ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P62937


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PPIA_HUMAN
Primary accession number P62937
Secondary accession numbers P05092 Q3KQW3 Q6IBU5 Q96IX3 Q9BRU4 Q9BTY9 Q9UC61
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 67)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase A
Synonyms PPIase A
Rotamase A
EC 5.2.1.8
Cyclophilin A
Cyclosporin A-binding protein
Gene name
Name: PPIA
Synonyms: CYPA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leukemic T-cell;
PubMed=3297675 [NCBI, ExPASy, EBI, Israel, Japan]
Haendler B., Hofer-Warbinek R., Hofer E.;
"Complementary DNA for human T-cell cyclophilin.";
EMBO J. 6:947-950(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1111/j.1432-1033.1990.tb15598.x; PubMed=2197089 [NCBI, ExPASy, EBI, Israel, Japan]
Haendler B., Hofer E.;
"Characterization of the human cyclophilin gene and of related processed pseudogenes.";
Eur. J. Biochem. 190:477-482(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, Brain, Cervix, Colon, Lung, Skeletal muscle, Skin, and Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-30.
PubMed=7657784 [NCBI, ExPASy, EBI, Israel, Japan]
Meier U., Beier-Hellwig K., Klug J., Linder D., Beier H.M.;
"Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy.";
Hum. Reprod. 10:1305-1310(1995).
[7]
PROTEIN SEQUENCE OF 2-19.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 2-31; 56-69; 77-118; 132-144 AND 155-165, AND MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[10]
MUTAGENESIS OF TRP-121.
DOI=10.1021/bi00223a003; PubMed=2001362 [NCBI, ExPASy, EBI, Israel, Japan]
Liu J., Chen C.-M., Walsh C.T.;
"Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue.";
Biochemistry 30:2306-2310(1991).
[11]
INTERACTION WITH HIV-1 CAPSID PROTEIN.
DOI=10.1016/0092-8674(93)90637-6; PubMed=8513493 [NCBI, ExPASy, EBI, Israel, Japan]
Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.;
"Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B.";
Cell 73:1067-1078(1993).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, AND MASS SPECTROMETRY.
TISSUE=Hepatocyte;
DOI=10.1002/pmic.200401217; PubMed=16097034 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.;
"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.";
Proteomics 5:3589-3599(2005).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[14]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-28, AND MASS SPECTROMETRY.
DOI=10.1021/pr800468j; PubMed=18781797 [NCBI, ExPASy, EBI, Israel, Japan]
Meierhofer D., Wang X., Huang L., Kaiser P.;
"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.";
J. Proteome Res. 7:4566-4576(2008).
[15]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[16]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND STRUCTURE BY NMR.
DOI=10.1038/353276a0; PubMed=1896075 [NCBI, ExPASy, EBI, Israel, Japan]
Kallen J., Spitzfaden C., Zurini M.G.M., Wider G., Widmer H., Wuethrich K., Walkinshaw M.D.;
"Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy.";
Nature 353:276-279(1991).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1073/pnas.88.21.9483; PubMed=1946361 [NCBI, ExPASy, EBI, Israel, Japan]
Ke H., Zydowsky L.D., Liu J., Walsh C.T.;
"Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 88:9483-9487(1991).
[18]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CYCLOPHILIN.
DOI=10.1038/361091a0; PubMed=8421501 [NCBI, ExPASy, EBI, Israel, Japan]
Pfuegl G., Kallen J., Schirmer T., Jansonius J.N., Zurini M.G.M., Walkinshaw M.D.;
"X-ray structure of a decameric cyclophilin-cyclosporin crystal complex.";
Nature 361:91-94(1993).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1006/jmbi.1993.1664; PubMed=8263916 [NCBI, ExPASy, EBI, Israel, Japan]
Mikol V., Kallen J., Pfluegl G., Walkinshaw M.D.;
"X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1-A resolution.";
J. Mol. Biol. 234:1119-1130(1993).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1021/bi9602775; PubMed=8652511 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao Y., Ke H.;
"Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization.";
Biochemistry 35:7356-7361(1996).
