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Database: UniProt
Entry: P62937
LinkDB: P62937
Original site: P62937 
ID   PPIA_HUMAN              Reviewed;         165 AA.
AC   P62937; A8K220; P05092; Q3KQW3; Q567Q0; Q6IBU5; Q96IX3; Q9BRU4;
AC   Q9BTY9; Q9UC61;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   26-NOV-2014, entry version 128.
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;
DE   Contains:
DE     RecName: Full=Peptidyl-prolyl cis-trans isomerase A, N-terminally processed;
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] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Subthalamic nucleus, and Trachea;
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] (ISOFORM 1).
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] (ISOFORM 1).
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 GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Blood, Bone marrow, Brain, Cervix, Colon, Lung,
RC   Skeletal muscle, Skin, 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   [9]
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   [10]
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   [11]
RP   PROTEIN SEQUENCE OF 2-31; 56-69; 77-118; 132-144 AND 155-165, AND
RP   IDENTIFICATION BY MASS 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   [12]
RP   PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE,
RP   ACETYLATION AT VAL-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Platelet;
RA   Bienvenut W.V., Claeys D.;
RL   Submitted (NOV-2005) to UniProtKB.
RN   [13]
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   [14]
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   [15]
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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-44; LYS-76; LYS-82;
RP   LYS-125 AND LYS-131, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [19]
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   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [21]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [22]
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   [23]
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   [24]
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   [25]
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   [26]
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   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
RX   PubMed=9385632; DOI=10.1002/pro.5560061103;
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   [28]
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   [29]
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   [30]
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   [31]
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   [32]
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   [33]
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       {ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
CC       ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:8513493}.
CC   -!- INTERACTION:
CC       Q99IB8:- (xeno); NbExp=2; IntAct=EBI-437708, EBI-6927873;
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 {ECO:0000269|PubMed:16527992}.
CC       Secreted {ECO:0000269|PubMed:16527992}. Note=Secretion occurs in
CC       response to oxidative stress in vascular smooth muscle through a
CC       vesicular secretory pathway that involves actin remodeling and
CC       myosin II activation, and mediates ERK1/2 activation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P62937-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P62937-2; Sequence=VSP_056050;
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. {ECO:0000269|PubMed:19413330,
CC       ECO:0000269|PubMed:19608861, ECO:0000269|PubMed:20364129,
CC       ECO:0000269|PubMed:22223895, ECO:0000269|PubMed:22814378,
CC       ECO:0000269|Ref.12}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       A subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00156}.
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; AK293003; BAF85692.1; -; 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; AC004854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC013436; -; NOT_ANNOTATED_CDS; 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; BC093076; AAH93076.1; -; mRNA.
DR   EMBL; BC106030; AAI06031.1; -; mRNA.
DR   EMBL; BC137057; AAI37058.1; -; mRNA.
DR   EMBL; BC137058; AAI37059.1; -; mRNA.
DR   CCDS; CCDS5494.1; -. [P62937-1]
DR   PIR; A94496; CSHUA.
DR   RefSeq; NP_001287910.1; NM_001300981.1. [P62937-2]
DR   RefSeq; NP_066953.1; NM_021130.4. [P62937-1]
DR   UniGene; Hs.356331; -.
DR   PDB; 1AK4; X-ray; 2.36 A; A/B=1-165.
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=1-165.
DR   PDB; 1FGL; X-ray; 1.80 A; A=1-165.
DR   PDB; 1M63; X-ray; 2.80 A; C/G=1-165.
DR   PDB; 1M9C; X-ray; 2.00 A; A/B=1-165.
DR   PDB; 1M9D; X-ray; 1.90 A; A/B=1-165.
DR   PDB; 1M9E; X-ray; 1.72 A; A/B=1-164.
DR   PDB; 1M9F; X-ray; 1.73 A; A/B=1-165.
DR   PDB; 1M9X; X-ray; 1.70 A; A/B/E/F=1-165.
DR   PDB; 1M9Y; X-ray; 1.90 A; A/B/E/F=1-165.
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=2-165.
DR   PDB; 1W8M; X-ray; 1.65 A; A=2-165.
