ID PPIA_HUMAN Reviewed; 165 AA.
AC P62937; A8K220; P05092; Q3KQW3; Q6IBU5; Q96IX3; Q9BRU4; Q9BTY9;
AC Q9UC61;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 01-MAY-2013, entry version 110.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE Short=PPIase A;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin A;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase A;
GN Name=PPIA; Synonyms=CYPA;
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=Leukemic T-cell;
RX PubMed=3297675;
RA Haendler B., Hofer-Warbinek R., Hofer E.;
RT "Complementary DNA for human T-cell cyclophilin.";
RL EMBO J. 6:947-950(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2197089; DOI=10.1111/j.1432-1033.1990.tb15598.x;
RA Haendler B., Hofer E.;
RT "Characterization of the human cyclophilin gene and of related
RT processed pseudogenes.";
RL Eur. J. Biochem. 190:477-482(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, Cervix, Colon, Lung, Skeletal muscle, Skin,
RC and Urinary bladder;
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 [8]
RP PROTEIN SEQUENCE OF 2-30.
RX PubMed=7657784;
RA Meier U., Beier-Hellwig K., Klug J., Linder D., Beier H.M.;
RT "Identification of cyclophilin A from human decidual and placental
RT tissue in the first trimester of pregnancy.";
RL Hum. Reprod. 10:1305-1310(1995).
RN [9]
RP PROTEIN SEQUENCE OF 2-19.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-31; 56-69; 77-118; 132-144 AND 155-165, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT VAL-2, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [12]
RP MUTAGENESIS OF TRP-121.
RX PubMed=2001362; DOI=10.1021/bi00223a003;
RA Liu J., Chen C.-M., Walsh C.T.;
RT "Human and Escherichia coli cyclophilins: sensitivity to inhibition by
RT the immunosuppressant cyclosporin A correlates with a specific
RT tryptophan residue.";
RL Biochemistry 30:2306-2310(1991).
RN [13]
RP INTERACTION WITH HIV-1 CAPSID PROTEIN.
RX PubMed=8513493; DOI=10.1016/0092-8674(93)90637-6;
RA Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.;
RT "Human immunodeficiency virus type 1 Gag protein binds to cyclophilins
RT A and B.";
RL Cell 73:1067-1078(1993).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=16527992; DOI=10.1161/01.RES.0000216405.85080.a6;
RA Suzuki J., Jin Z.G., Meoli D.F., Matoba T., Berk B.C.;
RT "Cyclophilin A is secreted by a vesicular pathway in vascular smooth
RT muscle cells.";
RL Circ. Res. 98:811-817(2006).
RN [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-28, AND MASS
RP SPECTROMETRY.
RX PubMed=18781797; DOI=10.1021/pr800468j;
RA Meierhofer D., Wang X., Huang L., Kaiser P.;
RT "Quantitative analysis of global ubiquitination in HeLa cells by mass
RT spectrometry.";
RL J. Proteome Res. 7:4566-4576(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-44; LYS-76; LYS-82;
RP LYS-125 AND LYS-131, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND STRUCTURE BY NMR.
RX PubMed=1896075; DOI=10.1038/353276a0;
RA Kallen J., Spitzfaden C., Zurini M.G.M., Wider G., Widmer H.,
RA Wuethrich K., Walkinshaw M.D.;
RT "Structure of human cyclophilin and its binding site for cyclosporin A
RT determined by X-ray crystallography and NMR spectroscopy.";
RL Nature 353:276-279(1991).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1946361; DOI=10.1073/pnas.88.21.9483;
RA Ke H., Zydowsky L.D., Liu J., Walsh C.T.;
RT "Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A
RT resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9483-9487(1991).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CYCLOPHILIN.
