Full text data of PDIA2
PDIA2
(PDIP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Protein disulfide-isomerase A2; 5.3.4.1 (Pancreas-specific protein disulfide isomerase; PDIp; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein disulfide-isomerase A2; 5.3.4.1 (Pancreas-specific protein disulfide isomerase; PDIp; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00011571
IPI00011571 Protein disulfide-isomerase A2 precursor Protein disulfide-isomerase A2 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 2 membrane bound n/a expected molecular weight found in band > 188 kDa together with ubiquitin
IPI00011571 Protein disulfide-isomerase A2 precursor Protein disulfide-isomerase A2 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 2 membrane bound n/a expected molecular weight found in band > 188 kDa together with ubiquitin
UniProt
Q13087
ID PDIA2_HUMAN Reviewed; 525 AA.
AC Q13087; A6ZJ64; B4DI27; Q2WGM4; Q4TT67; Q6B010; Q96KJ6; Q9BW95;
read moreDT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Protein disulfide-isomerase A2;
DE EC=5.3.4.1;
DE AltName: Full=Pancreas-specific protein disulfide isomerase;
DE Short=PDIp;
DE Flags: Precursor;
GN Name=PDIA2; Synonyms=PDIP;
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), AND VARIANT SER-502.
RA Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T.,
RA Saito T.;
RT "A human polycistronic mRNA composed of ARHGDIG and PDIP.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-525 (ISOFORM 1), AND
RP VARIANT SER-502.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-525 (ISOFORM 1), TISSUE SPECIFICITY,
RP AND VARIANT SER-502.
RC TISSUE=Pancreas;
RX PubMed=8561901; DOI=10.1089/dna.1996.15.9;
RA Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L.,
RA Lan M.S.;
RT "Characterization and chromosomal localization of a new protein
RT disulfide isomerase, PDIp, highly expressed in human pancreas.";
RL DNA Cell Biol. 15:9-16(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-525 (ISOFORM 1).
RC TISSUE=Corpus callosum;
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 [8]
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=9115635;
RA Desilva M.G., Notkins A.L., Lan M.S.;
RT "Molecular characterization of a pancreas-specific protein disulfide
RT isomerase, PDIp.";
RL DNA Cell Biol. 16:269-274(1997).
RN [9]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein
RT complexes in endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [10]
RP FUNCTION, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF CYS-18 AND
RP CYS-364.
RX PubMed=19150607; DOI=10.1016/j.abb.2008.12.021;
RA Fu X., Zhu B.T.;
RT "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is
RT redox-regulated through formation of an inter-subunit disulfide
RT bond.";
RL Arch. Biochem. Biophys. 485:1-9(2009).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19429457; DOI=10.1016/j.jsbmb.2009.02.008;
RA Fu X.M., Zhu B.T.;
RT "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is
RT an intracellular estrogen-binding protein that modulates estrogen
RT levels and actions in target cells.";
RL J. Steroid Biochem. Mol. Biol. 115:20-29(2009).
RN [12]
RP GLYCOSYLATION AT ASN-127; ASN-284 AND ASN-516, AND MUTAGENESIS OF
RP ASN-284.
RX PubMed=23167757; DOI=10.1111/febs.12063;
RA Walker A.K., Soo K.Y., Levina V., Talbo G.H., Atkin J.D.;
RT "N-linked glycosylation modulates dimerization of protein disulfide
RT isomerase family A member 2 (PDIA2).";
RL FEBS J. 280:233-243(2013).
CC -!- FUNCTION: Acts as an intracellular estrogen-binding protein. May
CC be involved in modulating cellular levels and biological functions
CC of estrogens in the pancreas. May act as a chaperone that inhibits
CC aggregation of misfolded proteins.
CC -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC proteins.
CC -!- SUBUNIT: Monomer; predominantly as monomer under reducing
CC conditions. Homodimer; disulfide-linked. Part of a large chaperone
CC multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU,
CC PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts
CC of ERP29, but not, or at very low levels, CALR nor CANX.
CC -!- INTERACTION:
CC P16333:NCK1; NbExp=3; IntAct=EBI-1752525, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13087-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13087-2; Sequence=VSP_039292;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas (at protein
CC level).
