ID   PPIH_HUMAN              Reviewed;         177 AA.
AC   O43447;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-JAN-2012, entry version 104.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE            Short=PPIase H;
DE            EC=5.2.1.8;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164, AND
RP   INTERACTION WITH PRPF3; PRPF4 AND U4/U6 SNRNPS.
RC   TISSUE=Liver;
RX   MEDLINE=98067393; PubMed=9404889;
RA   Horowitz D.S., Kobayashi R., Krainer A.R.;
RT   "A new cyclophilin and the human homologues of yeast Prp3 and Prp4
RT   form a complex associated with U4/U6 snRNPs.";
RL   RNA 3:1374-1387(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-67; 71-81 AND
RP   153-164, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE
RP   U4/U5/U6 TRI-SNRNP COMPLEX.
RC   TISSUE=Liver;
RX   MEDLINE=98230239; 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
RT   cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD
RT   proteins.";
RL   RNA 4:127-141(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF TRP-133, AND INTERACTION WITH PRPF4 AND
RP   PRPF18.
RX   MEDLINE=21681414; 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   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [6]
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.,
RA   Buerckstuemmer T., 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   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177.
RX   MEDLINE=20179828; PubMed=10713041; DOI=10.1074/jbc.275.11.7439;
RA   Reidt U., Reuter K., Achsel T., Ingelfinger D., Luehrmann R.,
RA   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   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4,
RP   AND FUNCTION.
RX   MEDLINE=22758607; PubMed=12875835; DOI=10.1016/S0022-2836(03)00684-3;
RA   Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R.,
RA   Ficner R.;
RT   "Crystal structure of a complex between human spliceosomal cyclophilin
RT   H and a U4/U6 snRNP-60K peptide.";
RL   J. Mol. Biol. 331:45-56(2003).
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. May act as a
CC       chaperone.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited by cyclosporin A.
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. This complex interacts with the U4/U5/U6 tri-snRNP
CC       complex. Heterodimer with PRPF18.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm. Note=Colocalizes
CC       with spliceosomal snRNPs. A small proportion may also be
CC       cytoplasmic.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       H subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF016371; AAC51927.1; -; mRNA.
DR   EMBL; AF036331; AAC60793.1; -; mRNA.
DR   EMBL; BC003412; AAH03412.1; -; mRNA.
DR   IPI; IPI00007346; -.
DR   RefSeq; NP_006338.1; NM_006347.3.
DR   UniGene; Hs.256639; -.
DR   PDB; 1MZW; X-ray; 2.00 A; A=1-177.
DR   PDB; 1QOI; X-ray; 2.00 A; A=1-177.
DR   PDBsum; 1MZW; -.
DR   PDBsum; 1QOI; -.
DR   ProteinModelPortal; O43447; -.
DR   SMR; O43447; 5-177.
DR   IntAct; O43447; 5.
DR   MINT; MINT-270606; -.
DR   STRING; O43447; -.
DR   PhosphoSite; O43447; -.
DR   PRIDE; O43447; -.
DR   Ensembl; ENST00000304979; ENSP00000306614; ENSG00000171960.
DR   GeneID; 10465; -.
DR   KEGG; hsa:10465; -.
DR   UCSC; uc001chq.1; human.
DR   CTD; 10465; -.
DR   GeneCards; GC01P043097; -.
DR   H-InvDB; HIX0199949; -.
DR   HGNC; HGNC:14651; PPIH.
DR   MIM; 606095; gene.
DR   neXtProt; NX_O43447; -.
DR   PharmGKB; PA33586; -.
DR   eggNOG; prNOG07606; -.
DR   HOGENOM; HBG610621; -.
DR   HOVERGEN; HBG001065; -.
DR   InParanoid; O43447; -.
DR   OMA; GPNSNGC; -.
DR   OrthoDB; EOG4ZS946; -.
DR   PhylomeDB; O43447; -.
DR   DrugBank; DB00172; L-Proline.
DR   NextBio; 39685; -.
DR   ArrayExpress; O43447; -.
DR   Bgee; O43447; -.
DR   CleanEx; HS_PPIH; -.
DR   Genevestigator; O43447; -.
DR   GermOnline; ENSG00000171960; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL.
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; TAS:ProtInc.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
DR   GO; GO:0005515; F:protein binding; IPI:BHF-UCL.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IC:BHF-UCL.
DR   GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR   GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR   InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   KO; K09567; -.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; CSA_PPIase; 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; Chaperone; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Isomerase; mRNA processing; mRNA splicing;
KW   Nucleus; Reference proteome; Rotamase; Spliceosome.
FT   CHAIN         1    177       Peptidyl-prolyl cis-trans isomerase H.
FT                                /FTId=PRO_0000064162.
FT   DOMAIN       14    176       PPIase cyclophilin-type.
FT   MOD_RES      38     38       N6-acetyllysine.
FT   MUTAGEN     133    133       W->F: Abolishes inhibition by cyclosporin
FT                                A.
FT   STRAND       12     19
FT   STRAND       22     31
FT   TURN         33     35
FT   HELIX        37     48
FT   STRAND       67     69
FT   TURN         70     72
FT   STRAND       73     76
FT   TURN         79     81
FT   STRAND       82     84
FT   STRAND      109    112
FT   STRAND      124    129
FT   HELIX       132    134
FT   TURN        135    137
FT   STRAND      140    146
FT   HELIX       148    155
FT   HELIX       161    163
FT   STRAND      165    167
FT   STRAND      169    176
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
//