RX PubMed=8421501; DOI=10.1038/361091a0;
RA Pfuegl G., Kallen J., Schirmer T., Jansonius J.N., Zurini M.G.M.,
RA Walkinshaw M.D.;
RT "X-ray structure of a decameric cyclophilin-cyclosporin crystal
RT complex.";
RL Nature 361:91-94(1993).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=8263916; DOI=10.1006/jmbi.1993.1664;
RA Mikol V., Kallen J., Pfluegl G., Walkinshaw M.D.;
RT "X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal
RT complex at 2.1-A resolution.";
RL J. Mol. Biol. 234:1119-1130(1993).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8652511; DOI=10.1021/bi9602775;
RA Zhao Y., Ke H.;
RT "Crystal structure implies that cyclophilin predominantly catalyzes
RT the trans to cis isomerization.";
RL Biochemistry 35:7356-7361(1996).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
RX PubMed=9385632;
RA Vajdos F.F., Yoo S., Houseweart M., Sundquist W.I., Hill C.P.;
RT "Crystal structure of cyclophilin A complexed with a binding site
RT peptide from the HIV-1 capsid protein.";
RL Protein Sci. 6:2297-2307(1997).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9769216; DOI=10.1006/jmbi.1998.2108;
RA Kallen J., Mikol V., Taylor P., Walkinshaw M.D.;
RT "X-ray structures and analysis of 11 cyclosporin derivatives complexed
RT with cyclophilin A.";
RL J. Mol. Biol. 283:435-449(1998).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
RX PubMed=12218175; DOI=10.1073/pnas.192206699;
RA Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.;
RT "Crystal structure of calcineurin-cyclophilin-cyclosporin shows common
RT but distinct recognition of immunophilin-drug complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
RX PubMed=12357034; DOI=10.1073/pnas.212504399;
RA Jin L., Harrison S.C.;
RT "Crystal structure of human calcineurin complexed with cyclosporin A
RT and human cyclophilin.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
RN [28]
RP STRUCTURE BY NMR OF COMPLEX WITH CYCLOPHILIN.
RX PubMed=8421500; DOI=10.1038/361088a0;
RA Theriault Y., Logan T.M., Meadows R., Yu L., Olejniczak E.T.,
RA Holzman T.F., Simmer R.L., Fesik S.W.;
RT "Solution structure of the cyclosporin A/cyclophilin complex by NMR.";
RL Nature 361:88-91(1993).
RN [29]
RP STRUCTURE BY NMR.
RX PubMed=9299338; DOI=10.1006/jmbi.1997.1220;
RA Ottiger M., Zerbe O., Guentert P., Wuethrich K.;
RT "The NMR solution conformation of unligated human cyclophilin A.";
RL J. Mol. Biol. 272:64-81(1997).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) ALONE AND IN COMPLEX WITH
RP CYCLOSPORINE AND HIV-1 CAPSID, AND ACETYLATION AT LYS-125.
RX PubMed=20364129; DOI=10.1038/nchembio.342;
RA Lammers M., Neumann H., Chin J.W., James L.C.;
RT "Acetylation regulates cyclophilin A catalysis, immunosuppression and
RT HIV isomerization.";
RL Nat. Chem. Biol. 6:331-337(2010).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC the cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC -!- SUBUNIT: Interacts with HIV-1 Capsid protein.
CC -!- INTERACTION:
CC Q72497:gag (xeno); NbExp=6; IntAct=EBI-437708, EBI-1036263;
CC Q16849:PTPRN; NbExp=3; IntAct=EBI-437708, EBI-728153;
CC O00267:SUPT5H; NbExp=2; IntAct=EBI-437708, EBI-710464;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion occurs
CC in response to oxidative stress in vascular smooth muscle through
CC a vesicular secretory pathway that involves actin remodeling and
CC myosin II activation, and mediates ERK1/2 activation.
CC -!- PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to
CC trans isomerization and stabilizes cis rather than trans forms of
CC the HIV-1 capsid. PPIA acetylation also antagonizes the
CC immunosuppressive effects of cyclosporine by inhibiting the
CC sequential steps of cyclosporine binding and calcineurin
CC inhibition.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC A subfamily.
CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ppia/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry;
CC URL="http://en.wikipedia.org/wiki/Cyclophilin";
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DR EMBL; Y00052; CAA68264.1; -; mRNA.
DR EMBL; X52851; CAA37039.1; -; Genomic_DNA.
DR EMBL; AK290085; BAF82774.1; -; mRNA.
DR EMBL; CR456707; CAG32988.1; -; mRNA.
DR EMBL; AB451307; BAG70121.1; -; mRNA.
DR EMBL; AB451438; BAG70252.1; -; mRNA.
DR EMBL; AY739283; AAU13906.1; -; Genomic_DNA.
DR EMBL; BC000689; AAH00689.1; -; mRNA.
DR EMBL; BC003026; AAH03026.2; -; mRNA.
