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2024-04-19 21:23:05, GGRNA : RefSeq release 60 (20130726)
LOCUS NM_005038 1851 bp mRNA linear PRI 29-APR-2013
DEFINITION Homo sapiens peptidylprolyl isomerase D (PPID), mRNA.
ACCESSION NM_005038
VERSION NM_005038.2 GI:45439320
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (bases 1 to 1851)
AUTHORS Tavecchio,M., Lisanti,S., Lam,A., Ghosh,J.C., Martin,N.M.,
O'Connell,M., Weeraratna,A.T., Kossenkov,A.V., Showe,L.C. and
Altieri,D.C.
TITLE Cyclophilin D extramitochondrial signaling controls cell cycle
progression and chemokine-directed cell motility
JOURNAL J. Biol. Chem. 288 (8), 5553-5561 (2013)
PUBMED 23303179
REMARK GeneRIF: CypD directs mitochondria-to-nuclei inflammatory gene
expression in normal and tumor cells
REFERENCE 2 (bases 1 to 1851)
AUTHORS Linard,D., Kandlbinder,A., Degand,H., Morsomme,P., Dietz,K.J. and
Knoops,B.
TITLE Redox characterization of human cyclophilin D: identification of a
new mammalian mitochondrial redox sensor?
JOURNAL Arch. Biochem. Biophys. 491 (1-2), 39-45 (2009)
PUBMED 19735641
REMARK GeneRIF: Cyclophilin D may play a role as a redox sensor in
mitochondria of mammalian cells transmitting information on the
redox environment to target proteins.
REFERENCE 3 (bases 1 to 1851)
AUTHORS Kajitani,K., Fujihashi,M., Kobayashi,Y., Shimizu,S., Tsujimoto,Y.
and Miki,K.
TITLE Crystal structure of human cyclophilin D in complex with its
inhibitor, cyclosporin A at 0.96-A resolution
JOURNAL Proteins 70 (4), 1635-1639 (2008)
PUBMED 18076075
REMARK GeneRIF: Crystal structure of human cyclophilin D in complex with
its inhibitor, cyclosporin A at 0.96-A resolution, using a K133I
mutant of human CypD
REFERENCE 4 (bases 1 to 1851)
AUTHORS Mok,D., Allan,R.K., Carrello,A., Wangoo,K., Walkinshaw,M.D. and
Ratajczak,T.
TITLE The chaperone function of cyclophilin 40 maps to a cleft between
the prolyl isomerase and tetratricopeptide repeat domains
JOURNAL FEBS Lett. 580 (11), 2761-2768 (2006)
PUBMED 16650407
REMARK GeneRIF: CyP40 chaperone function then, is localized within the
linker that forms a binding cleft with potential to accommodate
non-native substrates
REFERENCE 5 (bases 1 to 1851)
AUTHORS Ward,B.K., Allan,R.K., Mok,D., Temple,S.E., Taylor,P., Dornan,J.,
Mark,P.J., Shaw,D.J., Kumar,P., Walkinshaw,M.D. and Ratajczak,T.
TITLE A structure-based mutational analysis of cyclophilin 40 identifies
key residues in the core tetratricopeptide repeat domain that
mediate binding to Hsp90
JOURNAL J. Biol. Chem. 277 (43), 40799-40809 (2002)
PUBMED 12145316
REFERENCE 6 (bases 1 to 1851)
AUTHORS Mark,P.J., Ward,B.K., Kumar,P., Lahooti,H., Minchin,R.F. and
Ratajczak,T.
TITLE Human cyclophilin 40 is a heat shock protein that exhibits altered
intracellular localization following heat shock
JOURNAL Cell Stress Chaperones 6 (1), 59-70 (2001)
PUBMED 11525244
REFERENCE 7 (bases 1 to 1851)
AUTHORS Silverstein,A.M., Galigniana,M.D., Chen,M.S., Owens-Grillo,J.K.,
Chinkers,M. and Pratt,W.B.
TITLE Protein phosphatase 5 is a major component of glucocorticoid
receptor.hsp90 complexes with properties of an FK506-binding
immunophilin
JOURNAL J. Biol. Chem. 272 (26), 16224-16230 (1997)
PUBMED 9195923
REFERENCE 8 (bases 1 to 1851)
AUTHORS Yokoi,H., Shimizu,Y., Anazawa,H., Lefebvre,C.A., Korneluk,R.G. and
Ikeda,J.E.