CC -!- PTM: The disulfide-linked homodimer exhibits an enhanced chaperone
CC activity.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC -!- SIMILARITY: Contains 2 thioredoxin domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50401.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC Sequence=AAH75029.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC Sequence=BAG58339.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB127078; BAE48734.1; -; mRNA.
DR EMBL; AE006463; AAK61223.1; -; Genomic_DNA.
DR EMBL; Z69667; CAI95586.1; -; Genomic_DNA.
DR EMBL; Z69667; CAO78188.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85838.1; -; Genomic_DNA.
DR EMBL; BC000537; AAH00537.2; -; mRNA.
DR EMBL; BC075029; AAH75029.1; ALT_SEQ; mRNA.
DR EMBL; U19948; AAC50401.1; ALT_SEQ; mRNA.
DR EMBL; AK295383; BAG58339.1; ALT_INIT; mRNA.
DR RefSeq; NP_006840.2; NM_006849.2.
DR UniGene; Hs.66581; -.
DR ProteinModelPortal; Q13087; -.
DR SMR; Q13087; 32-495.
DR IntAct; Q13087; 10.
DR MINT; MINT-1513985; -.
DR STRING; 9606.ENSP00000219406; -.
DR PhosphoSite; Q13087; -.
DR DMDM; 21264492; -.
DR PaxDb; Q13087; -.
DR PRIDE; Q13087; -.
DR DNASU; 64714; -.
DR Ensembl; ENST00000219406; ENSP00000219406; ENSG00000185615.
DR Ensembl; ENST00000404312; ENSP00000384410; ENSG00000185615.
DR GeneID; 64714; -.
DR KEGG; hsa:64714; -.
DR UCSC; uc002cgn.1; human.
DR CTD; 64714; -.
DR GeneCards; GC16P000336; -.
DR H-InvDB; HIX0202311; -.
DR HGNC; HGNC:14180; PDIA2.
DR HPA; HPA051692; -.
DR HPA; HPA053492; -.
DR MIM; 608012; gene.
DR neXtProt; NX_Q13087; -.
DR PharmGKB; PA33153; -.
DR eggNOG; COG0526; -.
DR HOVERGEN; HBG005920; -.
DR InParanoid; Q13087; -.
DR KO; K09581; -.
DR OMA; TEFNSQT; -.
DR OrthoDB; EOG7VHSX1; -.
DR PhylomeDB; Q13087; -.
DR BRENDA; 5.3.4.1; 2681.
DR ChiTaRS; PDIA2; human.
DR GenomeRNAi; 64714; -.
DR NextBio; 66651; -.
DR PRO; PR:Q13087; -.
DR ArrayExpress; Q13087; -.
DR Bgee; Q13087; -.
DR CleanEx; HS_PDIA2; -.
DR Genevestigator; Q13087; -.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; TAS:ProtInc.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR GO; GO:0006621; P:protein retention in ER lumen; TAS:ProtInc.
DR Gene3D; 3.40.30.10; -; 4.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Complete proteome; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Isomerase; Lipid-binding;
KW Polymorphism; Redox-active center; Reference proteome; Repeat; Signal;
KW Steroid-binding.
FT SIGNAL 1 21 Potential.
FT CHAIN 22 525 Protein disulfide-isomerase A2.
FT /FTId=PRO_0000034222.
FT DOMAIN 27 152 Thioredoxin 1.
FT DOMAIN 367 496 Thioredoxin 2.
FT MOTIF 522 525 Prevents secretion from ER (Potential).
FT ACT_SITE 71 71 Nucleophile (By similarity).
FT ACT_SITE 74 74 Nucleophile (By similarity).
FT ACT_SITE 418 418 Nucleophile (By similarity).
FT ACT_SITE 421 421 Nucleophile (By similarity).
FT SITE 72 72 Contributes to redox potential value (By
FT similarity).
FT SITE 73 73 Contributes to redox potential value (By
FT similarity).
FT SITE 138 138 Lowers pKa of C-terminal Cys of first
FT active site (By similarity).
FT SITE 419 419 Contributes to redox potential value (By
FT similarity).
FT SITE 420 420 Contributes to redox potential value (By
FT similarity).
