Full text data of PPIL1
PPIL1
(CYPL1)
[Confidence: low (only semi-automatic identification from reviews)]
Peptidyl-prolyl cis-trans isomerase-like 1; PPIase; 5.2.1.8 (Rotamase PPIL1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Peptidyl-prolyl cis-trans isomerase-like 1; PPIase; 5.2.1.8 (Rotamase PPIL1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y3C6
ID PPIL1_HUMAN Reviewed; 166 AA.
AC Q9Y3C6; O15001; Q5TDC9;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 1;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase PPIL1;
GN Name=PPIL1; Synonyms=CYPL1; ORFNames=CGI-124, UNQ2425/PRO4984;
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].
RC TISSUE=Fetal brain;
RX PubMed=8978786;
RA Ozaki K., Fujiwara T., Kawai A., Shimizu F., Takami S., Okuno S.,
RA Takeda S., Shimada Y., Nagata M., Watanabe T., Takaichi A.,
RA Takahashi E., Nakamura Y., Shin S.;
RT "Cloning, expression and chromosomal mapping of a novel cyclophilin-
RT related gene (PPIL1) from human fetal brain.";
RL Cytogenet. Cell Genet. 72:242-245(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [7]
RP FUNCTION, KINETIC PARAMETERS, ENZYME REGULATION, CYCLOSPORIN A
RP BINDING, INTERACTION WITH SNW1, AND STRUCTURE BY NMR.
RX PubMed=16595688; DOI=10.1074/jbc.M511155200;
RA Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y.,
RA Huang Q., Zhang Q.;
RT "Solution structure of human peptidyl prolyl isomerase-like protein 1
RT and insights into its interaction with SKIP.";
RL J. Biol. Chem. 281:15900-15908(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), AND INTERACTION WITH SNW1.
RX PubMed=20368803; DOI=10.1371/journal.pone.0010013;
RA Stegmann C.M., Luhrmann R., Wahl M.C.;
RT "The crystal structure of PPIL1 bound to cyclosporine A suggests a
RT binding mode for a linear epitope of the SKIP protein.";
RL PLoS ONE 5:E10013-E10013(2010).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. May be involved in pre-mRNA splicing.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- ENZYME REGULATION: Inhibited by Cyclosporin A.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide;
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
CC SNW1.
CC -!- INTERACTION:
CC Q13573:SNW1; NbExp=4; IntAct=EBI-2557649, EBI-632715;
CC Q9BRX9:WDR83; NbExp=2; IntAct=EBI-2557649, EBI-7705033;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the most abundant expression
CC in heart and skeletal muscle.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC subfamily.
CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR EMBL; AF151882; AAD34119.1; -; mRNA.
DR EMBL; AY359032; AAQ89391.1; -; mRNA.
DR EMBL; Z85996; CAI20894.1; -; Genomic_DNA.
DR EMBL; AL122034; CAI20894.1; JOINED; Genomic_DNA.
DR EMBL; AL122034; CAI23296.1; -; Genomic_DNA.
DR EMBL; Z85996; CAI23296.1; JOINED; Genomic_DNA.
DR EMBL; CH471081; EAX03916.1; -; Genomic_DNA.
DR EMBL; BC003048; AAH03048.1; -; mRNA.
DR RefSeq; NP_057143.1; NM_016059.4.
DR UniGene; Hs.27693; -.
DR PDB; 1XWN; NMR; -; A=1-166.
DR PDB; 2K7N; NMR; -; A=1-166.
DR PDB; 2X7K; X-ray; 1.15 A; A=1-166.
DR PDBsum; 1XWN; -.
DR PDBsum; 2K7N; -.
DR PDBsum; 2X7K; -.
DR ProteinModelPortal; Q9Y3C6; -.
DR SMR; Q9Y3C6; 1-166.
DR IntAct; Q9Y3C6; 15.
DR MINT; MINT-4654404; -.
DR STRING; 9606.ENSP00000362803; -.
DR PhosphoSite; Q9Y3C6; -.
DR DMDM; 20177874; -.
DR PaxDb; Q9Y3C6; -.
DR PeptideAtlas; Q9Y3C6; -.
DR PRIDE; Q9Y3C6; -.
DR DNASU; 51645; -.
DR Ensembl; ENST00000373699; ENSP00000362803; ENSG00000137168.
DR GeneID; 51645; -.
DR KEGG; hsa:51645; -.
DR UCSC; uc003omu.2; human.
DR CTD; 51645; -.
DR GeneCards; GC06M036869; -.
DR HGNC; HGNC:9260; PPIL1.
DR MIM; 601301; gene.
