PIN4_TAEGU
ID PIN4_TAEGU Reviewed; 128 AA.
AC B5KFL3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 47.
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;
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA Hayashizaki Y., Carninci P., Jarvis E.D.;
RT "A molecular neuroethological approach for identifying and characterizing a
RT cascade of behaviorally regulated genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
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; EF191799; ACH46361.1; -; mRNA.
DR RefSeq; NP_001232346.1; NM_001245417.1.
DR AlphaFoldDB; B5KFL3; -.
DR SMR; B5KFL3; -.
DR STRING; 59729.ENSTGUP00000031258; -.
DR GeneID; 100190566; -.
DR KEGG; tgu:100190566; -.
DR CTD; 5303; -.
DR InParanoid; B5KFL3; -.
DR OrthoDB; 1397633at2759; -.
DR Proteomes; UP000007754; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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_0000379925"
FT DOMAIN 32..126
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 128 AA; 13428 MW; F532D280D01EA9A6 CRC64;
MAPKGKGGGK AGKGGDGGSS SEGKAQGPKG GGSAVKVRHI LCEKHGRAME AMEKLKSGQR
FSEVAAQYSE DKARQGGDLG WMTRGSMVGP FQEAAFALPV SSMDKPVYTD PPVKTKFGYH
IIMVEGRK
