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PITX1_XENLA
ID   PITX1_XENLA             Reviewed;         305 AA.
AC   Q9W751; Q9DEN6; Q9IA98;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Pituitary homeobox 1;
DE   AltName: Full=Homeobox protein PITX1;
DE            Short=X-PITX-1;
DE            Short=xPitx1;
DE   AltName: Full=Paired-like homeodomain transcription factor 1;
GN   Name=pitx1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10534625; DOI=10.1016/s0925-4773(99)00184-7;
RA   Hollemann T., Pieler T.;
RT   "Xpitx-1: a homeobox gene expressed during pituitary and cement gland
RT   formation of Xenopus embryos.";
RL   Mech. Dev. 88:249-252(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11170348;
RX   DOI=10.1002/1526-968x(200102)29:2<78::aid-gene1008>3.0.co;2-r;
RA   Chang W.Y., Khosrowshahian F., Chang R., Crawford M.J.;
RT   "xPitx1 plays a role in specifying cement gland and head during early
RT   Xenopus development.";
RL   Genesis 29:78-90(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11477694; DOI=10.1002/gene.1051;
RA   Schweickert A., Deissler K., Blum M., Steinbeisser H.;
RT   "Pitx1 and Pitx2c are required for ectopic cement gland formation in
RT   Xenopus laevis.";
RL   Genesis 30:144-148(2001).
CC   -!- FUNCTION: Sequence-specific transcription factor that binds gene
CC       promoters and activates their transcription. May play a role in the
CC       development of anterior structures, and in particular, the brain and
CC       facies and in specifying the identity or structure of hindlimb.
CC       {ECO:0000250|UniProtKB:P56673}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the anterior neural ridge and in the
CC       cement gland Anlage during late gastrulation/early neurulation.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF155206; AAD45292.1; -; mRNA.
DR   EMBL; AF217647; AAF29531.1; -; mRNA.
DR   EMBL; AJ278330; CAC12834.1; -; mRNA.
DR   RefSeq; NP_001080981.1; NM_001087512.1.
DR   RefSeq; NP_001091900.1; NM_001098430.1.
DR   AlphaFoldDB; Q9W751; -.
DR   SMR; Q9W751; -.
DR   GeneID; 394310; -.
DR   GeneID; 398122; -.
DR   KEGG; xla:394310; -.
DR   CTD; 394310; -.
DR   CTD; 5307; -.
DR   Xenbase; XB-GENE-485445; pitx1.L.
DR   OrthoDB; 1432356at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 394310; Expressed in neurula embryo and 6 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR016233; Homeobox_Pitx/unc30.
DR   InterPro; IPR003654; OAR_dom.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF03826; OAR; 1.
DR   PIRSF; PIRSF000563; Homeobox_protein_Pitx/Unc30; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS50803; OAR; 1.
PE   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Homeobox; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..305
FT                   /note="Pituitary homeobox 1"
FT                   /id="PRO_0000049222"
FT   DNA_BIND        78..137
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..270
FT                   /note="Interaction with PIT-1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           271..284
FT                   /note="OAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00138"
FT   MOTIF           284..288
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        21..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        7
FT                   /note="G -> A (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="A -> V (in Ref. 3; CAC12834)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   305 AA;  34128 MW;  ACA215A5BA86B43F CRC64;
     MDSFKGGMNL ERLPESLRPQ PSHDMATSFH LQRSSEARDP MDNSASESSD TEIAEKERTG
     EPKGEDGNGD DPSKKKKQRR QRTHFTSQQL QELEATFQRN RYPDMSMREE IAVWTNLTEA
     RVRVWFKNRR AKWRKRERNQ QMDLCKNGYV PQFSGLMQPY DEMYAGYPYN NWATKSLTPA
     PLSTKSFTFF NSMSPLSSQS MFSGPSSISS MSMPSSMGHS AVPGMANSSL NNINNLNNIS
     GSSLNSAMSS TGCPYGPPGS PYTVYRDTCN SSLASLRLKS KQHSTFGYSS LQSPASSLNA
     CQYNS
 
 
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