[1]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164, AND INTERACTION WITH PRPF3; PRPF4 AND U4/U6 SNRNPS. TISSUE=Liver; PubMed=9404889 [NCBI, ExPASy, EBI, Israel, Japan] Horowitz D.S., Kobayashi R., Krainer A.R.; "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs."; RNA 3:1374-1387(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-67; 71-81 AND 153-164, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE U4/U5/U6 TRI-SNRNP COMPLEX. TISSUE=Liver; PubMed=9570313 [NCBI, ExPASy, EBI, Israel, Japan] Teigelkamp S., Achsel T., Mundt C., Goethel S.-F., Cronshagen U., Lane W.S., Marahiel M., Luehrmann R.; "The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins."; RNA 4:127-141(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	FUNCTION, MUTAGENESIS OF TRP-133, AND INTERACTION WITH PRPF4 AND PRPF18. DOI=10.1093/emboj/21.3.470; PubMed=11823439 [NCBI, ExPASy, EBI, Israel, Japan] Horowitz D.S., Lee E.J., Mabon S.A., Misteli T.; "A cyclophilin functions in pre-mRNA splicing."; EMBO J. 21:470-480(2002).
[5]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[6]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177. DOI=10.1074/jbc.275.11.7439; PubMed=10713041 [NCBI, ExPASy, EBI, Israel, Japan] Reidt U., Reuter K., Achsel T., Ingelfinger D., Luehrmann R., Ficner R.; "Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin."; J. Biol. Chem. 275:7439-7442(2000).
[7]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4, AND FUNCTION. DOI=10.1016/S0022-2836(03)00684-3; PubMed=12875835 [NCBI, ExPASy, EBI, Israel, Japan] Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R., Ficner R.; "Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide."; J. Mol. Biol. 331:45-56(2003).

Comments

FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex. May act as a chaperone.
CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
SUBUNIT: Interacts directly with PRPF4. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. This complex interacts with the U4/U5/U6 tri-snRNP complex. Heterodimer with PRPF18.
SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.
MISCELLANEOUS: Inhibited by cyclosporin A.
SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H subfamily.
SIMILARITY: Contains 1 PPIase cyclophilin-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF016371; AAC51927.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF036331; AAC60793.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003412; AAH03412.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00007346; -.

NP_006338.1; -.

3D structure databases

PDB

1MZW; X-ray; 2.00 A; A=1-177.	[ExPASy / RCSB / EBI]
1QOI; X-ray; 2.00 A; A=1-177.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MZW; -.
1QOI; -.

ModBase

O43447.

Protein-protein interaction databases

IntAct

O43447; 1.

Enzyme and pathway databases

BRENDA

5.2.1.8; 247.

Organism-specific databases

GeneCards

GC01P042897; -.

H-InvDB

HIX0000490; -.
HIX0056545; -.

HGNC:14651; PPIH.

606095; gene. [NCBI / EBI]

PharmGKB

PA33586; -.

Gene expression databases

O43447; -.

O43447; -.

HS_PPIH; -.

ENSG00000171960; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016607;	Cellular component: nuclear speck (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005681;	Cellular component: spliceosome (traceable author statement from ProtInc).
GO:0016018;	Molecular function: cyclosporin A binding (traceable author statement from ProtInc).
GO:0003755;	Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006397;	Biological process: mRNA processing (inferred from electronic annotation from UniProtKB-KW).
GO:0006461;	Biological process: protein complex assembly (traceable author statement from ProtInc).
GO:0006457;	Biological process: protein folding (traceable author statement from ProtInc).
GO:0008380;	Biological process: RNA splicing (inferred from electronic annotation from UniProtKB-KW).
GO:0006608;	Biological process: snRNP protein import into nucleus (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002130; PPIase_cyclophilin.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.100.10; PPIase_cyclophilin; 1.

Pfam

PF00160; Pro_isomerase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00153; CSAPPISMRASE.

PROSITE

PS00170; CSA_PPIASE_1; 1.
PS50072; CSA_PPIASE_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O43447; -.

Genome annotation databases

Ensembl

ENSG00000171960; Homo sapiens. [Contig view]

GeneID

10465; -.

KEGG

hsa:10465; -.

Phylogenomic databases

HOGENOM

O43447; -.

HOVERGEN

O43447; -.

OMA

O43447; DGLLIMR.

Other

DB00172; L-Proline.

39685; -.

PPIH; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase; mRNA processing; mRNA splicing; Nucleus; Rotamase; Spliceosome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 177`	`177`	`Peptidyl-prolyl cis-trans isomerase H.`	`PRO_0000064162`
`DOMAIN`	`14 176`	`163`	`PPIase cyclophilin-type.`
`MUTAGEN`	`133 133`		`W->F: Abolishes inhibition by cyclosporin A.`
`STRAND`	`12 19`	`8`
`STRAND`	`22 31`	`10`
`TURN`	`33 35`	`3`
`HELIX`	`37 48`	`12`
`STRAND`	`67 69`	`3`
`TURN`	`70 72`	`3`
`STRAND`	`73 76`	`4`
`TURN`	`79 81`	`3`
`STRAND`	`82 84`	`3`
`STRAND`	`109 112`	`4`
`STRAND`	`124 129`	`6`
`HELIX`	`132 134`	`3`
`TURN`	`135 137`	`3`
`STRAND`	`140 146`	`7`
`HELIX`	`148 155`	`8`
`HELIX`	`161 163`	`3`
`STRAND`	`165 167`	`3`
`STRAND`	`169 176`	`8`

Sequence information

Length: 177 AA [This is the length of the unprocessed precursor]

Molecular weight: 19208 Da [This is the MW of the unprocessed precursor]

CRC64: 566BCE6361E0F339 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE FRKDGVPIGY 

        70         80         90        100        110        120 
KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN 

       130        140        150        160        170 
GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM

O43447 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools