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Q5XI02 (PDILT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein disulfide-isomerase-like protein of the testis
Gene names
Name:Pdilt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable redox-inactive chaperone involved in spermatogenesis By similarity.

Subunit structure

Homodimer. The homodimer is not disulfide-linked. Interacts with ERO1L and CLGN By similarity.

Subcellular location

Endoplasmic reticulum By similarity.

Tissue specificity

Testis-specific. Expressed exclusively in postmeiotic male germ cells (at protein level). Ref.2

Developmental stage

Induced during puberty. Ref.2

Domain

The thioredoxin domain lacks the conserved redox-active Cys at position 414 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 1 thioredoxin domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 590570Protein disulfide-isomerase-like protein of the testis
PRO_0000325852

Regions

Domain385 – 44864Thioredoxin
Motif587 – 5904Prevents secretion from ER Potential

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5XI02 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 6F73FA1B8CD304DD

FASTA59068,267
        10         20         30         40         50         60 
MELLWTPLLL LAACLSEVLG SPEMDTGINI SQPLHILEDH NLMVLTPAGL TQTLNETRFL 

        70         80         90        100        110        120 
MVIFHNPTLK QSRKLAKELG KAAEIFGKGK NGLGFGKVDI TMETELKQEF DITHAPELKL 

       130        140        150        160        170        180 
FYEGNRLEPI SCKDVVESTA LVVWLRRQIS KKALLFNNSN EVADFVKSRP LVIVGFFQDL 

       190        200        210        220        230        240 
EEEVAELFYD TIKDFPELTF GAIQIKNSFG RFHVILDSVL VFKKGRVVKR QELINDSTNK 

       250        260        270        280        290        300 
DYLNQVIKQQ LTGFVIEFNP ENKDLIYEMN ILNHMLLFIS KNSEPYSTII RHYRQISKEF 

       310        320        330        340        350        360 
QNKILFVLVN SDEPKNKRIF EYFQISRVNV PSVQILNLSS DARYKMPTDN ITFESLKKFC 

       370        380        390        400        410        420 
NSFLSRTAKK HKSSEEIPKY WDQEPVKKLV GKNFNVVVFD KEKDVFVMFY APWSEKCRVL 

       430        440        450        460        470        480 
LPLLEELGIK YQNHSTVIIA KIDITANDIQ LANPEQYPFF RLFPTDSQEA VMYKGEHTMK 

       490        500        510        520        530        540 
GFCDFLESHV KVRIEEDDEL LYIEQNEVAE EEVLAEPEMQ HIDKLPEKPP LKVEDTSKQD 

       550        560        570        580        590 
RPAKESPALG SISQPEELER RKETAEKEKK VAQPKEQPKP ERKLDIKEEL 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[2]"A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells."
van Lith M., Karala A.R., Bown D., Gatehouse J.A., Ruddock L.W., Saunders P.T.K., Benham A.M.
Mol. Biol. Cell 18:2795-2804(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC083897 mRNA. Translation: AAH83897.1.
RefSeqNP_001013924.1. NM_001013902.1.
UniGeneRn.146183.

3D structure databases

ProteinModelPortalQ5XI02.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000020817.

PTM databases

PhosphoSiteQ5XI02.

Proteomic databases

PRIDEQ5XI02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000020817; ENSRNOP00000020817; ENSRNOG00000015368.
GeneID293544.
KEGGrno:293544.
UCSCRGD:1307822. rat.

Organism-specific databases

CTD204474.
RGD1307822. Pdilt.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115202.
HOGENOMHOG000115479.
HOVERGENHBG108240.
InParanoidQ5XI02.
OMAQKAFLFN.
OrthoDBEOG7VHSX1.
PhylomeDBQ5XI02.
TreeFamTF106381.

Gene expression databases

GenevestigatorQ5XI02.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio636364.

Entry information

Entry namePDILT_RAT
AccessionPrimary (citable) accession number: Q5XI02
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families