PPIH_HUMAN
ID PPIH_HUMAN Reviewed; 177 AA.
AC O43447; A6NNE7;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE Short=PPIase H;
DE EC=5.2.1.8 {ECO:0000269|PubMed:20676357};
DE AltName: Full=Rotamase H;
DE AltName: Full=Small nuclear ribonucleoprotein particle-specific cyclophilin H;
DE Short=CypH;
DE AltName: Full=U-snRNP-associated cyclophilin SnuCyp-20;
DE Short=USA-CYP;
GN Name=PPIH; Synonyms=CYP20, CYPH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 154-164, AND
RP INTERACTION WITH PRPF3; PRPF4 AND U4/U6 SNRNPS.
RC TISSUE=Liver;
RX PubMed=9404889;
RA Horowitz D.S., Kobayashi R., Krainer A.R.;
RT "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a
RT complex associated with U4/U6 snRNPs.";
RL RNA 3:1374-1387(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 62-67; 71-81
RP AND 153-164, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE
RP U4/U5/U6 TRI-SNRNP COMPLEX.
RC TISSUE=Liver;
RX PubMed=9570313;
RA Teigelkamp S., Achsel T., Mundt C., Goethel S.-F., Cronshagen U.,
RA Lane W.S., Marahiel M., Luehrmann R.;
RT "The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin
RT that forms a complex with the U4/U6-specific 60kD and 90kD proteins.";
RL RNA 4:127-141(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [7]
RP FUNCTION, MUTAGENESIS OF TRP-133, AND INTERACTION WITH PRPF4 AND PRPF18.
RX PubMed=11823439; DOI=10.1093/emboj/21.3.470;
RA Horowitz D.S., Lee E.J., Mabon S.A., Misteli T.;
RT "A cyclophilin functions in pre-mRNA splicing.";
RL EMBO J. 21:470-480(2002).
RN [8]
RP SUBUNIT.
RX PubMed=16723661; DOI=10.1261/rna.55406;
RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT "The network of protein-protein interactions within the human U4/U6.U5 tri-
RT snRNP.";
RL RNA 12:1418-1430(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177.
RX PubMed=10713041; DOI=10.1074/jbc.275.11.7439;
RA Reidt U., Reuter K., Achsel T., Ingelfinger D., Luehrmann R., Ficner R.;
RT "Crystal structure of the human U4/U6 small nuclear ribonucleoprotein
RT particle-specific SnuCyp-20, a nuclear cyclophilin.";
RL J. Biol. Chem. 275:7439-7442(2000).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4, AND
RP FUNCTION.
RX PubMed=12875835; DOI=10.1016/s0022-2836(03)00684-3;
RA Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R., Ficner R.;
RT "Crystal structure of a complex between human spliceosomal cyclophilin H
RT and a U4/U6 snRNP-60K peptide.";
RL J. Mol. Biol. 331:45-56(2003).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding (PubMed:20676357). Participates in pre-mRNA splicing. May play
CC a role 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.
CC {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835,
CC ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:9570313}.
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:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A.
CC {ECO:0000305|PubMed:20676357}.
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. {ECO:0000269|PubMed:11823439,
CC ECO:0000269|PubMed:12875835, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:9404889, ECO:0000269|PubMed:9570313}.
CC -!- INTERACTION:
CC O43447; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-1055615, EBI-953896;
CC O43447; Q7L591-3: DOK3; NbExp=5; IntAct=EBI-1055615, EBI-10694655;
CC O43447; P42858: HTT; NbExp=10; IntAct=EBI-1055615, EBI-466029;
CC O43447; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1055615, EBI-739832;
CC O43447; Q92802: N4BP2L2; NbExp=10; IntAct=EBI-1055615, EBI-2514973;
CC O43447; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-1055615, EBI-740897;
CC O43447; Q99633: PRPF18; NbExp=7; IntAct=EBI-1055615, EBI-2798416;
CC O43447; O43172: PRPF4; NbExp=5; IntAct=EBI-1055615, EBI-718395;
CC O43447; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1055615, EBI-947187;
CC O43447; P98170: XIAP; NbExp=5; IntAct=EBI-1055615, EBI-517127;
CC O43447; PRO_0000037309 [P0C6X7]: rep; Xeno; NbExp=4; IntAct=EBI-1055615, EBI-25475797;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9570313}.
CC Cytoplasm {ECO:0000269|PubMed:9570313}. Note=Colocalizes with
CC spliceosomal snRNPs. A small proportion may also be cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43447-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43447-2; Sequence=VSP_056587;
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H
CC subfamily. {ECO:0000305}.
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DR EMBL; AF016371; AAC51927.1; -; mRNA.
DR EMBL; AF036331; AAC60793.1; -; mRNA.
DR EMBL; AK294288; BAH11725.1; -; mRNA.
DR EMBL; AC098484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07155.1; -; Genomic_DNA.
DR EMBL; BC003412; AAH03412.1; -; mRNA.
