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P29828

- PDI_MEDSA

UniProt

P29828 - PDI_MEDSA

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Protein

Protein disulfide-isomerase

Gene
PDI
Organism
Medicago sativa (Alfalfa)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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 – 621Nucleophile By similarity
Sitei63 – 631Contributes to redox potential value By similarity
Sitei64 – 641Contributes to redox potential value By similarity
Active sitei65 – 651Nucleophile By similarity
Sitei130 – 1301Lowers pKa of C-terminal Cys of first active site By similarity
Active sitei407 – 4071Nucleophile By similarity
Sitei408 – 4081Contributes to redox potential value By similarity
Sitei409 – 4091Contributes to redox potential value By similarity
Active sitei410 – 4101Nucleophile By similarity
Sitei471 – 4711Lowers pKa of C-terminal Cys of second active site By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

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 Reviewed prediction

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 65Redox-active By similarity
Glycosylationi278 – 2781N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi407 ↔ 410Redox-active By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

ProMEXiP29828.

Structurei

3D structure databases

ProteinModelPortaliP29828.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 144120Thioredoxin 1Add
BLAST
Domaini357 – 485129Thioredoxin 2Add
BLAST

Motif

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

Sequence similaritiesi

Contains 2 thioredoxin domains.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161L → V in AAA32662. 1 Publication
Sequence conflicti395 – 3951G → A in AAA32662. 1 Publication
Sequence conflicti491 – 4911H → Q in AAA32662. 1 Publication

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: September 3, 2014
This is version 97 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

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