Full text data of PDIA4
PDIA4
(ERP70, ERP72)
[Confidence: high (present in two of the MS resources)]
Protein disulfide-isomerase A4; 5.3.4.1 (Endoplasmic reticulum resident protein 70; ER protein 70; ERp70; Endoplasmic reticulum resident protein 72; ER protein 72; ERp-72; ERp72; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein disulfide-isomerase A4; 5.3.4.1 (Endoplasmic reticulum resident protein 70; ER protein 70; ERp70; Endoplasmic reticulum resident protein 72; ER protein 72; ERp-72; ERp72; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P13667
ID PDIA4_HUMAN Reviewed; 645 AA.
AC P13667; A8K4K6; Q549T6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1991, sequence version 2.
DT 22-JAN-2014, entry version 158.
DE RecName: Full=Protein disulfide-isomerase A4;
DE EC=5.3.4.1;
DE AltName: Full=Endoplasmic reticulum resident protein 70;
DE Short=ER protein 70;
DE Short=ERp70;
DE AltName: Full=Endoplasmic reticulum resident protein 72;
DE Short=ER protein 72;
DE Short=ERp-72;
DE Short=ERp72;
DE Flags: Precursor;
GN Name=PDIA4; Synonyms=ERP70, ERP72;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2549034;
RA Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RT "Human deoxycytidine kinase. Sequence of cDNA clones and analysis of
RT expression in cell lines with and without enzyme activity.";
RL J. Biol. Chem. 264:14762-14768(1989).
RN [2]
RP ERRATUM, AND SEQUENCE REVISION.
RX PubMed=2002068;
RA Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RL J. Biol. Chem. 266:5353-5353(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Muscle;
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 [7]
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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).
CC -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC proteins.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
CC UGT1A1 and very small amounts of ERP29, but not, or at very low
CC levels, CALR nor CANX.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=3; IntAct=EBI-1054653, EBI-6248077;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome.
CC Note=Identified by mass spectrometry in melanosome fractions from
CC stage I to stage IV.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC -!- SIMILARITY: Contains 3 thioredoxin domains.
CC -!- CAUTION: Was originally (PubMed:2549034) thought to be a
CC deoxycytidine kinase.
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DR EMBL; J05016; AAA58460.1; -; mRNA.
DR EMBL; AK290971; BAF83660.1; -; mRNA.
DR EMBL; AC093743; AAQ96863.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80065.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80066.1; -; Genomic_DNA.
DR EMBL; BC000425; AAH00425.1; -; mRNA.
DR EMBL; BC001928; AAH01928.1; -; mRNA.
DR EMBL; BC006344; AAH06344.1; -; mRNA.
DR EMBL; BC011754; AAH11754.1; -; mRNA.
DR PIR; A23723; A23723.
DR RefSeq; NP_004902.1; NM_004911.4.
DR UniGene; Hs.93659; -.
DR PDB; 3IDV; X-ray; 1.95 A; A=53-284.
DR PDBsum; 3IDV; -.
DR ProteinModelPortal; P13667; -.
DR SMR; P13667; 54-645.
DR IntAct; P13667; 12.
DR MINT; MINT-4999858; -.
DR STRING; 9606.ENSP00000286091; -.
DR PhosphoSite; P13667; -.
DR DMDM; 119530; -.
DR OGP; P13667; -.
DR REPRODUCTION-2DPAGE; IPI00009904; -.
DR PaxDb; P13667; -.
DR PeptideAtlas; P13667; -.
DR PRIDE; P13667; -.
DR DNASU; 9601; -.
DR Ensembl; ENST00000286091; ENSP00000286091; ENSG00000155660.
DR GeneID; 9601; -.
DR KEGG; hsa:9601; -.
DR UCSC; uc003wff.2; human.
DR CTD; 9601; -.
DR GeneCards; GC07M148700; -.
DR HGNC; HGNC:30167; PDIA4.
DR HPA; CAB017368; -.
DR HPA; HPA006139; -.
DR HPA; HPA006140; -.
DR neXtProt; NX_P13667; -.
DR PharmGKB; PA142671190; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000162459; -.
DR HOVERGEN; HBG005920; -.
DR InParanoid; P13667; -.
DR KO; K09582; -.
DR OMA; HHTFSTE; -.
DR OrthoDB; EOG7VHSX1; -.
DR PhylomeDB; P13667; -.
DR BRENDA; 5.3.4.1; 2681.
DR ChiTaRS; PDIA4; human.