FT SITE 482 482 Lowers pKa of C-terminal Cys of second
FT active site (By similarity).
FT CARBOHYD 127 127 N-linked (GlcNAc...).
FT CARBOHYD 284 284 N-linked (GlcNAc...).
FT CARBOHYD 516 516 N-linked (GlcNAc...).
FT DISULFID 18 18 Interchain.
FT DISULFID 71 74 Redox-active (By similarity).
FT DISULFID 418 421 Redox-active (By similarity).
FT VAR_SEQ 181 183 Missing (in isoform 2).
FT /FTId=VSP_039292.
FT VARIANT 39 39 P -> S (in dbSNP:rs45455191).
FT /FTId=VAR_048087.
FT VARIANT 119 119 T -> R (in dbSNP:rs45614840).
FT /FTId=VAR_048088.
FT VARIANT 185 185 E -> K (in dbSNP:rs419949).
FT /FTId=VAR_048089.
FT VARIANT 286 286 T -> M (in dbSNP:rs2685127).
FT /FTId=VAR_048090.
FT VARIANT 382 382 P -> A (in dbSNP:rs45529833).
FT /FTId=VAR_048091.
FT VARIANT 388 388 R -> Q (in dbSNP:rs400037).
FT /FTId=VAR_048092.
FT VARIANT 502 502 P -> S (in dbSNP:rs1048786).
FT /FTId=VAR_048093.
FT MUTAGEN 18 18 C->A: Impairs interchain disulfide bridge
FT formation.
FT MUTAGEN 284 284 N->Q: Increases formation of a highly
FT stable disulfide-bonded PDIA2 dimer.
FT MUTAGEN 364 364 C->A: No effect on interchain disulfide
FT bridge formation.
FT CONFLICT 96 96 T -> M (in Ref. 7; BAG58339).
FT CONFLICT 484 484 L -> Q (in Ref. 7; BAG58339).
SQ SEQUENCE 525 AA; 58206 MW; B741851AA2C40540 CRC64;
MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP
ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV DGPAQRELAE EFGVTEYPTL
KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR VGPSAMRLED EAAAQALIGG RDLVVIGFFQ
DLQDEDVATF LALAQDALDM TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL
GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA
APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTAASI
TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH
CKEMAPAWEA LAEKYQDHED IIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS
TRDLETFSKF LDNGGVLPTE EPPEEPAAPF PEPPANSTMG SKEEL
//
ID PDIA2_HUMAN Reviewed; 525 AA.
AC Q13087; A6ZJ64; B4DI27; Q2WGM4; Q4TT67; Q6B010; Q96KJ6; Q9BW95;
read moreDT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Protein disulfide-isomerase A2;
DE EC=5.3.4.1;
DE AltName: Full=Pancreas-specific protein disulfide isomerase;
DE Short=PDIp;
DE Flags: Precursor;
GN Name=PDIA2; Synonyms=PDIP;
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), AND VARIANT SER-502.
RA Hayashi A., Tabata Y., Sato S., Mitsuyama M., Kanai S., Furuya T.,
RA Saito T.;
RT "A human polycistronic mRNA composed of ARHGDIG and PDIP.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-525 (ISOFORM 1), AND
RP VARIANT SER-502.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-525 (ISOFORM 1), TISSUE SPECIFICITY,
RP AND VARIANT SER-502.
RC TISSUE=Pancreas;
RX PubMed=8561901; DOI=10.1089/dna.1996.15.9;
RA Desilva M.G., Lu J., Donadel G., Modi W.S., Xie H., Notkins A.L.,
RA Lan M.S.;
RT "Characterization and chromosomal localization of a new protein
RT disulfide isomerase, PDIp, highly expressed in human pancreas.";
RL DNA Cell Biol. 15:9-16(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-525 (ISOFORM 1).
RC TISSUE=Corpus callosum;
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 [8]
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=9115635;
RA Desilva M.G., Notkins A.L., Lan M.S.;
RT "Molecular characterization of a pancreas-specific protein disulfide
RT isomerase, PDIp.";
RL DNA Cell Biol. 16:269-274(1997).
RN [9]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein
RT complexes in endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [10]
RP FUNCTION, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF CYS-18 AND
RP CYS-364.
