ID Q3URP6_MOUSE Unreviewed; 509 AA. AC Q3URP6; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00039846, ECO:0000256|RuleBase:RU361130}; DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130}; GN Name=P4hb {ECO:0000313|MGI:MGI:97464}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE24642.1}; RN [1] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE24642.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE24642.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:BAE24642.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). 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: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. CC Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. 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; AK141304; BAE24642.1; -; mRNA. DR AlphaFoldDB; Q3URP6; -. DR PeptideAtlas; Q3URP6; -. DR AGR; MGI:97464; -. DR MGI; MGI:97464; P4hb. DR ChiTaRS; P4hb; mouse. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC. DR CDD; cd02961; PDI_a_family; 1. DR CDD; cd02995; PDI_a_PDI_a'_C; 1. DR CDD; cd02982; PDI_b'_family; 1. DR CDD; cd02981; PDI_b_family; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 4. DR InterPro; IPR005788; PDI_thioredoxin-like_dom. DR InterPro; IPR005792; Prot_disulphide_isomerase. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR NCBIfam; TIGR01130; ER_PDI_fam; 1. DR NCBIfam; TIGR01126; pdi_dom; 2. DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1. DR PANTHER; PTHR18929:SF101; PROTEIN DISULFIDE-ISOMERASE; 1. DR Pfam; PF00085; Thioredoxin; 2. DR Pfam; PF13848; Thioredoxin_6; 1. DR PRINTS; PR00421; THIOREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 4. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 2. PE 2: Evidence at transcript level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186}; 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 Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|PIRSR:PIRSR605792-51}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|RuleBase:RU361130" FT CHAIN 22..509 FT /note="Protein disulfide-isomerase" FT /evidence="ECO:0000256|RuleBase:RU361130" FT /id="PRO_5005143197" FT DOMAIN 11..136 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT DOMAIN 348..477 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT DISULFID 55..58 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51" FT DISULFID 399..402 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51" SQ SEQUENCE 509 AA; 56998 MW; 79353DD9B826F02E CRC64; MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFEEAL AAHKYLLVEF YAPWCGHCKA LAPECAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLSDTAAAES LVDSSEVTVI GFFKDVESDS AKQFLLAAEA IDDIPFGITS NSGVFSKYQL DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI EFTEQTAPKI FGGEIKTHIL LFLPKSVSDY DGKLSSFKRA AEGFKGKILF IFIDSDHTDN QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE GKIKPHLMSQ EVPEDWDKQP VKVLVGANFE EVAFDEKKNV FVEFYAPWCG HCKQLAPIWD KLGETYKDHE NIIIAKMDST ANEVEAVKVH SFPTLKFFPA SADRTVIDYN GERTLDGFKK FLESGGQDGA GDDEDLDLEE ALEPDMEEDD DQKAVKDEL //