[21]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
PubMed=9385632 [NCBI, ExPASy, EBI, Israel, Japan]
Vajdos F.F., Yoo S., Houseweart M., Sundquist W.I., Hill C.P.;
"Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.";
Protein Sci. 6:2297-2307(1997).
[22]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1006/jmbi.1998.2108; PubMed=9769216 [NCBI, ExPASy, EBI, Israel, Japan]
Kallen J., Mikol V., Taylor P., Walkinshaw M.D.;
"X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.";
J. Mol. Biol. 283:435-449(1998).
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
DOI=10.1073/pnas.192206699; PubMed=12218175 [NCBI, ExPASy, EBI, Israel, Japan]
Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.;
"Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.";
Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
[24]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
DOI=10.1073/pnas.212504399; PubMed=12357034 [NCBI, ExPASy, EBI, Israel, Japan]
Jin L., Harrison S.C.;
"Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin.";
Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
[25]
STRUCTURE BY NMR OF COMPLEX WITH CYCLOPHILIN.
DOI=10.1038/361088a0; PubMed=8421500 [NCBI, ExPASy, EBI, Israel, Japan]
Theriault Y., Logan T.M., Meadows R., Yu L., Olejniczak E.T., Holzman T.F., Simmer R.L., Fesik S.W.;
"Solution structure of the cyclosporin A/cyclophilin complex by NMR.";
Nature 361:88-91(1993).
[26]
STRUCTURE BY NMR.
DOI=10.1006/jmbi.1997.1220; PubMed=9299338 [NCBI, ExPASy, EBI, Israel, Japan]
Ottiger M., Zerbe O., Guentert P., Wuethrich K.;
"The NMR solution conformation of unligated human cyclophilin A.";
J. Mol. Biol. 272:64-81(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00052; CAA68264.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52851; CAA37039.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456707; CAG32988.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY739283; AAU13906.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000689; AAH00689.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003026; AAH03026.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005320; AAH05320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005982; AAH05982.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007104; AAH07104.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013915; AAH13915.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073992; AAH73992.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC106030; AAI06031.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00419585; -.
PIR A94496; CSHUA.
RefSeq NP_066953.1; -.
UniGene Hs.356331
3D structure databases
PDB
1AK4; X-ray; 2.36 A; A/B=2-164.[ExPASy / RCSB / EBI]
1AWQ; X-ray; 1.58 A; A=2-165.[ExPASy / RCSB / EBI]
1AWR; X-ray; 1.58 A; A/B/C/D/E/F=2-165.[ExPASy / RCSB / EBI]
1AWS; X-ray; 2.55 A; A=2-165.[ExPASy / RCSB / EBI]
1AWT; X-ray; 2.55 A; A/B/C/D/E/F=2-165.[ExPASy / RCSB / EBI]
1AWU; X-ray; 2.34 A; A=2-165.[ExPASy / RCSB / EBI]