RX PubMed=19150607; DOI=10.1016/j.abb.2008.12.021;
RA Fu X., Zhu B.T.;
RT "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is
RT redox-regulated through formation of an inter-subunit disulfide
RT bond.";
RL Arch. Biochem. Biophys. 485:1-9(2009).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19429457; DOI=10.1016/j.jsbmb.2009.02.008;
RA Fu X.M., Zhu B.T.;
RT "Human pancreas-specific protein disulfide isomerase homolog (PDIp) is
RT an intracellular estrogen-binding protein that modulates estrogen
RT levels and actions in target cells.";
RL J. Steroid Biochem. Mol. Biol. 115:20-29(2009).
RN [12]
RP GLYCOSYLATION AT ASN-127; ASN-284 AND ASN-516, AND MUTAGENESIS OF
RP ASN-284.
RX PubMed=23167757; DOI=10.1111/febs.12063;
RA Walker A.K., Soo K.Y., Levina V., Talbo G.H., Atkin J.D.;
RT "N-linked glycosylation modulates dimerization of protein disulfide
RT isomerase family A member 2 (PDIA2).";
RL FEBS J. 280:233-243(2013).
CC -!- FUNCTION: Acts as an intracellular estrogen-binding protein. May
CC be involved in modulating cellular levels and biological functions
CC of estrogens in the pancreas. May act as a chaperone that inhibits
CC aggregation of misfolded proteins.
CC -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC proteins.
CC -!- SUBUNIT: Monomer; predominantly as monomer under reducing
CC conditions. Homodimer; disulfide-linked. Part of a large chaperone
CC multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU,
CC PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts
CC of ERP29, but not, or at very low levels, CALR nor CANX.
CC -!- INTERACTION:
CC P16333:NCK1; NbExp=3; IntAct=EBI-1752525, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13087-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13087-2; Sequence=VSP_039292;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas (at protein
CC level).
CC -!- PTM: The disulfide-linked homodimer exhibits an enhanced chaperone
CC activity.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC -!- SIMILARITY: Contains 2 thioredoxin domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50401.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC Sequence=AAH75029.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC Sequence=BAG58339.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB127078; BAE48734.1; -; mRNA.
DR EMBL; AE006463; AAK61223.1; -; Genomic_DNA.
DR EMBL; Z69667; CAI95586.1; -; Genomic_DNA.
DR EMBL; Z69667; CAO78188.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85838.1; -; Genomic_DNA.
DR EMBL; BC000537; AAH00537.2; -; mRNA.
DR EMBL; BC075029; AAH75029.1; ALT_SEQ; mRNA.
DR EMBL; U19948; AAC50401.1; ALT_SEQ; mRNA.
DR EMBL; AK295383; BAG58339.1; ALT_INIT; mRNA.
DR RefSeq; NP_006840.2; NM_006849.2.
DR UniGene; Hs.66581; -.
DR ProteinModelPortal; Q13087; -.
DR SMR; Q13087; 32-495.
DR IntAct; Q13087; 10.
DR MINT; MINT-1513985; -.
DR STRING; 9606.ENSP00000219406; -.
DR PhosphoSite; Q13087; -.
DR DMDM; 21264492; -.
DR PaxDb; Q13087; -.
DR PRIDE; Q13087; -.
DR DNASU; 64714; -.
DR Ensembl; ENST00000219406; ENSP00000219406; ENSG00000185615.
DR Ensembl; ENST00000404312; ENSP00000384410; ENSG00000185615.
DR GeneID; 64714; -.
DR KEGG; hsa:64714; -.
DR UCSC; uc002cgn.1; human.
DR CTD; 64714; -.
DR GeneCards; GC16P000336; -.
DR H-InvDB; HIX0202311; -.
DR HGNC; HGNC:14180; PDIA2.
DR HPA; HPA051692; -.
DR HPA; HPA053492; -.
DR MIM; 608012; gene.
DR neXtProt; NX_Q13087; -.
DR PharmGKB; PA33153; -.
DR eggNOG; COG0526; -.
DR HOVERGEN; HBG005920; -.
DR InParanoid; Q13087; -.