TITLE The structure and complete nucleotide sequence of the human
cyclophilin 40 (PPID) gene
JOURNAL Genomics 35 (3), 448-455 (1996)
PUBMED 8812478
REFERENCE 9 (bases 1 to 1851)
AUTHORS Kieffer,L.J., Seng,T.W., Li,W., Osterman,D.G., Handschumacher,R.E.
and Bayney,R.M.
TITLE Cyclophilin-40, a protein with homology to the P59 component of the
steroid receptor complex. Cloning of the cDNA and further
characterization
JOURNAL J. Biol. Chem. 268 (17), 12303-12310 (1993)
PUBMED 8509368
REFERENCE 10 (bases 1 to 1851)
AUTHORS Kieffer,L.J., Thalhammer,T. and Handschumacher,R.E.
TITLE Isolation and characterization of a 40-kDa cyclophilin-related
protein
JOURNAL J. Biol. Chem. 267 (8), 5503-5507 (1992)
PUBMED 1544925
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from BG699755.1, L11667.1,
BC030707.2 and BU726810.1.
On Mar 15, 2004 this sequence version replaced gi:4826931.
Summary: The protein encoded by this gene is a member of the
peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases
catalyze the cis-trans isomerization of proline imidic peptide
bonds in oligopeptides and accelerate the folding of proteins. This
protein has been shown to possess PPIase activity and, similar to
other family members, can bind to the immunosuppressant cyclosporin
A. [provided by RefSeq, Jul 2008].
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: BC030707.2, L11667.1 [ECO:0000332]
RNAseq introns :: mixed/partial sample support
ERS025081, ERS025082 [ECO:0000350]
##Evidence-Data-END##
COMPLETENESS: complete on the 3' end.
PRIMARY REFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP
1-51 BG699755.1 6-56
52-1574 L11667.1 39-1561
1575-1827 BC030707.2 1571-1823
1828-1851 BU726810.1 1-24 c
FEATURES Location/Qualifiers
source 1..1851
/organism="Homo sapiens"
/mol_type="mRNA"
/db_xref="taxon:9606"
/chromosome="4"
/map="4q31.3"
gene 1..1851
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="peptidylprolyl isomerase D"
/db_xref="GeneID:5481"
/db_xref="HGNC:9257"
/db_xref="HPRD:11875"
/db_xref="MIM:601753"
exon 1..197
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
variation 41
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="g"
/replace="t"
/db_xref="dbSNP:17843880"
variation 52
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="a"
/replace="g"
/db_xref="dbSNP:2070629"
variation 59
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="c"
/replace="g"
/db_xref="dbSNP:2070630"
misc_feature 92..94
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="upstream in-frame stop codon"
CDS 113..1225
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/EC_number="5.2.1.8"
/note="cyclophilin D; 40 kDa peptidyl-prolyl cis-trans
isomerase D; cyclophilin-related protein; cyclophilin 40;
cyclophilin-40; PPIase D; rotamase D"
/codon_start=1
/product="peptidyl-prolyl cis-trans isomerase D"
/protein_id="NP_005029.1"
/db_xref="GI:4826932"
/db_xref="CCDS:CCDS3801.1"
/db_xref="GeneID:5481"
/db_xref="HGNC:9257"
/db_xref="HPRD:11875"
/db_xref="MIM:601753"
/translation="
MSHPSPQAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGHTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGELKEGDDGGIFPKDGSGDSHPDFPEDADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIETADRAKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDKEKAVYAKMFA
"
misc_feature 158..658
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="cyclophilin_ABH_like: Cyclophilin A, B and H-like
cyclophilin-type peptidylprolyl cis- trans isomerase
(PPIase) domain. This family represents the archetypal
cystolic cyclophilin similar to human cyclophilins A, B
and H. PPIase is an enzyme which...; Region:
cyclophilin_ABH_like; cd01926"
/db_xref="CDD:29397"
misc_feature order(332..337,350..352,503..505,509..511,533..535)
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="active site"
/db_xref="CDD:29397"
misc_feature 665..757
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="non-experimental evidence, no additional
details recorded"
/note="propagated from UniProtKB/Swiss-Prot (Q08752.3);
Region: Chaperone activity (By similarity)"
misc_feature 704..706
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphoserine; propagated from UniProtKB/Swiss-Prot