1AWV; X-ray; 2.34 A; A/B/C/D/E/F=2-165.[ExPASy / RCSB / EBI]
1BCK; X-ray; 1.80 A; A=1-165.[ExPASy / RCSB / EBI]
1CWA; X-ray; 2.10 A; A=1-165.[ExPASy / RCSB / EBI]
1CWB; X-ray; 2.20 A; A=1-165.[ExPASy / RCSB / EBI]
1CWC; X-ray; 1.86 A; A=1-165.[ExPASy / RCSB / EBI]
1CWF; X-ray; 1.86 A; A=1-165.[ExPASy / RCSB / EBI]
1CWH; X-ray; 1.86 A; A=1-165.[ExPASy / RCSB / EBI]
1CWI; X-ray; 1.90 A; A=1-165.[ExPASy / RCSB / EBI]
1CWJ; X-ray; 1.80 A; A=1-165.[ExPASy / RCSB / EBI]
1CWK; X-ray; 1.80 A; A=1-165.[ExPASy / RCSB / EBI]
1CWL; X-ray; 1.80 A; A=1-165.[ExPASy / RCSB / EBI]
1CWM; X-ray; 2.00 A; A=1-165.[ExPASy / RCSB / EBI]
1CWO; X-ray; 1.86 A; A=2-164.[ExPASy / RCSB / EBI]
1FGL; X-ray; 1.80 A; A=2-164.[ExPASy / RCSB / EBI]
1M63; X-ray; 2.80 A; C/G=1-165.[ExPASy / RCSB / EBI]
1M9C; X-ray; 2.00 A; A/B=1-164.[ExPASy / RCSB / EBI]
1M9D; X-ray; 1.90 A; A/B=1-164.[ExPASy / RCSB / EBI]
1M9E; X-ray; 1.72 A; A/B=1-163.[ExPASy / RCSB / EBI]
1M9F; X-ray; 1.73 A; A/B=1-164.[ExPASy / RCSB / EBI]
1M9X; X-ray; 1.70 A; A/B/E/F=1-164.[ExPASy / RCSB / EBI]
1M9Y; X-ray; 1.90 A; A/B/E/F=1-164.[ExPASy / RCSB / EBI]
1MF8; X-ray; 3.10 A; C=1-165.[ExPASy / RCSB / EBI]
1MIK; X-ray; 1.76 A; A=1-165.[ExPASy / RCSB / EBI]
1NMK; X-ray; 2.10 A; A/B=1-165.[ExPASy / RCSB / EBI]
1OCA; NMR; -; A=1-165.[ExPASy / RCSB / EBI]
1RMH; X-ray; 2.40 A; A/B=2-165.[ExPASy / RCSB / EBI]
1VBS; X-ray; 2.00 A; A=1-165.[ExPASy / RCSB / EBI]
1VBT; X-ray; 2.30 A; A/B=1-165.[ExPASy / RCSB / EBI]
1W8L; X-ray; 1.80 A; A=2-164.[ExPASy / RCSB / EBI]
1W8M; X-ray; 1.65 A; A=2-164.[ExPASy / RCSB / EBI]
1W8V; X-ray; 1.70 A; A=2-164.[ExPASy / RCSB / EBI]
1YND; X-ray; 1.60 A; A/B=1-165.[ExPASy / RCSB / EBI]
1ZKF; X-ray; 2.55 A; A/B=1-165.[ExPASy / RCSB / EBI]
2ALF; X-ray; 1.90 A; A=2-164.[ExPASy / RCSB / EBI]
2CPL; X-ray; 1.63 A; A=2-164.[ExPASy / RCSB / EBI]
2CYH; X-ray; 1.64 A; A=2-165.[ExPASy / RCSB / EBI]
2RMA; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=2-164.[ExPASy / RCSB / EBI]
2RMB; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=2-164.[ExPASy / RCSB / EBI]
3CYH; X-ray; 1.90 A; A=2-165.[ExPASy / RCSB / EBI]
3CYS; NMR; -; A=1-165.[ExPASy / RCSB / EBI]
4CYH; X-ray; 2.10 A; A=2-165.[ExPASy / RCSB / EBI]
5CYH; X-ray; 2.10 A; A=2-165.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AK4; -.
1AWQ; -.
1AWR; -.
1AWS; -.
1AWT; -.
1AWU; -.
1AWV; -.
1BCK; -.
1CWA; -.
1CWB; -.
1CWC; -.
1CWF; -.
1CWH; -.
1CWI; -.
1CWJ; -.
1CWK; -.
1CWL; -.
1CWM; -.
1CWO; -.
1FGL; -.
1M63; -.
1M9C; -.
1M9D; -.
1M9E; -.
1M9F; -.
1M9X; -.
1M9Y; -.
1MF8; -.
1MIK; -.
1NMK; -.
1OCA; -.
1RMH; -.
1VBS; -.
1VBT; -.
1W8L; -.
1W8M; -.
1W8V; -.
1YND; -.
1ZKF; -.
2ALF; -.
2CPL; -.
2CYH; -.
2RMA; -.
2RMB; -.
3CYH; -.
3CYS; -.
4CYH; -.
5CYH; -.
ModBase P62937.
Protein-protein interaction databases
IntAct P62937; 11.
PTM databases
PhosphoSite P62937; -.
Enzyme and pathway databases
BRENDA 5.2.1.8; 247.
Reactome REACT_604; Hemostasis.
REACT_6185; HIV Infection.
REACT_6900; Signaling in Immune system.
2D gel databases
SWISS-2DPAGE P62937; -.