DR KO; K09581; -.
DR OMA; TEFNSQT; -.
DR OrthoDB; EOG7VHSX1; -.
DR PhylomeDB; Q13087; -.
DR BRENDA; 5.3.4.1; 2681.
DR ChiTaRS; PDIA2; human.
DR GenomeRNAi; 64714; -.
DR NextBio; 66651; -.
DR PRO; PR:Q13087; -.
DR ArrayExpress; Q13087; -.
DR Bgee; Q13087; -.
DR CleanEx; HS_PDIA2; -.
DR Genevestigator; Q13087; -.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; TAS:ProtInc.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR GO; GO:0006621; P:protein retention in ER lumen; TAS:ProtInc.
DR Gene3D; 3.40.30.10; -; 4.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Complete proteome; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Isomerase; Lipid-binding;
KW Polymorphism; Redox-active center; Reference proteome; Repeat; Signal;
KW Steroid-binding.
FT SIGNAL 1 21 Potential.
FT CHAIN 22 525 Protein disulfide-isomerase A2.
FT /FTId=PRO_0000034222.
FT DOMAIN 27 152 Thioredoxin 1.
FT DOMAIN 367 496 Thioredoxin 2.
FT MOTIF 522 525 Prevents secretion from ER (Potential).
FT ACT_SITE 71 71 Nucleophile (By similarity).
FT ACT_SITE 74 74 Nucleophile (By similarity).
FT ACT_SITE 418 418 Nucleophile (By similarity).
FT ACT_SITE 421 421 Nucleophile (By similarity).
FT SITE 72 72 Contributes to redox potential value (By
FT similarity).
FT SITE 73 73 Contributes to redox potential value (By
FT similarity).
FT SITE 138 138 Lowers pKa of C-terminal Cys of first
FT active site (By similarity).
FT SITE 419 419 Contributes to redox potential value (By
FT similarity).
FT SITE 420 420 Contributes to redox potential value (By
FT similarity).
FT SITE 482 482 Lowers pKa of C-terminal Cys of second
FT active site (By similarity).
FT CARBOHYD 127 127 N-linked (GlcNAc...).
FT CARBOHYD 284 284 N-linked (GlcNAc...).
FT CARBOHYD 516 516 N-linked (GlcNAc...).
FT DISULFID 18 18 Interchain.
FT DISULFID 71 74 Redox-active (By similarity).
FT DISULFID 418 421 Redox-active (By similarity).
FT VAR_SEQ 181 183 Missing (in isoform 2).
FT /FTId=VSP_039292.
FT VARIANT 39 39 P -> S (in dbSNP:rs45455191).
FT /FTId=VAR_048087.
FT VARIANT 119 119 T -> R (in dbSNP:rs45614840).
FT /FTId=VAR_048088.
FT VARIANT 185 185 E -> K (in dbSNP:rs419949).
FT /FTId=VAR_048089.
FT VARIANT 286 286 T -> M (in dbSNP:rs2685127).
FT /FTId=VAR_048090.
FT VARIANT 382 382 P -> A (in dbSNP:rs45529833).
FT /FTId=VAR_048091.
FT VARIANT 388 388 R -> Q (in dbSNP:rs400037).
FT /FTId=VAR_048092.
FT VARIANT 502 502 P -> S (in dbSNP:rs1048786).
FT /FTId=VAR_048093.
FT MUTAGEN 18 18 C->A: Impairs interchain disulfide bridge
FT formation.
FT MUTAGEN 284 284 N->Q: Increases formation of a highly
FT stable disulfide-bonded PDIA2 dimer.
FT MUTAGEN 364 364 C->A: No effect on interchain disulfide
FT bridge formation.
FT CONFLICT 96 96 T -> M (in Ref. 7; BAG58339).
FT CONFLICT 484 484 L -> Q (in Ref. 7; BAG58339).
