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P29828

- PDI_MEDSA

UniProt

P29828 - PDI_MEDSA

Protein

Protein disulfide-isomerase

Gene

PDI

Organism
Medicago sativa (Alfalfa)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.By similarity

    Catalytic activityi

    Catalyzes the rearrangement of -S-S- bonds in proteins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei62 – 621NucleophileBy similarity
    Sitei63 – 631Contributes to redox potential valueBy similarity
    Sitei64 – 641Contributes to redox potential valueBy similarity
    Active sitei65 – 651NucleophileBy similarity
    Sitei130 – 1301Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei407 – 4071NucleophileBy similarity
    Sitei408 – 4081Contributes to redox potential valueBy similarity
    Sitei409 – 4091Contributes to redox potential valueBy similarity
    Active sitei410 – 4101NucleophileBy similarity
    Sitei471 – 4711Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. protein disulfide isomerase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase (EC:5.3.4.1)
    Short name:
    PDI
    Gene namesi
    Name:PDI
    OrganismiMedicago sativa (Alfalfa)
    Taxonomic identifieri3879 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424By similarityAdd
    BLAST
    Chaini25 – 512488Protein disulfide-isomerasePRO_0000034209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi62 ↔ 65Redox-activePROSITE-ProRule annotation
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi407 ↔ 410Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    ProMEXiP29828.

    Structurei

    3D structure databases

    ProteinModelPortaliP29828.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 144120Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini357 – 485129Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi509 – 5124Prevents secretion from ER

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 2 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 4 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 2 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P29828-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKNVAIFGL LFSLLLLVPS QIFAEESSTD AKEFVLTLDN TNFHDTVKKH    50
    DFIVVEFYAP WCGHCKKLAP EYEKAASILS THEPPVVLAK VDANEEHNKD 100
    LASENDVKGF PTIKIFRNGG KNIQEYKGPR EAEGIVEYLK KQSGPASTEI 150
    KSADDATAFV GDNKVVIVGV FPKFSGEEYD NFIALAEKLR SDYDFAHTLN 200
    AKHLPKGDSS VSGPVVRLFK PFDELFVDSK DFNVEALEKF IEESSTPIVT 250
    VFNNEPSNHP FVVKFFNSPN AKAMLFINFT TEGAESFKTK YHEVAEQYKQ 300
    QGVSFLVGDV ESSQGAFQYF GLKEEQVPLI IIQHNDGKKF FKPNLELDQL 350
    PTWLKAYKDG KVEPFVKSEP IPETNNEPVK VVVGQTLEDV VFKSGKNVLI 400
    EFYAPWCGHC KQLAPILDEV AVSFQSDADV VIAKLDATAN DIPTDTFDVQ 450
    GYPTLYFRSA SGKLSQYDGG RTKEDIIEFI EKNKDKTGAA HQEVEQPKAA 500
    AQPEAEQPKD EL 512
    Length:512
    Mass (Da):57,087
    Last modified:April 1, 1993 - v1
    Checksum:iE5EC7341A3FF7935
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161L → V in AAA32662. (PubMed:1720555)Curated
    Sequence conflicti395 – 3951G → A in AAA32662. (PubMed:1720555)Curated
    Sequence conflicti491 – 4911H → Q in AAA32662. (PubMed:1720555)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11499 mRNA. Translation: CAA77575.1.
    M82973 mRNA. Translation: AAA32662.1.
    PIRiA41440.
    S22479. ISAASS.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11499 mRNA. Translation: CAA77575.1 .
    M82973 mRNA. Translation: AAA32662.1 .
    PIRi A41440.
    S22479. ISAASS.

    3D structure databases

    ProteinModelPortali P29828.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    ProMEXi P29828.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 2 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis and developmental expression of an alfalfa protein disulfide isomerase."
      Shorrosh B.S., Dixon R.A.
      Plant Mol. Biol. 19:319-321(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Apollo.
    2. "Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C."
      Shorrosh B.S., Dixon R.A.
      Proc. Natl. Acad. Sci. U.S.A. 88:10941-10945(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPDI_MEDSA
    AccessioniPrimary (citable) accession number: P29828
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3