Aarhus/Ghent-2DPAGE 2003; NEPHGE.
DOSAC-COBS-2DPAGE P62937; -.
OGP P62937; -.
PMMA-2DPAGE P62937; -.
REPRODUCTION-2DPAGE IPI00419585; -.
P62937; -.
Siena-2DPAGE P62937; -.
Organism-specific databases
GeneCards GC07P044802; -.
GC07P044803; -.
H-InvDB HIX0041072; -.
HGNC HGNC:9253; PPIA.
GenAtlas PPIA.
HPA CAB004655; -.
MIM 123840; gene. [NCBI / EBI]
PharmGKB PA33574; -.
Gene expression databases
ArrayExpress P62937; -.
Bgee P62937; -.
CleanEx HS_PPIA; -.
GermOnline ENSG00000196262; Homo sapiens.
ENSG00000198618; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005576; Cellular component: extracellular region (inferred from experiment from Reactome).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0042277; Molecular function: peptide binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0051082; Molecular function: unfolded protein binding (traceable author statement from UniProtKB).
GO:0046790; Molecular function: virion binding (non-traceable author statement from UniProtKB).
GO:0019059; Biological process: initiation of viral infection (inferred from experiment from Reactome).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006457; Biological process: protein folding (traceable author statement from UniProtKB).
GO:0019047; Biological process: provirus integration (inferred from experiment from Reactome).
GO:0045069; Biological process: regulation of viral genome replication (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002130; PPIase_cyclophilin.
Graphical view of domain structure.
Gene3D G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
Pfam PF00160; Pro_isomerase; 1.
Pfam graphical view of domain structure.
PRINTS PR00153; CSAPPISMRASE.
PROSITE PS00170; CSA_PPIASE_1; 1.
PS50072; CSA_PPIASE_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P62937; -.
PRIDE P62937; -.
Genome annotation databases
Ensembl ENSG00000196262; Homo sapiens. [Contig view]
GeneID 5478; -.
KEGG hsa:5478; -.
Phylogenomic databases
HOVERGEN P62937; -.
OMA P62937; TMELFND.
Other
DrugBank DB00091; Cyclosporine.
DB00172; L-Proline.
NextBio 21206; -.
SOURCE PPIA; Homo sapiens.
ProtoNet P62937.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cyclosporin; Cytoplasm; Direct protein sequencing; Host-virus interaction; Isomerase; Isopeptide bond; Phosphoprotein; Rotamase; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   165  164     Peptidyl-prolyl cis-trans isomerase A. PRO_0000064115
DOMAIN   7   163  157     PPIase cyclophilin-type. 
MOD_RES   2     2        N-acetylvaline; partial. 
MOD_RES   21    21        Phosphoserine (By similarity). 
MOD_RES   125   125        N6-acetyllysine. 
MOD_RES   157   157        Phosphothreonine. 
CROSSLNK   28    28        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
MUTAGEN   121   121        W->A: 200-fold decrease of sensitivity to CsA. 
MUTAGEN   121   121        W->F: 75-fold decrease of sensitivity to CsA. 
CONFLICT   89    89        I -> T (in Ref. 5; AAH05982). 
CONFLICT   106   106        N -> I (in Ref. 5; AAH07104). 
CONFLICT   165   165        E -> D (in Ref. 3; CAG32988). 
STRAND   5    12  8      
STRAND   15    24  10      
TURN   26    28  3      
HELIX   30    41  12      
TURN   42    44  3      
STRAND   55    57  3      
TURN   58    60  3      
STRAND   61    64  4      
TURN   67    69  3      
STRAND   70    73  4      
STRAND   97   100  4      
STRAND   108   110  3      
STRAND   112   117  6      
HELIX   120   122  3      
TURN   123   125  3      
STRAND   128   134  7      
HELIX   136   143  8      
STRAND   156   163  8      
Sequence information
Length: 165 AA [This is the length of the unprocessed precursor] Molecular weight: 18012 Da [This is the MW of the unprocessed precursor] CRC64: 9B2E637A555E4434 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF 

        70         80         90        100        110        120 
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE 

       130        140        150        160 
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE 

P62937 in FASTA format

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

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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!