DR EvolutionaryTrace; P13667; -.
DR GenomeRNAi; 9601; -.
DR NextBio; 36019; -.
DR PRO; PR:P13667; -.
DR ArrayExpress; P13667; -.
DR Bgee; P13667; -.
DR CleanEx; HS_PDIA4; -.
DR Genevestigator; P13667; -.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:ProtInc.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR GO; GO:0009306; P:protein secretion; TAS:ProtInc.
DR Gene3D; 3.40.30.10; -; 4.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR017068; Protein_diS-isomerase_A4.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 5.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Isomerase; Polymorphism; Redox-active center; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 645 Protein disulfide-isomerase A4.
FT /FTId=PRO_0000034229.
FT DOMAIN 21 169 Thioredoxin 1.
FT DOMAIN 158 301 Thioredoxin 2.
FT DOMAIN 505 636 Thioredoxin 3.
FT MOTIF 642 645 Prevents secretion from ER.
FT COMPBIAS 39 55 Asp/Glu-rich (acidic).
FT MOD_RES 366 366 N6-acetyllysine.
FT DISULFID 91 94 Redox-active (By similarity).
FT DISULFID 206 209 Redox-active (By similarity).
FT DISULFID 555 558 Redox-active (By similarity).
FT VARIANT 173 173 T -> M (in dbSNP:rs2290971).
FT /FTId=VAR_052580.
FT CONFLICT 102 102 E -> G (in Ref. 3; BAF83660).
FT STRAND 59 61
FT STRAND 64 66
FT TURN 69 71
FT HELIX 72 76
FT STRAND 80 87
FT HELIX 92 109
FT STRAND 111 113
FT STRAND 117 121
FT TURN 122 124
FT HELIX 126 131
FT STRAND 136 144
FT STRAND 147 150
FT HELIX 157 168
FT STRAND 178 181
FT TURN 184 186
FT HELIX 187 193
FT STRAND 195 202
FT HELIX 208 211
FT HELIX 213 224
FT STRAND 226 228
FT STRAND 232 236
FT TURN 237 239
FT HELIX 241 246
FT STRAND 251 259
FT STRAND 262 265
FT HELIX 272 282
SQ SEQUENCE 645 AA; 72932 MW; 1919C2AE12CD2684 CRC64;
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE
ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD KDPPIPVAKI
DATSASVLAS RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL
VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE
TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP
EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KVSNDAKRYT RRPLVVVYYS
VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD
ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM
DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL
//
ID PDIA4_HUMAN Reviewed; 645 AA.
AC P13667; A8K4K6; Q549T6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1991, sequence version 2.
DT 22-JAN-2014, entry version 158.
DE RecName: Full=Protein disulfide-isomerase A4;
DE EC=5.3.4.1;
DE AltName: Full=Endoplasmic reticulum resident protein 70;
DE Short=ER protein 70;
DE Short=ERp70;
DE AltName: Full=Endoplasmic reticulum resident protein 72;
DE Short=ER protein 72;
DE Short=ERp-72;
DE Short=ERp72;
DE Flags: Precursor;
GN Name=PDIA4; Synonyms=ERP70, ERP72;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2549034;
RA Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RT "Human deoxycytidine kinase. Sequence of cDNA clones and analysis of
RT expression in cell lines with and without enzyme activity.";
RL J. Biol. Chem. 264:14762-14768(1989).
RN [2]
RP ERRATUM, AND SEQUENCE REVISION.
RX PubMed=2002068;
RA Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RL J. Biol. Chem. 266:5353-5353(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Muscle;
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 [7]
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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).
CC -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC proteins.
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
CC UGT1A1 and very small amounts of ERP29, but not, or at very low
CC levels, CALR nor CANX.
CC -!- INTERACTION:
CC Q76353:- (xeno); NbExp=3; IntAct=EBI-1054653, EBI-6248077;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome.
CC Note=Identified by mass spectrometry in melanosome fractions from
CC stage I to stage IV.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC -!- SIMILARITY: Contains 3 thioredoxin domains.
CC -!- CAUTION: Was originally (PubMed:2549034) thought to be a
CC deoxycytidine kinase.
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DR EMBL; J05016; AAA58460.1; -; mRNA.
DR EMBL; AK290971; BAF83660.1; -; mRNA.
DR EMBL; AC093743; AAQ96863.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80065.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80066.1; -; Genomic_DNA.
DR EMBL; BC000425; AAH00425.1; -; mRNA.
