.
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   1: Evidence at protein level;
KW   Activator; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..389
FT                   /note="POU domain, class 5, transcription factor 3"
FT                   /id="PRO_0000433626"
FT   DOMAIN          170..244
FT                   /note="POU-specific"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT   DNA_BIND        264..323
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  41198 MW;  0500F7B0B7AAA741 CRC64;
     MFSPDGGLPA APFGLLPDGG PPFPRGGYDG AAAQQLFFPF ASEPDGARDA ATARAWLPPP
     AGPPAKAEAR PARPCRQGSP EPRAAPPATP CCGPAWAAPP WPGPAPPAAT AVPGPPFPGP
     AAAAFPAAPG HALCPAALQP SSGGLANLGS SGSSSGAASE GGHSSDSGDE DAPTSEELEQ
     FAKDLKHKRI MLGFTQADVG LALGTLYGKM FSQTTICRFE ALQLSFKNMC KLKPLLQRWL
     NEAENTDNMQ EMCNAEQVLA QARKRKRRTS IETNVKGTLE SFFRKCVKPS PQEISQIAED
     LNLDKDVVRV WFCNRRQKGK RLLLPFGNES EGVMYDMNQS LVPPGLPIPV TSQGYSLAPS
     PPVYMPPFHK AEMFPPPLQP GISMNNSSH
//
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