Entry sw:PPIH_BOVIN

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   02-NOV-2016, entry version 80.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE            Short=PPIase H;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase H;
GN   Name=PPIH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Participates in pre-mRNA splicing. May play a role
CC       in the assembly of the U4/U5/U6 tri-snRNP complex, one of the
CC       building blocks of the spliceosome. May act as a chaperone (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited by cyclosporin A. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts directly with PRPF4. Part of a heteromeric
CC       complex containing PPIH, PRPF3 and PRPF4 that is stable in the
CC       absence of RNA. Component of the U4/U6-U5 tri-snRNP complex
CC       composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4,
CC       PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2,
CC       PPIH, SNU13, EFTUD2, SART1 and USP39. Heterodimer with PRPF18.
CC       Heterodimer with PRPF18 (By similarity). {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
CC       H subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00156}.
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   UniGene; Bt.6641; -.
DR   ProteinModelPortal; 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   eggNOG; KOG0546; Eukaryota.
DR   eggNOG; COG0652; LUCA.
DR   GeneTree; ENSGT00760000119072; -.
DR   HOGENOM; HOG000065981; -.
DR   HOVERGEN; HBG001065; -.
DR   InParanoid; Q0P5D0; -.
DR   KO; K09567; -.
DR   OMA; PTWNQIQ; -.
DR   OrthoDB; EOG091G0BGL; -.
DR   TreeFam; TF312958; -.
DR   Reactome; R-BTA-72163; mRNA Splicing - Major Pathway.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000004590; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0071001; C:U4/U6 snRNP; IEA:Ensembl.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:Ensembl.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PTHR11071; 1.
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; Complete proteome; Cytoplasm; Isomerase;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Rotamase;
KW   Spliceosome.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O43447}.
FT   CHAIN         2    177       Peptidyl-prolyl cis-trans isomerase H.
FT                                /FTId=PRO_0000282598.
FT   DOMAIN       14    176       PPIase cyclophilin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00156}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:O43447}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        21    175       ipfam:Pro_isomerase [T]
FT   MYHIT        14    176       iprf:CSA_PPIASE_2 [T]
FT   MYHIT        60     77       ipat:CSA_PPIASE_1 [T]
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
//