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Database: UniProt
Entry: P13667
LinkDB: P13667
Original site: P13667 
ID   PDIA4_HUMAN             Reviewed;         645 AA.
AC   P13667; A8K4K6; Q549T6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   16-APR-2014, entry version 161.
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].
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].
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 IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [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       P23284:PPIB; NbExp=3; IntAct=EBI-1054653, EBI-8771982;
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   BioGrid; 114966; 52.
DR   IntAct; P13667; 16.
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   TreeFam; TF106382; -.
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:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProt.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProt.
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
//
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