DR EMBL; BC005320; AAH05320.1; -; mRNA.
DR EMBL; BC005982; AAH05982.1; -; mRNA.
DR EMBL; BC007104; AAH07104.1; -; mRNA.
DR EMBL; BC013915; AAH13915.1; -; mRNA.
DR EMBL; BC073992; AAH73992.1; -; mRNA.
DR EMBL; BC106030; AAI06031.1; -; mRNA.
DR EMBL; BC137057; AAI37058.1; -; mRNA.
DR EMBL; BC137058; AAI37059.1; -; mRNA.
DR IPI; IPI00419585; -.
DR PIR; A94496; CSHUA.
DR RefSeq; NP_066953.1; NM_021130.3.
DR UniGene; Hs.356331; -.
DR PDB; 1AK4; X-ray; 2.36 A; A/B=2-164.
DR PDB; 1AWQ; X-ray; 1.58 A; A=2-165.
DR PDB; 1AWR; X-ray; 1.58 A; A/B/C/D/E/F=2-165.
DR PDB; 1AWS; X-ray; 2.55 A; A=2-165.
DR PDB; 1AWT; X-ray; 2.55 A; A/B/C/D/E/F=2-165.
DR PDB; 1AWU; X-ray; 2.34 A; A=2-165.
DR PDB; 1AWV; X-ray; 2.34 A; A/B/C/D/E/F=2-165.
DR PDB; 1BCK; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWA; X-ray; 2.10 A; A=1-165.
DR PDB; 1CWB; X-ray; 2.20 A; A=1-165.
DR PDB; 1CWC; X-ray; 1.86 A; A=1-165.
DR PDB; 1CWF; X-ray; 1.86 A; A=1-165.
DR PDB; 1CWH; X-ray; 1.86 A; A=1-165.
DR PDB; 1CWI; X-ray; 1.90 A; A=1-165.
DR PDB; 1CWJ; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWK; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWL; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWM; X-ray; 2.00 A; A=1-165.
DR PDB; 1CWO; X-ray; 1.86 A; A=2-164.
DR PDB; 1FGL; X-ray; 1.80 A; A=2-164.
DR PDB; 1M63; X-ray; 2.80 A; C/G=1-165.
DR PDB; 1M9C; X-ray; 2.00 A; A/B=1-164.
DR PDB; 1M9D; X-ray; 1.90 A; A/B=1-164.
DR PDB; 1M9E; X-ray; 1.72 A; A/B=1-163.
DR PDB; 1M9F; X-ray; 1.73 A; A/B=1-164.
DR PDB; 1M9X; X-ray; 1.70 A; A/B/E/F=1-164.
DR PDB; 1M9Y; X-ray; 1.90 A; A/B/E/F=1-164.
DR PDB; 1MF8; X-ray; 3.10 A; C=1-165.
DR PDB; 1MIK; X-ray; 1.76 A; A=1-165.
DR PDB; 1NMK; X-ray; 2.10 A; A/B=1-165.
DR PDB; 1OCA; NMR; -; A=1-165.
DR PDB; 1RMH; X-ray; 2.40 A; A/B=2-165.
DR PDB; 1VBS; X-ray; 2.00 A; A=1-165.
DR PDB; 1VBT; X-ray; 2.30 A; A/B=1-165.
DR PDB; 1W8L; X-ray; 1.80 A; A=2-164.
DR PDB; 1W8M; X-ray; 1.65 A; A=2-164.
DR PDB; 1W8V; X-ray; 1.70 A; A=2-164.
DR PDB; 1YND; X-ray; 1.60 A; A/B=1-165.
DR PDB; 1ZKF; X-ray; 2.55 A; A/B=1-165.
DR PDB; 2ALF; X-ray; 1.90 A; A=2-164.
DR PDB; 2CPL; X-ray; 1.63 A; A=2-164.
DR PDB; 2CYH; X-ray; 1.64 A; A=2-165.
DR PDB; 2RMA; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=2-164.
DR PDB; 2RMB; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=2-164.
DR PDB; 2X25; X-ray; 1.20 A; B=2-165.
DR PDB; 2X2A; X-ray; 1.40 A; A/B=1-165.
DR PDB; 2X2C; X-ray; 2.41 A; K/M/O/Q/S=1-165.
