PPIH_MOUSE
ID PPIH_MOUSE Reviewed; 188 AA.
AC Q9D868; Q9CQU7;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Head, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary cancer, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D868-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D868-2; Sequence=VSP_008325;
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H
CC subfamily. {ECO:0000305}.
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DR EMBL; AK003179; BAB22623.1; -; mRNA.
DR EMBL; AK008394; BAB25645.1; -; mRNA.
DR EMBL; AK005202; BAB23880.1; -; mRNA.
DR EMBL; AK014665; BAB29493.1; -; mRNA.
DR EMBL; BC016565; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC050116; AAH50116.1; -; mRNA.
DR CCDS; CCDS18580.1; -. [Q9D868-2]
DR CCDS; CCDS51288.1; -. [Q9D868-1]
DR RefSeq; NP_001103599.1; NM_001110129.1. [Q9D868-2]
DR RefSeq; NP_001103600.1; NM_001110130.1. [Q9D868-1]
DR RefSeq; NP_082953.1; NM_028677.4. [Q9D868-2]
DR AlphaFoldDB; Q9D868; -.
DR SMR; Q9D868; -.
DR BioGRID; 211213; 1.
DR IntAct; Q9D868; 1.
DR STRING; 10090.ENSMUSP00000101924; -.
DR iPTMnet; Q9D868; -.
DR PhosphoSitePlus; Q9D868; -.
DR EPD; Q9D868; -.
DR MaxQB; Q9D868; -.
DR PaxDb; Q9D868; -.
DR PeptideAtlas; Q9D868; -.
DR PRIDE; Q9D868; -.
DR ProteomicsDB; 289806; -. [Q9D868-1]
DR ProteomicsDB; 289807; -. [Q9D868-2]
DR DNASU; 66101; -.
DR Ensembl; ENSMUST00000056458; ENSMUSP00000051221; ENSMUSG00000060288. [Q9D868-2]
DR Ensembl; ENSMUST00000106317; ENSMUSP00000101924; ENSMUSG00000060288. [Q9D868-1]
DR Ensembl; ENSMUST00000106318; ENSMUSP00000101925; ENSMUSG00000060288. [Q9D868-2]
DR Ensembl; ENSMUST00000106321; ENSMUSP00000101928; ENSMUSG00000060288. [Q9D868-2]
DR Ensembl; ENSMUST00000122204; ENSMUSP00000142767; ENSMUSG00000033036. [Q9D868-2]
DR GeneID; 66101; -.
DR KEGG; mmu:66101; -.
DR UCSC; uc008ulz.2; mouse. [Q9D868-1]
DR CTD; 10465; -.
DR MGI; MGI:106499; Ppih.
DR VEuPathDB; HostDB:ENSMUSG00000033036; -.
DR VEuPathDB; HostDB:ENSMUSG00000060288; -.
DR eggNOG; KOG0879; Eukaryota.
DR GeneTree; ENSGT00940000154721; -.
DR InParanoid; Q9D868; -.
DR OMA; RHPNNPV; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q9D868; -.
DR TreeFam; TF312958; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 66101; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Ppih; mouse.
DR PRO; PR:Q9D868; -.
DR Proteomes; UP000000589; Chromosome 4.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D868; protein.
DR Bgee; ENSMUSG00000033036; Expressed in yolk sac and 42 other tissues.
DR ExpressionAtlas; Q9D868; baseline and differential.
DR Genevisible; Q9D868; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0071001; C:U4/U6 snRNP; ISO:MGI.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI.
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:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
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; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; Isomerase;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Rotamase;
KW Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43447"
FT CHAIN 2..188
FT /note="Peptidyl-prolyl cis-trans isomerase H"
FT /id="PRO_0000064163"
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"
FT VAR_SEQ 156..188
FT /note="FQAPLGKRVQAWTHSLTCPALTGILALILMPTE -> NVPTGPNNKPKLPVV
FT ISQCGEM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_008325"
SQ SEQUENCE 188 AA; 20464 MW; E11D29067BA98101 CRC64;
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE FRKDGVPIGY
KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN
GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIEFQAPL GKRVQAWTHS LTCPALTGIL
ALILMPTE
