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PAX6_BOVIN
ID   PAX6_BOVIN              Reviewed;         422 AA.
AC   Q1LZF1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Paired box protein Pax-6;
DE   AltName: Full=Oculorhombin;
GN   Name=PAX6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor with important functions in the
CC       development of the eye, nose, central nervous system and pancreas.
CC       Required for the differentiation of pancreatic islet alpha cells.
CC       Competes with PAX4 in binding to a common element in the glucagon,
CC       insulin and somatostatin promoters. Regulates specification of the
CC       ventral neuron subtypes by establishing the correct progenitor domains
CC       (By similarity). Acts as a transcriptional repressor of NFATC1-mediated
CC       gene expression (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P63015}.
CC   -!- SUBUNIT: Interacts with MAF and MAFB (By similarity). Interacts with
CC       TRIM11; this interaction leads to ubiquitination and proteasomal
CC       degradation, as well as inhibition of transactivation, possibly in part
CC       by preventing PAX6 binding to consensus DNA sequences (By similarity).
CC       Interacts with TLE6/GRG6 (By similarity).
CC       {ECO:0000250|UniProtKB:P63015}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P63015}.
CC   -!- PTM: Ubiquitinated by TRIM11, leading to ubiquitination and proteasomal
CC       degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}.
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DR   EMBL; BC116038; AAI16039.1; -; mRNA.
DR   RefSeq; NP_001035735.1; NM_001040645.1.
DR   RefSeq; XP_010811018.1; XM_010812716.2.
DR   AlphaFoldDB; Q1LZF1; -.
DR   SMR; Q1LZF1; -.
DR   STRING; 9913.ENSBTAP00000005994; -.
DR   PaxDb; Q1LZF1; -.
DR   Ensembl; ENSBTAT00000005994; ENSBTAP00000005994; ENSBTAG00000004561.
DR   GeneID; 286857; -.
DR   KEGG; bta:286857; -.
DR   CTD; 5080; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004561; -.
DR   VGNC; VGNC:32598; PAX6.
DR   eggNOG; KOG0849; Eukaryota.
DR   GeneTree; ENSGT00940000155391; -.
DR   HOGENOM; CLU_019281_1_0_1; -.
DR   InParanoid; Q1LZF1; -.
DR   OrthoDB; 1152885at2759; -.
DR   TreeFam; TF320146; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000004561; Expressed in pigment epithelium of eye and 35 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:1904798; P:positive regulation of core promoter binding; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00086; homeodomain; 1.
DR   CDD; cd00131; PAX; 1.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR043182; PAIRED_DNA-bd_dom.
DR   InterPro; IPR001523; Paired_dom.
DR   InterPro; IPR043565; PAX_fam.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR45636; PTHR45636; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; DNA-binding; Homeobox; Nucleus;
KW   Paired box; Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..422
FT                   /note="Paired box protein Pax-6"
FT                   /id="PRO_0000263070"
FT   DNA_BIND        4..130
FT                   /note="Paired"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   DNA_BIND        210..269
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          7..63
FT                   /note="PAI subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          82..130
FT                   /note="RED subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00381"
FT   REGION          162..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..422
FT                   /note="Required for suppression of NFATC1-mediated
FT                   transcription"
FT                   /evidence="ECO:0000250|UniProtKB:P63015"
FT   COMPBIAS        167..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  46653 MW;  B5E7AD2C1B13C383 CRC64;
     MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY
     YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV
     SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ
     EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR
     ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP
     QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT
     SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG ATSTGLISPG VSVPVQVPGS EPDMSQYWPR
     LQ
 
 
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