ID A0A499FI48_HUMAN Unreviewed; 646 AA. AC A0A499FI48; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 07-APR-2021, entry version 13. DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130}; DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130}; GN Name=PDIA4 {ECO:0000313|Ensembl:ENSP00000286091}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000286091, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000286091, ECO:0000313|Proteomes:UP000005640} 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., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., 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., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000286091} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2019) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182, CC ECO:0000256|RuleBase:RU361130}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000256|ARBA:ARBA00004319}. Melanosome CC {ECO:0000256|ARBA:ARBA00004223}. CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family. CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093743; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006716248.1; XM_006716185.2. DR PeptideAtlas; A0A499FI48; -. DR Antibodypedia; 3377; 465 antibodies. DR Ensembl; ENST00000286091; ENSP00000286091; ENSG00000155660. DR HGNC; HGNC:30167; PDIA4. DR OpenTargets; ENSG00000155660; -. DR GeneTree; ENSGT00940000157738; -. DR OMA; TQFWRNK; -. DR ChiTaRS; PDIA4; human. DR Proteomes; UP000005640; Chromosome 7. DR ExpressionAtlas; A0A499FI48; baseline and differential. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC. DR CDD; cd03068; PDI_b_ERp72; 1. DR Gene3D; 3.40.30.10; -; 5. DR InterPro; IPR005788; Disulphide_isomerase. DR InterPro; IPR041866; PDIA4_PDI_b. DR InterPro; IPR005792; Prot_disulphide_isomerase. DR InterPro; IPR017068; Protein_diS-isomerase_A4. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR Pfam; PF00085; Thioredoxin; 3. DR PIRSF; PIRSF036862; Disulphide_isom_A4; 1. DR SUPFAM; SSF52833; SSF52833; 5. DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1. DR TIGRFAMs; TIGR01126; pdi_dom; 3. DR PROSITE; PS00194; THIOREDOXIN_1; 3. DR PROSITE; PS51352; THIOREDOXIN_2; 3. PE 1: Evidence at protein level; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130}; KW Proteomics identification {ECO:0007829|EPD:A0A499FI48, KW ECO:0007829|MaxQB:A0A499FI48}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|PIRSR:PIRSR605792-51}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|RuleBase:RU361130" FT CHAIN 25..646 FT /note="Protein disulfide-isomerase" FT /evidence="ECO:0000256|RuleBase:RU361130" FT /id="PRO_5019882486" FT DOMAIN 20..156 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT DOMAIN 158..301 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT DOMAIN 506..637 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT REGION 24..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..58 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 206..209 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51" FT DISULFID 556..559 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51" SQ SEQUENCE 646 AA; 73061 MW; 1D084B3CCD891CD0 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 SHMMDVQQGS TQDSAIKDFV LKYALPLVGH RKVSNDAKRY TRRPLVVVYY SVDFSFDYRA ATQFWRSKVL EVAKDFPEYT FAIADEEDYA GEVKDLGLSE SGEDVNAAIL DESGKKFAME PEEFDSDTLR EFVTAFKKGK LKPVIKSQPV PKNNKGPVKV VVGKTFDSIV MDPKKDVLIE FYAPWCGHCK QLEPVYNSLA KKYKGQKGLV IAKMDATAND VPSDRYKVEG FPTIYFAPSG DKKNPVKFEG GDRDLEHLSK FIEEHATKLS RTKEEL //