Q9XF61 (PDI_DATGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase
Short name=PDI
EC=5.3.4.1

Gene names

Name:

PDI

Organism

Datisca glomerata (Durango root)

Taxonomic identifier

34297 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Datiscaceae › Datisca

Protein attributes

Sequence length	507 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer By similarity.
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subcellular location	Endoplasmic reticulum lumen Potential.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 507	487	Protein disulfide-isomerase		PRO_0000034207
Regions
	Domain	21 – 144	124	Thioredoxin 1
	Domain	365 – 485	121	Thioredoxin 2
	Motif	504 – 507	4	Prevents secretion from ER By similarity
Sites
	Active site	62	1	Nucleophile By similarity
	Active site	65	1	Nucleophile By similarity
	Active site	407	1	Nucleophile By similarity
	Active site	410	1	Nucleophile By similarity
	Site	63	1	Contributes to redox potential value By similarity
	Site	64	1	Contributes to redox potential value By similarity
	Site	130	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	408	1	Contributes to redox potential value By similarity
	Site	409	1	Contributes to redox potential value By similarity
	Site	471	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	181	1	N-linked (GlcNAc...) Potential
	Glycosylation	278	1	N-linked (GlcNAc...) Potential
	Disulfide bond	62 ↔ 65		Redox-active By similarity
	Disulfide bond	407 ↔ 410		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9XF61 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 4CE20915BBB2B9D1	FASTA	507	57,089
	10 20 30 40 50 60 MASMVSFCFL LLFLAFFASS FNEIYAEESE SKEFVLTLDK SNFFDTVSKH NFIVVEFYAP 70 80 90 100 110 120 WCGHCKKLAP EYEKAASILS SHDPPVILAK VDANEEANKE LASEFEVRGF PTIKILRNGG 130 140 150 160 170 180 KIVQEYKGPR DADGIVDYLK KQSGPPSAEI KSIEDATNLV SEKKIVVVGI FPKFSGEEFE 190 200 210 220 230 240 NFSALAEKLR SDYEFGHTLD AKLLPRGESS VSGPVVRLFK PFDELFVDFQ DFDVNALEKL 250 260 270 280 290 300 VEESSVPTVT IFDKDPSNHP FVVKFFNNAN AKAMLFLNFT SEVVESFRSI YREVAEKNKG 310 320 330 340 350 360 EGISFLIGDT ESSQGAFQYF GLRDDQVPLI VIQNNDGTKY LKPNLEPDHI ASWVKEYKDC 370 380 390 400 410 420 KLSPYRKSEP IPEHNNEPVK VVVADSLDEI VFKSGKNVLL EFYAPWCGHC KQLAPILDEV 430 440 450 460 470 480 AVSFENDPDV LIAKLDATAN DYPTNTFDVK GYPTLYFKSA SGELLQYDGG RTKEDFIEFI 490 500 EKNREKSSKK ESIVKDDQTD SETKAEL

References

[1]	"DgPDIa, full-length cDNA from symbiotic root nodules of Datisca glomerata with homology to protein disulfide isomerase genes." Okubara P.A., Berry A.M. Plant Gene Register PGR99-052 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Root nodule.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF131223 mRNA. Translation: AAD28260.1.
3D structure databases
ProteinModelPortal	Q9XF61.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 3 hits.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 4 hits.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. Pdi_dom. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDI_DATGL

Accession

Primary (citable) accession number: Q9XF61

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	September 21, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program