(Q08752.3); phosphorylation site"
misc_feature 752..1222
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="non-experimental evidence, no additional
details recorded"
/note="propagated from UniProtKB/Swiss-Prot (Q08752.3);
Region: Interaction with HSP90AB1 (By similarity)"
misc_feature 782..1129
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="Tetratricopeptide repeat domain; typically contains
34 amino acids
[WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-
X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in
a variety of organisms including bacteria, cyanobacteria,
yeast, fungi; Region: TPR; cd00189"
/db_xref="CDD:29151"
misc_feature order(782..787,791..796,803..808,941..946,950..955,
962..967,1043..1048,1055..1060,1067..1072)
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="binding surface"
/db_xref="CDD:29151"
misc_feature 788..1024
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="TPR repeat; Region: TPR_11; pfam13414"
/db_xref="CDD:205592"
misc_feature order(800..802,836..838,848..850,857..859,950..952,
986..988,998..1000,1007..1009,1052..1054,1088..1090,
1100..1102,1109..1111)
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="TPR motif; other site"
/db_xref="CDD:29151"
misc_feature 944..1126
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/note="TPR repeat; Region: TPR_11; pfam13414"
/db_xref="CDD:205592"
exon 198..338
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
variation 257
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="c"
/replace="t"
/db_xref="dbSNP:2070631"
exon 339..445
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
variation 349
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="a"
/replace="g"
/db_xref="dbSNP:2230221"
exon 446..634
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
exon 635..757
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
STS 638..842
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/standard_name="BARC0073"
/db_xref="UniSTS:260479"
variation 699
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="a"
/replace="t"
/db_xref="dbSNP:2230222"
exon 758..864
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
variation 826
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="c"
/replace="t"
/db_xref="dbSNP:17843932"
exon 865..1006
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
exon 1007..1093
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
variation 1016
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="a"
/replace="c"
/db_xref="dbSNP:9410"
exon 1094..1136
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
variation 1116
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="a"
/replace="g"
/db_xref="dbSNP:17843956"
exon 1137..1834
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/inference="alignment:Splign:1.39.8"
STS 1145..1309
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/standard_name="STS-L11667"
/db_xref="UniSTS:47360"
variation 1296
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="a"
/replace="g"
/db_xref="dbSNP:8396"
STS 1425..1705
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/standard_name="D11S3316"
/db_xref="UniSTS:152558"
STS 1441..1565
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/standard_name="G44334"
/db_xref="UniSTS:95121"
variation 1472
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="c"
/replace="t"
/db_xref="dbSNP:17843962"
STS 1515..1603
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/standard_name="D8S2279"
/db_xref="UniSTS:473907"
variation 1578
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/replace="a"
/replace="c"
/db_xref="dbSNP:17843963"
STS 1645..1727
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/standard_name="SHGC-67406"
/db_xref="UniSTS:43466"
polyA_signal 1807..1812
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
polyA_site 1827
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
/experiment="experimental evidence, no additional details
recorded"
polyA_site 1834
/gene="PPID"
/gene_synonym="CYP-40; CYPD"
ORIGIN