DR   PDB; 1W8V; X-ray; 1.70 A; A=2-165.
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=2-165.
DR   PDB; 2CPL; X-ray; 1.63 A; A=1-165.
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=1-165.
DR   PDB; 2RMB; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165.
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; 4IPZ; X-ray; 1.67 A; A=1-165.
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; 4IPZ; -.
DR   PDBsum; 5CYH; -.
DR   ProteinModelPortal; P62937; -.
DR   SMR; P62937; 2-165.
DR   BioGrid; 111474; 62.
DR   DIP; DIP-6080N; -.
DR   IntAct; P62937; 38.
DR   MINT; MINT-4999116; -.
DR   STRING; 9606.ENSP00000419425; -.
DR   BindingDB; P62937; -.
DR   ChEMBL; CHEMBL1949; -.
DR   DrugBank; DB00091; Cyclosporine.
DR   DrugBank; DB00172; L-Proline.
DR   GuidetoPHARMACOLOGY; 2751; -.
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   MaxQB; P62937; -.
DR   PaxDb; P62937; -.
DR   PeptideAtlas; P62937; -.
DR   PRIDE; P62937; -.
DR   DNASU; 5478; -.
DR   Ensembl; ENST00000355968; ENSP00000430817; ENSG00000196262. [P62937-2]
DR   Ensembl; ENST00000468812; ENSP00000419425; ENSG00000196262. [P62937-1]
DR   Ensembl; ENST00000489459; ENSP00000427976; ENSG00000196262. [P62937-2]
DR   Ensembl; ENST00000620047; ENSP00000479961; ENSG00000196262. [P62937-2]
DR   GeneID; 5478; -.
DR   KEGG; hsa:5478; -.
DR   UCSC; uc003tlw.3; human. [P62937-1]
DR   CTD; 5478; -.
DR   GeneCards; GC07P044841; -.
DR   HGNC; HGNC:9253; PPIA.
DR   HPA; CAB004655; -.
DR   MIM; 123840; gene.
DR   neXtProt; NX_P62937; -.
DR   PharmGKB; PA33574; -.
DR   eggNOG; COG0652; -.
DR   GeneTree; ENSGT00760000119119; -.
DR   HOVERGEN; HBG001065; -.
DR   InParanoid; P62937; -.
DR   KO; K03767; -.
DR   OMA; HVERMVT; -.
DR   PhylomeDB; P62937; -.
DR   TreeFam; TF316719; -.
DR   Reactome; REACT_12560; Basigin interactions.
DR   Reactome; REACT_6266; Early Phase of HIV Life Cycle.
DR   Reactome; REACT_6359; Budding and maturation of HIV virion.
DR   Reactome; REACT_6818; Assembly Of The HIV Virion.
DR   Reactome; REACT_6903; Binding and entry of HIV virion.
DR   Reactome; REACT_6918; Integration of provirus.
DR   Reactome; REACT_6965; Uncoating of the HIV Virion.
DR   Reactome; REACT_9037; Plus-strand DNA synthesis.
DR   Reactome; REACT_9055; Minus-strand DNA synthesis.
DR   Reactome; REACT_9406; APOBEC3G mediated resistance to HIV-1 infection.
DR   ChiTaRS; PPIA; human.
DR   EvolutionaryTrace; P62937; -.
DR   GeneWiki; Peptidylprolyl_isomerase_A; -.
DR   GenomeRNAi; 5478; -.
DR   NextBio; 21206; -.
DR   PRO; PR:P62937; -.
DR   Bgee; P62937; -.
DR   CleanEx; HS_PPIA; -.
DR   ExpressionAtlas; P62937; baseline and differential.
DR   Genevestigator; P62937; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProt.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
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:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
DR   GO; GO:0046790; F:virion binding; NAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0030260; P:entry into host cell; TAS:Reactome.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; 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:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR   GO; GO:0045069; P:regulation of viral genome replication; IMP: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:0019058; P:viral life cycle; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; TAS:Reactome.
DR   GO; GO:0019076; P:viral release from host cell; TAS:UniProtKB.
DR   GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom.
