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UBL4A_DANRE
ID   UBL4A_DANRE             Reviewed;         157 AA.
AC   Q7ZWB2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Ubiquitin-like protein 4A;
GN   Name=ubl4a; ORFNames=si:dkey-32e23.2, zgc:56596;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: As part of a cytosolic protein quality control complex, the
CC       bag6/bat3 complex, maintains misfolded and hydrophobic patches-
CC       containing proteins in a soluble state and participates in their proper
CC       delivery to the endoplasmic reticulum or alternatively can promote
CC       their sorting to the proteasome where they undergo degradation. The
CC       bag6/bat3 complex is involved in the post-translational delivery of
CC       tail-anchored/type II transmembrane proteins to the endoplasmic
CC       reticulum membrane. Similarly, the bag6/bat3 complex also functions as
CC       a sorting platform for proteins of the secretory pathway that are
CC       mislocalized to the cytosol either delivering them to the proteasome
CC       for degradation or to the endoplasmic reticulum. The bag6/bat3 complex
CC       also plays a role in the endoplasmic reticulum-associated degradation
CC       (ERAD), a quality control mechanism that eliminates unwanted proteins
CC       of the endoplasmic reticulum through their retrotranslocation to the
CC       cytosol and their targeting to the proteasome. It maintains these
CC       retrotranslocated proteins in an unfolded yet soluble state condition
CC       in the cytosol to ensure their proper delivery to the proteasome.
CC       {ECO:0000250|UniProtKB:P11441}.
CC   -!- SUBUNIT: Component of the bag6/bat3 complex.
CC       {ECO:0000250|UniProtKB:P11441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P11441}. Nucleus {ECO:0000250|UniProtKB:P11441}.
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DR   EMBL; CR855300; CAX14238.1; -; Genomic_DNA.
DR   EMBL; BC049498; AAH49498.1; -; mRNA.
DR   RefSeq; NP_956594.1; NM_200300.1.
DR   AlphaFoldDB; Q7ZWB2; -.
DR   SMR; Q7ZWB2; -.
DR   STRING; 7955.ENSDARP00000009190; -.
DR   PaxDb; Q7ZWB2; -.
DR   Ensembl; ENSDART00000013870; ENSDARP00000009190; ENSDARG00000007359.
DR   GeneID; 393270; -.
DR   KEGG; dre:393270; -.
DR   ZFIN; ZDB-GENE-040426-1089; zgc:56596.
DR   eggNOG; KOG0001; Eukaryota.
DR   GeneTree; ENSGT00730000111022; -.
DR   HOGENOM; CLU_119809_0_0_1; -.
DR   InParanoid; Q7ZWB2; -.
DR   OMA; SMDTSYM; -.
DR   OrthoDB; 1586605at2759; -.
DR   PhylomeDB; Q7ZWB2; -.
DR   TreeFam; TF354228; -.
DR   PRO; PR:Q7ZWB2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000007359; Expressed in testis and 28 other tissues.
DR   GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR   CDD; cd01807; Ubl_UBL4A_like; 1.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   InterPro; IPR041421; Ubl4_C_TUGS.
DR   InterPro; IPR044724; Ubl_UBL4A-like.
DR   Pfam; PF17840; Tugs; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; Transport.
FT   CHAIN           1..157
FT                   /note="Ubiquitin-like protein 4A"
FT                   /id="PRO_0000403742"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   157 AA;  17320 MW;  8EACCDA50C90A09C CRC64;
     MILTVKPLQG KECNVQVTEN EKVSTVKELV SERLNIPASQ QRLLYKGKAL ADEHRLSDYS
     IGPEAKLNLV VRPAGERSSG AVGTSSANND KGGSGVWQLL STVLAKHFSP ADAAKVQEQL
     IKDYERSLRQ LSLDDIERLA SRLLHPETEV MDTSYMD
 
 
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