ggccggtcagcgtcgctgccggtctccggcggagacggactctggagtttgggcggcccgggcggccactaggtactctgatattccgtactaaacacgtctgcaagtcaagatgtcgcacccgtccccccaagccaagccctccaaccccagtaaccctcgagtcttctttgacgtggacatcggaggggagcgagttggtcgaattgtcttagaattgtttgcagatatcgtacccaaaactgcggaaaattttcgtgcactgtgtacaggagaaaaaggcattggacacacgactgggaaacctctccatttcaaaggatgcccttttcatcgaattattaagaaatttatgattcagggtggagacttctcaaatcagaatgggacaggtggagaaagtatttatggtgaaaaatttgaagatgaaaatttccattacaagcatgatcgggagggtttactgagcatggcaaatgcaggccgcaacacaaacggttctcagttttttatcacaacagttccaactcctcatttggatgggaaacatgtggtgtttggccaagtaattaaaggaataggagtggcaaggatattggaaaatgtggaagtgaaaggtgaaaaacctgctaaattgtgcgttattgcagaatgtggagaattgaaggaaggagatgacgggggaatattcccaaaagatggctctggcgacagtcatccagatttccctgaggatgcggatatagatttaaaagatgtagataaaattttattaataacagaagacttaaaaaacattggaaatacttttttcaaatcccagaactgggagatggctattaaaaaatatgcagaagttttaagatacgtggacagttcaaaggctgttattgagacagcagatagagccaagctgcaacctatagctttaagctgtgtactgaatattggtgcttgtaaactgaagatgtcaaattggcagggagcaattgacagttgtttagaggctcttgaactagacccatcaaataccaaagcattgtaccgcagagctcaaggatggcaaggattaaaagaatatgatcaagcattggctgatcttaagaaagctcaggggatagcaccagaagataaagctatccaggcagaattgctgaaagtcaaacaaaagataaaggcacagaaagataaagagaaggcagtatatgcaaaaatgtttgcttagaaaggattcagttttgcttattgtgtgttgattgtataaatgcaataagaaaatgtaaaggtttttgtctatgaatatgatccctaatgtgtttcttttgacaccttagttccttactgtttacagtttaggagtactgataggggttcatgcttaataaacatgtcacaatacagtaagtaaagtggttttgtttgtttctttgagatggagtcttgctctgtcacccaggctggagtgcggtggcgcaatctcggctcactgcatcctctgcctcccgggttcaagcaattctcctgcctcagcttcccaagtagctgggattacaggcacgtgccaccacgcccagctaatttttgtatttttagtagagatggggtttcaccatattggtcacgtcacgttggtcttgaactcctgaccttgtgatccaccccgccttggcctcccaaagtgctgggattacaggtgtgagccaccgtgcccggccaagtaaaatgttttttaaaatggttatgtgcattattcataaaaaataatggtgtccagtctttttaaacttgtaaagacacatcttattgaataaagagatgagagcttaagtttgtaaaaaaaaaaaaaaaaaa
//
ANNOTATIONS from NCBI Entrez Gene (20130726):
GeneID:5481 -> Molecular function: GO:0003755 [peptidyl-prolyl cis-trans isomerase activity] evidence: IDA
GeneID:5481 -> Molecular function: GO:0005515 [protein binding] evidence: IPI
GeneID:5481 -> Molecular function: GO:0008134 [transcription factor binding] evidence: IDA
GeneID:5481 -> Molecular function: GO:0016018 [cyclosporin A binding] evidence: TAS
GeneID:5481 -> Molecular function: GO:0030331 [estrogen receptor binding] evidence: ISS
GeneID:5481 -> Molecular function: GO:0030544 [Hsp70 protein binding] evidence: ISS
GeneID:5481 -> Molecular function: GO:0031072 [heat shock protein binding] evidence: IPI
GeneID:5481 -> Molecular function: GO:0051879 [Hsp90 protein binding] evidence: IDA
GeneID:5481 -> Biological process: GO:0000122 [negative regulation of transcription from RNA polymerase II promoter] evidence: IMP
GeneID:5481 -> Biological process: GO:0000413 [protein peptidyl-prolyl isomerization] evidence: IDA
GeneID:5481 -> Biological process: GO:0006457 [protein folding] evidence: ISS
GeneID:5481 -> Biological process: GO:0006461 [protein complex assembly] evidence: IDA
GeneID:5481 -> Biological process: GO:0006915 [apoptotic process] evidence: IEA
GeneID:5481 -> Biological process: GO:0015031 [protein transport] evidence: IEA
GeneID:5481 -> Biological process: GO:0019076 [viral release from host cell] evidence: TAS
GeneID:5481 -> Biological process: GO:0034389 [lipid particle organization] evidence: IMP
GeneID:5481 -> Biological process: GO:0043065 [positive regulation of apoptotic process] evidence: IMP
GeneID:5481 -> Biological process: GO:0045070 [positive regulation of viral genome replication] evidence: IMP
GeneID:5481 -> Biological process: GO:0050714 [positive regulation of protein secretion] evidence: IMP
GeneID:5481 -> Biological process: GO:0061077 [chaperone-mediated protein folding] evidence: IDA
GeneID:5481 -> Biological process: GO:0071492 [cellular response to UV-A] evidence: IMP
GeneID:5481 -> Cellular component: GO:0005634 [nucleus] evidence: IDA
GeneID:5481 -> Cellular component: GO:0005654 [nucleoplasm] evidence: IEA
GeneID:5481 -> Cellular component: GO:0005730 [nucleolus] evidence: IDA
GeneID:5481 -> Cellular component: GO:0005737 [cytoplasm] evidence: IDA
GeneID:5481 -> Cellular component: GO:0045111 [intermediate filament cytoskeleton] evidence: IDA
ANNOTATIONS from NCBI Entrez Gene (20130726):
NP_005029 -> EC 5.2.1.8
by
@meso_cacase at
DBCLS
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