DR neXtProt; NX_Q9Y3C6; -.
DR PharmGKB; PA33587; -.
DR eggNOG; COG0652; -.
DR HOGENOM; HOG000065981; -.
DR HOVERGEN; HBG001065; -.
DR InParanoid; Q9Y3C6; -.
DR KO; K12733; -.
DR OMA; PHHAERI; -.
DR OrthoDB; EOG7NW6BK; -.
DR PhylomeDB; Q9Y3C6; -.
DR ChiTaRS; PPIL1; human.
DR EvolutionaryTrace; Q9Y3C6; -.
DR GeneWiki; PPIL1; -.
DR GenomeRNAi; 51645; -.
DR NextBio; 55588; -.
DR PRO; PR:Q9Y3C6; -.
DR Bgee; Q9Y3C6; -.
DR CleanEx; HS_PPIL1; -.
DR Genevestigator; Q9Y3C6; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
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; Complete proteome; Isomerase; mRNA processing;
KW mRNA splicing; Polymorphism; Reference proteome; Rotamase;
KW Spliceosome.
FT CHAIN 1 166 Peptidyl-prolyl cis-trans isomerase-like
FT 1.
FT /FTId=PRO_0000064164.
FT DOMAIN 10 164 PPIase cyclophilin-type.
FT REGION 54 65 Cyclosporin A binding.
FT REGION 70 71 Cyclosporin A binding.
FT REGION 99 104 Cyclosporin A binding.
FT REGION 109 113 Cyclosporin A binding.
FT BINDING 119 119 Cyclosporin A.
FT BINDING 125 125 Cyclosporin A.
FT VARIANT 36 36 C -> S (in dbSNP:rs12194408).
FT /FTId=VAR_051772.
FT STRAND 12 18
FT STRAND 21 27
FT TURN 29 31
FT HELIX 33 45
FT TURN 46 50
FT STRAND 55 57
FT TURN 58 60
FT STRAND 61 64
FT STRAND 69 72
FT STRAND 97 100
FT STRAND 102 104
FT STRAND 112 117
FT HELIX 120 122
FT TURN 123 125
FT STRAND 128 134
FT HELIX 136 142
FT STRAND 149 151
FT STRAND 153 155
FT STRAND 158 164
SQ SEQUENCE 166 AA; 18237 MW; 2872DC3336CD05E4 CRC64;
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF
MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ
WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSG
//
ID PPIL1_HUMAN Reviewed; 166 AA.
AC Q9Y3C6; O15001; Q5TDC9;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 1;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase PPIL1;
GN Name=PPIL1; Synonyms=CYPL1; ORFNames=CGI-124, UNQ2425/PRO4984;
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].
RC TISSUE=Fetal brain;
RX PubMed=8978786;
RA Ozaki K., Fujiwara T., Kawai A., Shimizu F., Takami S., Okuno S.,
RA Takeda S., Shimada Y., Nagata M., Watanabe T., Takaichi A.,
RA Takahashi E., Nakamura Y., Shin S.;
RT "Cloning, expression and chromosomal mapping of a novel cyclophilin-
RT related gene (PPIL1) from human fetal brain.";
RL Cytogenet. Cell Genet. 72:242-245(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [7]
RP FUNCTION, KINETIC PARAMETERS, ENZYME REGULATION, CYCLOSPORIN A
RP BINDING, INTERACTION WITH SNW1, AND STRUCTURE BY NMR.
RX PubMed=16595688; DOI=10.1074/jbc.M511155200;
RA Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y.,
RA Huang Q., Zhang Q.;
RT "Solution structure of human peptidyl prolyl isomerase-like protein 1
RT and insights into its interaction with SKIP.";
RL J. Biol. Chem. 281:15900-15908(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), AND INTERACTION WITH SNW1.
RX PubMed=20368803; DOI=10.1371/journal.pone.0010013;
RA Stegmann C.M., Luhrmann R., Wahl M.C.;
RT "The crystal structure of PPIL1 bound to cyclosporine A suggests a
RT binding mode for a linear epitope of the SKIP protein.";
RL PLoS ONE 5:E10013-E10013(2010).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. May be involved in pre-mRNA splicing.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- ENZYME REGULATION: Inhibited by Cyclosporin A.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide;
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with
CC SNW1.
CC -!- INTERACTION:
CC Q13573:SNW1; NbExp=4; IntAct=EBI-2557649, EBI-632715;
CC Q9BRX9:WDR83; NbExp=2; IntAct=EBI-2557649, EBI-7705033;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with the most abundant expression
CC in heart and skeletal muscle.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL1
CC subfamily.
CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR EMBL; AF151882; AAD34119.1; -; mRNA.
DR EMBL; AY359032; AAQ89391.1; -; mRNA.
DR EMBL; Z85996; CAI20894.1; -; Genomic_DNA.
DR EMBL; AL122034; CAI20894.1; JOINED; Genomic_DNA.
DR EMBL; AL122034; CAI23296.1; -; Genomic_DNA.
DR EMBL; Z85996; CAI23296.1; JOINED; Genomic_DNA.
DR EMBL; CH471081; EAX03916.1; -; Genomic_DNA.
DR EMBL; BC003048; AAH03048.1; -; mRNA.
DR RefSeq; NP_057143.1; NM_016059.4.
DR UniGene; Hs.27693; -.
DR PDB; 1XWN; NMR; -; A=1-166.
DR PDB; 2K7N; NMR; -; A=1-166.
DR PDB; 2X7K; X-ray; 1.15 A; A=1-166.
DR PDBsum; 1XWN; -.
DR PDBsum; 2K7N; -.
DR PDBsum; 2X7K; -.
DR ProteinModelPortal; Q9Y3C6; -.
DR SMR; Q9Y3C6; 1-166.
DR IntAct; Q9Y3C6; 15.
DR MINT; MINT-4654404; -.
DR STRING; 9606.ENSP00000362803; -.
DR PhosphoSite; Q9Y3C6; -.
DR DMDM; 20177874; -.
DR PaxDb; Q9Y3C6; -.
DR PeptideAtlas; Q9Y3C6; -.
DR PRIDE; Q9Y3C6; -.
DR DNASU; 51645; -.
DR Ensembl; ENST00000373699; ENSP00000362803; ENSG00000137168.
DR GeneID; 51645; -.
DR KEGG; hsa:51645; -.
DR UCSC; uc003omu.2; human.
DR CTD; 51645; -.
DR GeneCards; GC06M036869; -.
DR HGNC; HGNC:9260; PPIL1.
DR MIM; 601301; gene.
DR neXtProt; NX_Q9Y3C6; -.
DR PharmGKB; PA33587; -.
DR eggNOG; COG0652; -.
DR HOGENOM; HOG000065981; -.
DR HOVERGEN; HBG001065; -.
DR InParanoid; Q9Y3C6; -.
DR KO; K12733; -.
DR OMA; PHHAERI; -.
DR OrthoDB; EOG7NW6BK; -.
DR PhylomeDB; Q9Y3C6; -.
DR ChiTaRS; PPIL1; human.
DR EvolutionaryTrace; Q9Y3C6; -.
DR GeneWiki; PPIL1; -.
DR GenomeRNAi; 51645; -.
DR NextBio; 55588; -.
DR PRO; PR:Q9Y3C6; -.
DR Bgee; Q9Y3C6; -.
DR CleanEx; HS_PPIL1; -.
DR Genevestigator; Q9Y3C6; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR InterPro; IPR002130; Cyclophilin-like_PPIase_dom.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
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; Complete proteome; Isomerase; mRNA processing;
KW mRNA splicing; Polymorphism; Reference proteome; Rotamase;
KW Spliceosome.
FT CHAIN 1 166 Peptidyl-prolyl cis-trans isomerase-like
FT 1.
FT /FTId=PRO_0000064164.
FT DOMAIN 10 164 PPIase cyclophilin-type.
FT REGION 54 65 Cyclosporin A binding.
FT REGION 70 71 Cyclosporin A binding.
FT REGION 99 104 Cyclosporin A binding.
FT REGION 109 113 Cyclosporin A binding.
FT BINDING 119 119 Cyclosporin A.
FT BINDING 125 125 Cyclosporin A.
FT VARIANT 36 36 C -> S (in dbSNP:rs12194408).
FT /FTId=VAR_051772.
FT STRAND 12 18
FT STRAND 21 27
FT TURN 29 31
FT HELIX 33 45
FT TURN 46 50
FT STRAND 55 57
FT TURN 58 60
FT STRAND 61 64
FT STRAND 69 72
FT STRAND 97 100
FT STRAND 102 104
FT STRAND 112 117
FT HELIX 120 122
FT TURN 123 125
FT STRAND 128 134
FT HELIX 136 142
FT STRAND 149 151
FT STRAND 153 155
FT STRAND 158 164
SQ SEQUENCE 166 AA; 18237 MW; 2872DC3336CD05E4 CRC64;
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF
MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ
WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSG
//
MIM
601301
*RECORD*
*FIELD* NO
601301
*FIELD* TI
*601301 PEPTIDYL-PROLYL ISOMERASE-LIKE 1; PPIL1
;;CYCLOPHILIN-RELATED GENE 1; CYPL1
read more*FIELD* TX
Cyclophilin (see 123840), first identified as a protein with high
binding affinity for the immunosuppressive agent cyclosporin A, is one
of the most effective therapeutic agents for prevention of graft
rejection after organ transplantation.