DR EMBL; BC001928; AAH01928.1; -; mRNA.
DR EMBL; BC006344; AAH06344.1; -; mRNA.
DR EMBL; BC011754; AAH11754.1; -; mRNA.
DR PIR; A23723; A23723.
DR RefSeq; NP_004902.1; NM_004911.4.
DR UniGene; Hs.93659; -.
DR PDB; 3IDV; X-ray; 1.95 A; A=53-284.
DR PDBsum; 3IDV; -.
DR ProteinModelPortal; P13667; -.
DR SMR; P13667; 54-645.
DR IntAct; P13667; 12.
DR MINT; MINT-4999858; -.
DR STRING; 9606.ENSP00000286091; -.
DR PhosphoSite; P13667; -.
DR DMDM; 119530; -.
DR OGP; P13667; -.
DR REPRODUCTION-2DPAGE; IPI00009904; -.
DR PaxDb; P13667; -.
DR PeptideAtlas; P13667; -.
DR PRIDE; P13667; -.
DR DNASU; 9601; -.
DR Ensembl; ENST00000286091; ENSP00000286091; ENSG00000155660.
DR GeneID; 9601; -.
DR KEGG; hsa:9601; -.
DR UCSC; uc003wff.2; human.
DR CTD; 9601; -.
DR GeneCards; GC07M148700; -.
DR HGNC; HGNC:30167; PDIA4.
DR HPA; CAB017368; -.
DR HPA; HPA006139; -.
DR HPA; HPA006140; -.
DR neXtProt; NX_P13667; -.
DR PharmGKB; PA142671190; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000162459; -.
DR HOVERGEN; HBG005920; -.
DR InParanoid; P13667; -.
DR KO; K09582; -.
DR OMA; HHTFSTE; -.
DR OrthoDB; EOG7VHSX1; -.
DR PhylomeDB; P13667; -.
DR BRENDA; 5.3.4.1; 2681.
DR ChiTaRS; PDIA4; human.
DR EvolutionaryTrace; P13667; -.
DR GenomeRNAi; 9601; -.
DR NextBio; 36019; -.
DR PRO; PR:P13667; -.
DR ArrayExpress; P13667; -.
DR Bgee; P13667; -.
DR CleanEx; HS_PDIA4; -.
DR Genevestigator; P13667; -.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:ProtInc.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR GO; GO:0009306; P:protein secretion; TAS:ProtInc.
DR Gene3D; 3.40.30.10; -; 4.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR017068; Protein_diS-isomerase_A4.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 5.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Isomerase; Polymorphism; Redox-active center; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 645 Protein disulfide-isomerase A4.
FT /FTId=PRO_0000034229.
FT DOMAIN 21 169 Thioredoxin 1.
FT DOMAIN 158 301 Thioredoxin 2.
FT DOMAIN 505 636 Thioredoxin 3.
FT MOTIF 642 645 Prevents secretion from ER.
FT COMPBIAS 39 55 Asp/Glu-rich (acidic).
FT MOD_RES 366 366 N6-acetyllysine.
FT DISULFID 91 94 Redox-active (By similarity).
FT DISULFID 206 209 Redox-active (By similarity).
FT DISULFID 555 558 Redox-active (By similarity).
FT VARIANT 173 173 T -> M (in dbSNP:rs2290971).
FT /FTId=VAR_052580.
FT CONFLICT 102 102 E -> G (in Ref. 3; BAF83660).
FT STRAND 59 61
FT STRAND 64 66
FT TURN 69 71
FT HELIX 72 76
FT STRAND 80 87
FT HELIX 92 109
FT STRAND 111 113
FT STRAND 117 121
FT TURN 122 124
FT HELIX 126 131
FT STRAND 136 144
FT STRAND 147 150
FT HELIX 157 168
FT STRAND 178 181
FT TURN 184 186
FT HELIX 187 193
FT STRAND 195 202
FT HELIX 208 211
FT HELIX 213 224
FT STRAND 226 228
FT STRAND 232 236
FT TURN 237 239
FT HELIX 241 246
FT STRAND 251 259
FT STRAND 262 265
FT HELIX 272 282
SQ SEQUENCE 645 AA; 72932 MW; 1919C2AE12CD2684 CRC64;
MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE
ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD KDPPIPVAKI
DATSASVLAS RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL
VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE
TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL
KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP
EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KVSNDAKRYT RRPLVVVYYS
VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD
ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM
DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL
//