DR PDB; 2X2D; X-ray; 1.95 A; B/C=1-165.
DR PDB; 2XGY; X-ray; 1.80 A; B=1-165.
DR PDB; 3CYH; X-ray; 1.90 A; A=2-165.
DR PDB; 3CYS; NMR; -; A=1-165.
DR PDB; 3K0M; X-ray; 1.25 A; A=1-165.
DR PDB; 3K0N; X-ray; 1.39 A; A=1-165.
DR PDB; 3K0O; X-ray; 1.55 A; A=1-165.
DR PDB; 3K0P; X-ray; 1.65 A; A=1-165.
DR PDB; 3K0Q; X-ray; 2.32 A; A=1-165.
DR PDB; 3K0R; X-ray; 2.42 A; A=1-165.
DR PDB; 3ODI; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S=1-165.
DR PDB; 3ODL; X-ray; 2.31 A; A/C/E/G/I/K/M/O/Q/S=1-165.
DR PDB; 3RDD; X-ray; 2.14 A; A=1-165.
DR PDB; 4CYH; X-ray; 2.10 A; A=2-165.
DR PDB; 5CYH; X-ray; 2.10 A; A=2-165.
DR PDBsum; 1AK4; -.
DR PDBsum; 1AWQ; -.
DR PDBsum; 1AWR; -.
DR PDBsum; 1AWS; -.
DR PDBsum; 1AWT; -.
DR PDBsum; 1AWU; -.
DR PDBsum; 1AWV; -.
DR PDBsum; 1BCK; -.
DR PDBsum; 1CWA; -.
DR PDBsum; 1CWB; -.
DR PDBsum; 1CWC; -.
DR PDBsum; 1CWF; -.
DR PDBsum; 1CWH; -.
DR PDBsum; 1CWI; -.
DR PDBsum; 1CWJ; -.
DR PDBsum; 1CWK; -.
DR PDBsum; 1CWL; -.
DR PDBsum; 1CWM; -.
DR PDBsum; 1CWO; -.
DR PDBsum; 1FGL; -.
DR PDBsum; 1M63; -.
DR PDBsum; 1M9C; -.
DR PDBsum; 1M9D; -.
DR PDBsum; 1M9E; -.
DR PDBsum; 1M9F; -.
DR PDBsum; 1M9X; -.
DR PDBsum; 1M9Y; -.
DR PDBsum; 1MF8; -.
DR PDBsum; 1MIK; -.
DR PDBsum; 1NMK; -.
DR PDBsum; 1OCA; -.
DR PDBsum; 1RMH; -.
DR PDBsum; 1VBS; -.
DR PDBsum; 1VBT; -.
DR PDBsum; 1W8L; -.
DR PDBsum; 1W8M; -.
DR PDBsum; 1W8V; -.
DR PDBsum; 1YND; -.
DR PDBsum; 1ZKF; -.
DR PDBsum; 2ALF; -.
DR PDBsum; 2CPL; -.
DR PDBsum; 2CYH; -.
DR PDBsum; 2RMA; -.
DR PDBsum; 2RMB; -.
DR PDBsum; 2X25; -.
DR PDBsum; 2X2A; -.
DR PDBsum; 2X2C; -.
DR PDBsum; 2X2D; -.
DR PDBsum; 2XGY; -.
DR PDBsum; 3CYH; -.
DR PDBsum; 3CYS; -.
DR PDBsum; 3K0M; -.
DR PDBsum; 3K0N; -.
DR PDBsum; 3K0O; -.
DR PDBsum; 3K0P; -.
DR PDBsum; 3K0Q; -.
DR PDBsum; 3K0R; -.
DR PDBsum; 3ODI; -.
DR PDBsum; 3ODL; -.
DR PDBsum; 3RDD; -.
DR PDBsum; 4CYH; -.
DR PDBsum; 5CYH; -.
DR ProteinModelPortal; P62937; -.
DR DIP; DIP-6080N; -.
DR IntAct; P62937; 33.
DR MINT; MINT-4999116; -.
DR STRING; 9606.ENSP00000419425; -.
DR PhosphoSite; P62937; -.
DR DMDM; 51702775; -.
DR DOSAC-COBS-2DPAGE; P62937; -.
DR OGP; P62937; -.
DR REPRODUCTION-2DPAGE; IPI00419585; -.
DR REPRODUCTION-2DPAGE; P62937; -.