CLONING
Ozaki et al. (1996) isolated a human cDNA clone encoding a protein
homologous to cyclophilins and showed that it is conserved in species
ranging from human to prokaryotes. This cDNA contained an open reading
frame of 498 nucleotides encoding a polypeptide of 166 amino acids. The
predicted amino acid sequence had 41.6% homology to the human
cyclophilins. Northern blot analysis indicated ubiquitous expression in
adult human tissues, with the most abundant expression in heart and
skeletal muscle.
MAPPING
Ozaki et al. (1996) localized the PPIL1 gene to 2p23.3-p23.1 by FISH.
However, Mann et al. (1998) assigned the PPIL1 gene to 6p21.1 by FISH
and radiation hybrid mapping.
*FIELD* RF
1. Mann, S. S.; Pettenati, M. J.; von Kap-herr, C.; Hart, T. C.:
Reassignment of peptidyl prolyl isomerase-like 1 gene (PPIL1) to human
chromosome region 6p21.1 by radiation hybrid mapping and fluorescence
in situ hybridization. Cytogenet. Cell Genet. 83: 228-229, 1998.
2. Ozaki, K.; Fujiwara, T.; Kawai, A.; Shimizu, F.; Takami, S.; Okuno,
S.; Takeda, S.; Shimada, Y.; Nagata, M.; Watanabe, T.; Takaichi, A.;
Takahashi, E.; Nakamura, Y.; Shin, S.: Cloning, expression and chromosomal
mapping of a novel cyclophilin-related gene (PPIL1) from human fetal
brain. Cytogenet. Cell Genet. 72: 242-245, 1996.
*FIELD* CN
Carol A. Bocchini - updated: 6/1/1999
*FIELD* CD
Victor A. McKusick: 6/11/1996
*FIELD* ED
carol: 07/10/2001
mgross: 6/1/1999
carol: 6/1/1999
mark: 6/11/1996
*RECORD*
*FIELD* NO
601301
*FIELD* TI
*601301 PEPTIDYL-PROLYL ISOMERASE-LIKE 1; PPIL1
;;CYCLOPHILIN-RELATED GENE 1; CYPL1
read more*FIELD* TX
Cyclophilin (see 123840), first identified as a protein with high
binding affinity for the immunosuppressive agent cyclosporin A, is one
of the most effective therapeutic agents for prevention of graft
rejection after organ transplantation.
CLONING
Ozaki et al. (1996) isolated a human cDNA clone encoding a protein
homologous to cyclophilins and showed that it is conserved in species
ranging from human to prokaryotes. This cDNA contained an open reading
frame of 498 nucleotides encoding a polypeptide of 166 amino acids. The
predicted amino acid sequence had 41.6% homology to the human
cyclophilins. Northern blot analysis indicated ubiquitous expression in
adult human tissues, with the most abundant expression in heart and
skeletal muscle.
MAPPING
Ozaki et al. (1996) localized the PPIL1 gene to 2p23.3-p23.1 by FISH.
However, Mann et al. (1998) assigned the PPIL1 gene to 6p21.1 by FISH
and radiation hybrid mapping.
*FIELD* RF
1. Mann, S. S.; Pettenati, M. J.; von Kap-herr, C.; Hart, T. C.:
Reassignment of peptidyl prolyl isomerase-like 1 gene (PPIL1) to human
chromosome region 6p21.1 by radiation hybrid mapping and fluorescence
in situ hybridization. Cytogenet. Cell Genet. 83: 228-229, 1998.
2. Ozaki, K.; Fujiwara, T.; Kawai, A.; Shimizu, F.; Takami, S.; Okuno,
S.; Takeda, S.; Shimada, Y.; Nagata, M.; Watanabe, T.; Takaichi, A.;
Takahashi, E.; Nakamura, Y.; Shin, S.: Cloning, expression and chromosomal
mapping of a novel cyclophilin-related gene (PPIL1) from human fetal
brain. Cytogenet. Cell Genet. 72: 242-245, 1996.
*FIELD* CN
Carol A. Bocchini - updated: 6/1/1999
*FIELD* CD
Victor A. McKusick: 6/11/1996
*FIELD* ED
carol: 07/10/2001
mgross: 6/1/1999
carol: 6/1/1999
mark: 6/11/1996