DR CCDS; CCDS469.1; -. [O43447-1]
DR CCDS; CCDS81308.1; -. [O43447-2]
DR RefSeq; NP_001317439.1; NM_001330510.1. [O43447-2]
DR RefSeq; NP_006338.1; NM_006347.3. [O43447-1]
DR RefSeq; XP_005270419.1; XM_005270362.1. [O43447-1]
DR RefSeq; XP_016855546.1; XM_017000057.1. [O43447-1]
DR RefSeq; XP_016855547.1; XM_017000058.1.
DR RefSeq; XP_016855548.1; XM_017000059.1. [O43447-2]
DR PDB; 1MZW; X-ray; 2.00 A; A=1-177.
DR PDB; 1QOI; X-ray; 2.00 A; A=1-177.
DR PDB; 5O9Z; EM; 4.50 A; M=1-177.
DR PDB; 6AHD; EM; 3.80 A; W=1-177.
DR PDBsum; 1MZW; -.
DR PDBsum; 1QOI; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AHD; -.
DR AlphaFoldDB; O43447; -.
DR SMR; O43447; -.
DR BioGRID; 115728; 75.
DR CORUM; O43447; -.
DR IntAct; O43447; 34.
DR MINT; O43447; -.
DR STRING; 9606.ENSP00000306614; -.
DR BindingDB; O43447; -.
DR DrugBank; DB00172; Proline.
DR GlyGen; O43447; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43447; -.
DR PhosphoSitePlus; O43447; -.
DR SwissPalm; O43447; -.
DR BioMuta; PPIH; -.
DR EPD; O43447; -.
DR jPOST; O43447; -.
DR MassIVE; O43447; -.
DR MaxQB; O43447; -.
DR PaxDb; O43447; -.
DR PeptideAtlas; O43447; -.
DR PRIDE; O43447; -.
DR ProteomicsDB; 1602; -.
DR ProteomicsDB; 48953; -. [O43447-1]
DR Antibodypedia; 32222; 187 antibodies from 25 providers.
DR DNASU; 10465; -.
DR Ensembl; ENST00000304979.8; ENSP00000306614.3; ENSG00000171960.12. [O43447-1]
DR Ensembl; ENST00000372550.6; ENSP00000361630.2; ENSG00000171960.12. [O43447-1]
DR Ensembl; ENST00000676675.1; ENSP00000503489.1; ENSG00000171960.12. [O43447-1]
DR Ensembl; ENST00000677900.1; ENSP00000504595.1; ENSG00000171960.12. [O43447-1]
DR Ensembl; ENST00000678038.1; ENSP00000504108.1; ENSG00000171960.12. [O43447-1]
DR Ensembl; ENST00000678333.1; ENSP00000503384.1; ENSG00000171960.12. [O43447-1]
DR Ensembl; ENST00000678803.1; ENSP00000503922.1; ENSG00000171960.12. [O43447-1]
DR GeneID; 10465; -.
DR KEGG; hsa:10465; -.
DR MANE-Select; ENST00000304979.8; ENSP00000306614.3; NM_006347.4; NP_006338.1.
DR UCSC; uc009vwl.3; human. [O43447-1]
DR CTD; 10465; -.
DR DisGeNET; 10465; -.
DR GeneCards; PPIH; -.
DR HGNC; HGNC:14651; PPIH.
DR HPA; ENSG00000171960; Low tissue specificity.
DR MIM; 606095; gene.
DR neXtProt; NX_O43447; -.
DR OpenTargets; ENSG00000171960; -.
DR PharmGKB; PA33586; -.
DR VEuPathDB; HostDB:ENSG00000171960; -.
DR eggNOG; KOG0879; Eukaryota.
DR GeneTree; ENSGT00940000154721; -.
DR InParanoid; O43447; -.
DR OMA; RHPNNPV; -.
DR PhylomeDB; O43447; -.
DR TreeFam; TF312958; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; O43447; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O43447; -.
DR BioGRID-ORCS; 10465; 292 hits in 1084 CRISPR screens.
DR ChiTaRS; PPIH; human.
DR EvolutionaryTrace; O43447; -.
DR GeneWiki; PPIH; -.
DR GenomeRNAi; 10465; -.
DR Pharos; O43447; Tbio.
DR PRO; PR:O43447; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43447; protein.
DR Bgee; ENSG00000171960; Expressed in embryo and 205 other tissues.
DR ExpressionAtlas; O43447; baseline and differential.
DR Genevisible; O43447; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005681; C:spliceosomal complex; IC:BHF-UCL.
DR GO; GO:0071001; C:U4/U6 snRNP; IDA:BHF-UCL.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:BHF-UCL.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:BHF-UCL.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Direct protein sequencing; Isomerase; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Rotamase; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..177
FT /note="Peptidyl-prolyl cis-trans isomerase H"
FT /id="PRO_0000064162"
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:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT VAR_SEQ 1..51
FT /note="MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEF
FT -> MIAGDSDR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056587"
FT MUTAGEN 133
FT /note="W->F: Abolishes inhibition by cyclosporin A."
FT /evidence="ECO:0000269|PubMed:11823439"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:1MZW"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1MZW"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1MZW"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1MZW"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1MZW"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1MZW"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:1MZW"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:1MZW"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1MZW"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:1MZW"
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
