ID   PPIH_BOVIN              Reviewed;         177 AA.
AC   Q0P5D0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE            Short=PPIase H;
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:O43447};
DE   AltName: Full=Rotamase H;
GN   Name=PPIH;
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=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC       imidic peptide bonds in oligopeptides and may therefore assist protein
CC       folding. Participates in pre-mRNA splicing. May play a role in the
CC       assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks
CC       of the spliceosome. May act as a chaperone.
CC       {ECO:0000250|UniProtKB:O43447}.
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         Evidence={ECO:0000250|UniProtKB:O43447};
CC   -!- ACTIVITY REGULATION: Inhibited by cyclosporin A.
CC       {ECO:0000250|UniProtKB:O43447}.
CC   -!- SUBUNIT: Interacts directly with PRPF4. Part of a heteromeric complex
CC       containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA.
CC       Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and
CC       U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200,
CC       TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39.
CC       Heterodimer with PRPF18. Heterodimer with PRPF18 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=Colocalizes with spliceosomal snRNPs. A small
CC       proportion may also be cytoplasmic (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC120220; AAI20221.1; -; mRNA.
DR   RefSeq; NP_001069086.1; NM_001075618.1.
DR   RefSeq; XP_005204783.2; XM_005204726.3.
DR   RefSeq; XP_010801917.2; XM_010803615.2.
DR   AlphaFoldDB; Q0P5D0; -.
DR   SMR; Q0P5D0; -.
DR   STRING; 9913.ENSBTAP00000006026; -.
DR   PaxDb; Q0P5D0; -.
DR   PRIDE; Q0P5D0; -.
DR   Ensembl; ENSBTAT00000006026; ENSBTAP00000006026; ENSBTAG00000004590.
DR   GeneID; 513428; -.
DR   KEGG; bta:513428; -.
DR   CTD; 10465; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004590; -.
DR   VGNC; VGNC:33200; PPIH.
DR   eggNOG; KOG0879; Eukaryota.
DR   GeneTree; ENSGT00940000154721; -.
DR   HOGENOM; CLU_012062_4_3_1; -.
DR   InParanoid; Q0P5D0; -.
DR   OMA; RHPNNPV; -.
DR   OrthoDB; 1403619at2759; -.
DR   TreeFam; TF312958; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000004590; Expressed in oocyte and 106 other tissues.
DR   ExpressionAtlas; Q0P5D0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Isomerase; mRNA processing;
KW   mRNA splicing; Nucleus; Reference proteome; Rotamase; Spliceosome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O43447"
FT   CHAIN           2..177
FT                   /note="Peptidyl-prolyl cis-trans isomerase H"
FT                   /id="PRO_0000282598"
FT   DOMAIN          14..176
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43447"
SQ   SEQUENCE   177 AA;  19208 MW;  566BCE6361E0F339 CRC64;
     MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE FRKDGVPIGY
     KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN
     GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM