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PIN4_DANRE
ID   PIN4_DANRE              Reviewed;         128 AA.
AC   Q503Y7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4;
DE            EC=5.2.1.8;
DE   AltName: Full=Parvulin-14;
DE            Short=Par14;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin4;
DE            Short=PPIase Pin4;
DE   AltName: Full=Rotamase Pin4;
GN   Name=pin4; ORFNames=zgc:110008;
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 MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved as a ribosomal RNA processing factor in
CC       ribosome biogenesis. Binds to DNA (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC095126; AAH95126.1; -; mRNA.
DR   RefSeq; NP_001018389.1; NM_001020553.1.
DR   AlphaFoldDB; Q503Y7; -.
DR   SMR; Q503Y7; -.
DR   STRING; 7955.ENSDARP00000023444; -.
DR   PaxDb; Q503Y7; -.
DR   Ensembl; ENSDART00000026846; ENSDARP00000023444; ENSDARG00000004527.
DR   GeneID; 553574; -.
DR   KEGG; dre:553574; -.
DR   CTD; 5303; -.
DR   ZFIN; ZDB-GENE-050522-117; pin4.
DR   eggNOG; KOG3258; Eukaryota.
DR   GeneTree; ENSGT00510000047029; -.
DR   HOGENOM; CLU_090028_2_1_1; -.
DR   InParanoid; Q503Y7; -.
DR   OMA; AMSINVR; -.
DR   OrthoDB; 1397633at2759; -.
DR   PhylomeDB; Q503Y7; -.
DR   TreeFam; TF101102; -.
DR   PRO; PR:Q503Y7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 14.
DR   Bgee; ENSDARG00000004527; Expressed in tail and 24 other tissues.
DR   ExpressionAtlas; Q503Y7; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR043323; PIN4.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   PANTHER; PTHR45995; PTHR45995; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; DNA-binding; Isomerase; Nucleus;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..128
FT                   /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT                   4"
FT                   /id="PRO_0000379926"
FT   DOMAIN          32..126
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   128 AA;  13664 MW;  214ED4DD20755C70 CRC64;
     MPPKGKGGKG AKGAAASGSG DSDKKEKAQK GGTAVKVRHI LCEKHGKCME AMEKIKSGMR
     FSEVAAQYSE DKARQGGDLG WMTRGSMVGP FQDAAFALPI STMDKPVYTD PPVKTKFGYH
     IIMVEGKK
 
 
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