ID A0A0L0C696_LUCCU Unreviewed; 3058 AA.
AC A0A0L0C696;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ORFNames=FF38_10849 {ECO:0000313|EMBL:KNC26939.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC26939.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC26939.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC26939.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC26939.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC26939.1}.
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DR EMBL; JRES01000945; KNC26939.1; -; Genomic_DNA.
DR STRING; 7375.A0A0L0C696; -.
DR EnsemblMetazoa; KNC26939; KNC26939; FF38_10849.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; 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; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
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 Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW 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..3058
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005394085"
FT DOMAIN 134..258
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 457..598
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 88..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1620..1849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2055..2097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2508..2533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2709..2733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2845..2870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2901..2993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1967
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2058..2090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2845..2864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2901..2917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2927..2993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 180..183
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 521..524
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 3058 AA; 346917 MW; 23C14F42A981EA5F CRC64;
MKFLLCSLLL VATATLGVVY ADEEIKTEDG VLVLTVDNFK KAIADNEFIL AKKSNLTETG
DKNHSNDDNQ EPYQPTTHIN QAYRRDSIHI SSSPPEGPEE HEEDDGTDVQ DEHDDALLNE
EVDEEEEPNA YAFLPTASKK PEKEIFAKQI RPMGPYPTYN NMQANDKVVF SQALTHAPWC
GHCKSLAPEY AKAAQTLAEK ESNIKLAKVD ATVEGPLAEE YQVRGYPTLK FFRNGAPVEY
TGGRQAADIV SWVNKKTGPP AKDLPTVEEA EKFLKDNEIA IIGFFKDLES DAAKTFVTAA
GELDPIPFGL TSSDDVVAKY EVKDGAVVMF KPFDDKKTVF EGELTLATLK KFAQVESLPL
IVEFNHESAS KIFGGQIKSH LLFFVSKEAG HIEKYVEPLK DIAKQYRDDI LFVTISSDEE
DHARIFEFFG MTKEEVPTIR LIKLEEDMAK YKPENNDLSA ETIKDFLQKF MDGKLKQHLL
SQELPEDWDK NPVKVLVATN FDDVAMDKSK DVLVEFYAPW CGHCKQLAPI YEQLGEKFKD
SETVVIAKID STANELEHTK ISSFPTIKLY RKGDNKVIDY NLDRTLDDFV KFLEAGGDLK