SQ SEQUENCE 525 AA; 58206 MW; B741851AA2C40540 CRC64;
MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP
ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV DGPAQRELAE EFGVTEYPTL
KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR VGPSAMRLED EAAAQALIGG RDLVVIGFFQ
DLQDEDVATF LALAQDALDM TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL
GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA
APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTAASI
TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH
CKEMAPAWEA LAEKYQDHED IIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS
TRDLETFSKF LDNGGVLPTE EPPEEPAAPF PEPPANSTMG SKEEL
//
MIM
608012
*RECORD*
*FIELD* NO
608012
*FIELD* TI
*608012 PROTEIN DISULFIDE ISOMERASE, FAMILY A, MEMBER 2; PDIA2
;;PROTEIN DISULFIDE ISOMERASE, PANCREATIC; PDIP
read more*FIELD* TX
DESCRIPTION
Protein disulfide isomerases (EC 5.3.4.1), such as PDIP, are endoplasmic
reticulum (ER) resident proteins that catalyze protein folding and
thiol-disulfide interchange reactions (Desilva et al., 1996).
CLONING
Desilva et al. (1996) cloned PDIP from an insulinoma subtraction cDNA
library. The deduced 511-amino acid protein has a calculated molecular
mass of about 56.6 kD and contains 2 thioredoxin (187700)-like catalytic
sites, a C-terminal ER retention sequence (KEEL), and 3 potential
N-glycosylation sites. PDIP shares about 46% identity with bovine,
mouse, rabbit, and human PDIs (176790). Northern blot analysis detected
a 2.0-kb transcript expressed exclusively in pancreas.
GENE FUNCTION
Desilva et al. (1996) determined that recombinant PDIP, expressed in E.
coli, catalyzed the reductive cleavage of radiolabeled insulin and
reactivated reduced RNase A.
MAPPING
By somatic cell hybrid analysis and FISH, Desilva et al. (1996) mapped
the PDIP gene to chromosome 16p13.3.
*FIELD* RF
1. Desilva, M. G.; Lu, J.; Donadel, G.; Modi, W. S.; Xie, H.; Notkins,
A. L.; Lan, M. S.: Characterization and chromosomal localization
of a new protein disulfide isomerase, PDIp, highly expressed in human
pancreas. DNA Cell Biol. 15: 9-16, 1996.
*FIELD* CD
Patricia A. Hartz: 8/6/2003
*FIELD* ED
mgross: 11/10/2009
terry: 11/3/2009
mgross: 6/7/2007
mgross: 8/6/2003
*RECORD*
*FIELD* NO
608012
*FIELD* TI
*608012 PROTEIN DISULFIDE ISOMERASE, FAMILY A, MEMBER 2; PDIA2
;;PROTEIN DISULFIDE ISOMERASE, PANCREATIC; PDIP
read more*FIELD* TX
DESCRIPTION
Protein disulfide isomerases (EC 5.3.4.1), such as PDIP, are endoplasmic
reticulum (ER) resident proteins that catalyze protein folding and
thiol-disulfide interchange reactions (Desilva et al., 1996).
CLONING
Desilva et al. (1996) cloned PDIP from an insulinoma subtraction cDNA
library. The deduced 511-amino acid protein has a calculated molecular
mass of about 56.6 kD and contains 2 thioredoxin (187700)-like catalytic
sites, a C-terminal ER retention sequence (KEEL), and 3 potential
N-glycosylation sites. PDIP shares about 46% identity with bovine,
mouse, rabbit, and human PDIs (176790). Northern blot analysis detected
a 2.0-kb transcript expressed exclusively in pancreas.
GENE FUNCTION
Desilva et al. (1996) determined that recombinant PDIP, expressed in E.
coli, catalyzed the reductive cleavage of radiolabeled insulin and
reactivated reduced RNase A.
MAPPING
By somatic cell hybrid analysis and FISH, Desilva et al. (1996) mapped
the PDIP gene to chromosome 16p13.3.
*FIELD* RF
1. Desilva, M. G.; Lu, J.; Donadel, G.; Modi, W. S.; Xie, H.; Notkins,
A. L.; Lan, M. S.: Characterization and chromosomal localization
of a new protein disulfide isomerase, PDIp, highly expressed in human
pancreas. DNA Cell Biol. 15: 9-16, 1996.
*FIELD* CD
Patricia A. Hartz: 8/6/2003
*FIELD* ED
mgross: 11/10/2009
terry: 11/3/2009
mgross: 6/7/2007
mgross: 8/6/2003