DR SWISS-2DPAGE; P62937; -.
DR UCD-2DPAGE; P62937; -.
DR PaxDb; P62937; -.
DR PeptideAtlas; P62937; -.
DR PRIDE; P62937; -.
DR DNASU; 5478; -.
DR Ensembl; ENST00000468812; ENSP00000419425; ENSG00000196262.
DR GeneID; 5478; -.
DR KEGG; hsa:5478; -.
DR UCSC; uc003tlw.3; human.
DR CTD; 5478; -.
DR GeneCards; GC07P044803; -.
DR HGNC; HGNC:9253; PPIA.
DR HPA; CAB004655; -.
DR MIM; 123840; gene.
DR neXtProt; NX_P62937; -.
DR PharmGKB; PA33574; -.
DR eggNOG; COG0652; -.
DR HOVERGEN; HBG001065; -.
DR InParanoid; P62937; -.
DR KO; K03767; -.
DR OMA; IVIQLFP; -.
DR OrthoDB; EOG4DJJXN; -.
DR PhylomeDB; P62937; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_604; Hemostasis.
DR BindingDB; P62937; -.
DR ChEMBL; CHEMBL1949; -.
DR ChiTaRS; PPIA; human.
DR DrugBank; DB00091; Cyclosporine.
DR DrugBank; DB00172; L-Proline.
DR EvolutionaryTrace; P62937; -.
DR GenomeRNAi; 5478; -.
DR NextBio; 21206; -.
DR ArrayExpress; P62937; -.
DR Bgee; P62937; -.
DR CleanEx; HS_PPIA; -.
DR Genevestigator; P62937; -.
DR GermOnline; ENSG00000196262; Homo sapiens.
DR GermOnline; ENSG00000198618; Homo sapiens.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
DR GO; GO:0046790; F:virion binding; NAS:UniProtKB.
DR GO; GO:0030260; P:entry into host cell; TAS:Reactome.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR GO; GO:0034389; P:lipid particle organization; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:UniProtKB.
DR GO; GO:0006278; P:RNA-dependent DNA replication; TAS:Reactome.
DR GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
DR GO; GO:0019076; P:viral release from host cell; TAS:UniProtKB.
DR GO; GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
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; 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; Complete proteome; Cyclosporin; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Host-virus interaction;
KW Isomerase; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Rotamase; Secreted; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 165 Peptidyl-prolyl cis-trans isomerase A.
FT /FTId=PRO_0000064115.
FT DOMAIN 7 163 PPIase cyclophilin-type.
FT MOD_RES 2 2 N-acetylvaline; partial.
FT MOD_RES 21 21 Phosphoserine (By similarity).
FT MOD_RES 28 28 N6-acetyllysine; alternate.
FT MOD_RES 44 44 N6-acetyllysine.
FT MOD_RES 76 76 N6-acetyllysine.
FT MOD_RES 82 82 N6-acetyllysine.
FT MOD_RES 93 93 Phosphothreonine.
FT MOD_RES 125 125 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine.
FT CARBOHYD 108 108 N-linked (GlcNAc...) (Potential).
FT CROSSLNK 28 28 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT MUTAGEN 121 121 W->A: 200-fold decrease of sensitivity to
FT CsA.
FT MUTAGEN 121 121 W->F: 75-fold decrease of sensitivity to
FT CsA.
FT CONFLICT 89 89 I -> T (in Ref. 7; AAH05982).
FT CONFLICT 106 106 N -> I (in Ref. 7; AAH07104).
FT CONFLICT 165 165 E -> D (in Ref. 4; CAG32988).
FT STRAND 5 12
FT STRAND 15 24
FT TURN 26 28
FT HELIX 30 41
FT TURN 42 44
FT STRAND 52 57
FT TURN 58 60
FT STRAND 61 64
FT TURN 67 69
FT STRAND 70 73
FT STRAND 78 81
FT STRAND 97 100
FT STRAND 102 104
FT STRAND 108 110
FT STRAND 112 117
FT HELIX 120 122
FT TURN 123 125
FT STRAND 128 134
FT HELIX 136 143
FT HELIX 148 150
FT TURN 153 155
FT STRAND 156 164
SQ SEQUENCE 165 AA; 18012 MW; 9B2E637A555E4434 CRC64;
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE
//
