ID   PIN4_BOVIN              Reviewed;         131 AA.
AC   A6QPY8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
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   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=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved as a ribosomal RNA processing factor in ribosome
CC       biogenesis. Binds to tightly bent AT-rich stretches of double-stranded
CC       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   -!- SUBUNIT: Found in pre-ribosomal ribonucleoprotein (pre-rRNP) complexes.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Colocalizes in the nucleolus during interphase and on the spindle
CC       apparatus during mitosis with NPM1. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. Phosphorylation occurs both in the nucleus and the
CC       cytoplasm. Phosphorylation at Ser-19 does not affect its PPIase
CC       activity but is required for nuclear localization, and the
CC       dephosphorylation is a prerequisite for the binding to DNA. The
CC       unphosphorylated form associates with the pre-rRNP complexes in the
CC       nucleus (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC149559; AAI49560.1; -; mRNA.
DR   RefSeq; NP_001099127.1; NM_001105657.1.
DR   AlphaFoldDB; A6QPY8; -.
DR   SMR; A6QPY8; -.
DR   STRING; 9913.ENSBTAP00000054808; -.
DR   PaxDb; A6QPY8; -.
DR   PRIDE; A6QPY8; -.
DR   Ensembl; ENSBTAT00000063342; ENSBTAP00000054808; ENSBTAG00000047376.
DR   GeneID; 100126055; -.
DR   KEGG; bta:100126055; -.
DR   CTD; 5303; -.
DR   VEuPathDB; HostDB:ENSBTAG00000047376; -.
DR   VGNC; VGNC:32903; PIN4.
DR   eggNOG; KOG3258; Eukaryota.
DR   GeneTree; ENSGT00510000047029; -.
DR   HOGENOM; CLU_090028_2_1_1; -.
DR   InParanoid; A6QPY8; -.
DR   OMA; AMSINVR; -.
DR   OrthoDB; 1397633at2759; -.
DR   TreeFam; TF101102; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000047376; Expressed in oocyte and 105 other tissues.
DR   GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; Phosphoprotein;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..131
FT                   /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT                   4"
FT                   /id="PRO_0000379924"
FT   DOMAIN          35..129
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT   REGION          1..41
FT                   /note="Necessary for association with the pre-rRNP
FT                   complexes"
FT                   /evidence="ECO:0000250"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1..25
FT                   /note="Necessary for nuclear localization and DNA-binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y237"
SQ   SEQUENCE   131 AA;  13903 MW;  113987729E060321 CRC64;
     MPPKGKSGSG KGGKGKAASG SESSEKKAQG PKGGGNAVKV RHILCEKHGK ILEAMEKLKS
     GMKFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPISVLDKPV FTDPPVKTKF
     GYHIIMVEGR K