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; Complete proteome;
KW   Cyclosporin; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW   Host-virus interaction; Isomerase; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Rotamase; Secreted; Ubl conjugation.
FT   CHAIN         1    165       Peptidyl-prolyl cis-trans isomerase A.
FT                                /FTId=PRO_0000423240.
FT   INIT_MET      1      1       Removed; alternate.
FT                                {ECO:0000269|PubMed:12665801,
FT                                ECO:0000269|PubMed:7657784,
FT                                ECO:0000269|Ref.11, ECO:0000269|Ref.12}.
FT   CHAIN         2    165       Peptidyl-prolyl cis-trans isomerase A, N-
FT                                terminally processed.
FT                                /FTId=PRO_0000064115.
FT   DOMAIN        7    163       PPIase cyclophilin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00156}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:22223895,
FT                                ECO:0000269|PubMed:22814378}.
FT   MOD_RES       2      2       N-acetylvaline; partial; in Peptidyl-
FT                                prolyl cis-trans isomerase A, N-
FT                                terminally processed.
FT                                {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|Ref.12}.
FT   MOD_RES      28     28       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      44     44       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      76     76       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      82     82       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      93     93       Phosphothreonine.
FT                                {ECO:0000269|PubMed:20068231}.
FT   MOD_RES     125    125       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861,
FT                                ECO:0000269|PubMed:20364129}.
FT   MOD_RES     131    131       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES     133    133       N6-acetyllysine. {ECO:0000250}.
FT   CARBOHYD    108    108       N-linked (GlcNAc...). {ECO:0000255}.
FT   CROSSLNK     28     28       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate.
FT   VAR_SEQ       1     60       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056050.
FT   MUTAGEN     121    121       W->A: 200-fold decrease of sensitivity to
FT                                CsA. {ECO:0000269|PubMed:2001362}.
FT   MUTAGEN     121    121       W->F: 75-fold decrease of sensitivity to
FT                                CsA. {ECO:0000269|PubMed:2001362}.
FT   CONFLICT     89     89       I -> T (in Ref. 8; AAH05982).
FT                                {ECO:0000305}.
FT   CONFLICT    106    106       N -> I (in Ref. 8; AAH07104).
FT                                {ECO:0000305}.
FT   CONFLICT    165    165       E -> D (in Ref. 4; CAG32988).
FT                                {ECO:0000305}.
FT   STRAND        5     12       {ECO:0000244|PDB:2X25}.
FT   STRAND       15     24       {ECO:0000244|PDB:2X25}.
FT   TURN         26     28       {ECO:0000244|PDB:2X25}.
FT   HELIX        30     41       {ECO:0000244|PDB:2X25}.
FT   TURN         42     44       {ECO:0000244|PDB:2X25}.
FT   STRAND       52     57       {ECO:0000244|PDB:2X25}.
FT   TURN         58     60       {ECO:0000244|PDB:2X25}.
FT   STRAND       61     64       {ECO:0000244|PDB:2X25}.
FT   TURN         67     69       {ECO:0000244|PDB:2X25}.
FT   STRAND       70     73       {ECO:0000244|PDB:2X25}.
FT   STRAND       78     81       {ECO:0000244|PDB:1AWQ}.
FT   STRAND       97    100       {ECO:0000244|PDB:2X25}.
FT   STRAND      102    104       {ECO:0000244|PDB:4IPZ}.
FT   STRAND      108    110       {ECO:0000244|PDB:1FGL}.
FT   STRAND      112    117       {ECO:0000244|PDB:2X25}.
FT   HELIX       120    122       {ECO:0000244|PDB:2X25}.
FT   TURN        123    125       {ECO:0000244|PDB:2X25}.
FT   STRAND      128    134       {ECO:0000244|PDB:2X25}.
FT   HELIX       136    143       {ECO:0000244|PDB:2X25}.
FT   HELIX       148    150       {ECO:0000244|PDB:3K0O}.
FT   TURN        153    155       {ECO:0000244|PDB:3CYS}.
FT   STRAND      156    164       {ECO:0000244|PDB:2X25}.
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
//
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