SAEEEEKVEE EEEHKKDEFM LSFKEFKATV CTAKVAGPQQ KEIKTTAAAI TTTTTKNSDS
AKDHNLVLPT TSTTAAAAAL AAASSPSSNS NASSNISSSA AATTTNLKMY KLFTFIDDIY
RDIRRYNSGL YKDSYSTQLM QTINKYKNGC NEIFGKVLES PDMSLKLSQN IVRTLDIFKQ
LSTCLSDLEE YHYRVCEIMS IFIVCELRLS VDAANTPQEQ LAIAHRIIYI MRRHLVQEEE
DATLYNILRT LVYIPKLYNA RDIMCAIFGE FIPIKPVSEV NVLPDKLYML YIIVFYRWMM
MQKDDDDKLL IVNFAESFMK PSVSLCSNNL YGSYLPMYTT HSTATRTILN NLKFYRDIRN
ASIIDNALKT IGSIVTPKKQ KKRVQFNTSP LGPTVPSSTH KMPLKPAIQQ QKYKASDASE
YFHLRDFDGS SYAGSVAGSS TSNSTSSSIK HQEQQESTNQ ECINKQEILK YTTNNVKDHN
NKCSNFNKNL SVFNQKSLNM NLKQKTIKNV KINLKKLRFN NDISLTNFKS NFSKEQLHLP
HTQQNTALII SNTKNNDNSS TYKRTETCQL KCNPIATITK QSDDDMIFKK PLPVTKKVFK
SSPKPLKIHK VVSLRRHQQQ HPYHMKPREV IKRETPELEN NLLKVCIKQE NVDDNRASEM
HLEPENVNDN KTQLSTTDED VEMDDLSKIS KLLTEEINSL TCDATEKSKE LKETSDLLIS
QELSKESLDK EKESVVTPKD LELKEILVEE NITKSNKQLV NESNTNLSED NETFDEVNPN
ILEEKEIVEQ QNNTEIVTET IEKDDSLNLE EKDKNTLNSK VEQKEDEVKD TAEEQPKETE
KVTEENLQPT NMEAEENPIR ETITKDGDTE DTTVAQEPEI LNEEQQSTDI ESTETLEEEE
RTETAKLVTN FCAEYLAGLQ NEPLPQTLSE TVEEKETGHC DSKNDNDFEF ENNCTTPISM
CHIDIDVMTE NTSELPASMP LTQLDAEACE AAKLLEDFNN KTEDIVDSAL NKKALDNNES
IENSVYQDDD KDSNEDRQPL KRLREKDEDH EEESLIEIKK SKCKETDEEC LNPSKENITT
SRKEEESSEH MEEETKIEVK ETEIISKDTK EPNITNSNNI NELKLTSSKT PKKQKNNSIQ
TELSKEKKLK RTNKSTKPQE KCPNYSKSEN IKEDDTEEKS NNENSQNDNQ ETNTEPLSEE
HSSKEEEMRT QEVEASLNEN QHMTLELGNW NKEDMENETK TNDSDSQGVS AIFSFPKIPI
ISISICTTPN NKTYFKISNR ENEKQSKEGN NKSKKSKSIQ QDLEAETKNE EKELSTSLET
QEIVKNLEES DDNAENINED EEEDVEEKDD EEEEEDDEEE EEEEADNMEI EKFNHDSNSA
CSLPLKKRPT QAEPNEETED TQLTLPTTYE QPQEIAAEVV IEDTDKDKET LIEVNQPEIK
EHLEQDLQQE VNKNVENENH SSEASFSLTA SDYDDNKPST SANSLRKLTD PSSPFKRRVH
MPIRPIGQPP IQIVAPQLKD NPLPCPTPEN RPMDPQQLPT VARMQTQTTQ SLPESYPATP
MLSVANVEKL MDLNRFIEDL LASPDVMTII DNANACGYYA EGQAYEMERI AILEHYNIAN
AKGNTSVTKP LYWKKSAGDT ISIFNDNDNE WIALPPSTAK QLLKLSFVLS ILQQQYKVSD
VRQRINIALT FLIQTSYTSK FKKNSKAANS LQQRMQLYSR SISEATNSGH NISQPLPSAS
YFRIATNNEA LNTSFNITHN MDAVQDFAST NYSSNATQNE MSLNQEPVVN ANQSWNNLMQ
FSTVANTGQV IEQNNNNTNS PQRMAEVEQQ QQQAQDKRNS TWEELNNDQL YINPPCATSP
QNEVIVNTNG VQLHEMPQNF QDQQNIFISI TDESVNDNGA LHKYNTRQQH QQQQQQHLRA
IGDEEPSSSS TQQFYAKRPC LTNNNAAANL MQNNFSRNNV INTFGNQEIN LQNPYRLQQN
QQQLQQQPTP LTLTNQHLNV TTSPNSNFSA QRNISPKSLG HNLPINIYNN NRNTNTPLAP
QQQQQRMNTR YSNSFNAATT ATTNQQQTVN KNPESNYKEI LQPYITYLIK DHEKTSKHLL
QVFEEVSNSH GNTTEQNNSN NSFNQPQSQF NSLLPPLIRN PQQNHMPGLH QLPSSSGSVL
PSLVRNPHQT TMPHRDSGAL QVVQSFLEQS QTEYDNAQQA KTTSVSASLS PTLPGFAKEY
VNFVGSRDEI VQKQKLPQHL PPQQLQENHT QQQELLQQDP QRLNSVKRKC QERNDKLAED
LKRKMMEFSL LKHNVQAKLM EKQQDEVKKD TSTNANIKRR GRPKKNLITT EPSSSASSAG
SLCNSDSSCE ASSPTTSKQK KAKQTSARVT RRQQNNNDLN NTNTNTSPNS TTTTIDHAYF
RQRTAAREAV KRINATSCKS AIIQKFKKEI GLICKTKSYD KWYISSGCSK GLHVDISL
//
