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Protein

Protein disulfide-isomerase-like protein of the testis

Gene

Pdilt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probable redox-inactive chaperone involved in spermatogenesis.By similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: GO_Central

GO - Biological processi

  1. cell migration Source: Ensembl
  2. cell redox homeostasis Source: InterPro
  3. multicellular organismal development Source: UniProtKB-KW
  4. protein folding Source: GO_Central
  5. spermatid development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Developmental protein, Isomerase

Keywords - Biological processi

Differentiation, Spermatogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase-like protein of the testis
Gene namesi
Name:Pdilt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi1307822. Pdilt.

Subcellular locationi

Endoplasmic reticulum PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 590570Protein disulfide-isomerase-like protein of the testisPRO_0000325852Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ5XI02.

PTM databases

PhosphoSiteiQ5XI02.

Expressioni

Tissue specificityi

Testis-specific. Expressed exclusively in postmeiotic male germ cells (at protein level).1 Publication

Developmental stagei

Induced during puberty.1 Publication

Gene expression databases

GenevestigatoriQ5XI02.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020817.

Structurei

3D structure databases

ProteinModelPortaliQ5XI02.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini385 – 44864ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi587 – 5904Prevents secretion from ERPROSITE-ProRule annotation

Domaini

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.

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000115479.
HOVERGENiHBG108240.
InParanoidiQ5XI02.
OMAiQKAFLFN.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ5XI02.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5XI02-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELLWTPLLL LAACLSEVLG SPEMDTGINI SQPLHILEDH NLMVLTPAGL
60 70 80 90 100
TQTLNETRFL MVIFHNPTLK QSRKLAKELG KAAEIFGKGK NGLGFGKVDI
110 120 130 140 150
TMETELKQEF DITHAPELKL FYEGNRLEPI SCKDVVESTA LVVWLRRQIS
160 170 180 190 200
KKALLFNNSN EVADFVKSRP LVIVGFFQDL EEEVAELFYD TIKDFPELTF
210 220 230 240 250
GAIQIKNSFG RFHVILDSVL VFKKGRVVKR QELINDSTNK DYLNQVIKQQ
260 270 280 290 300
LTGFVIEFNP ENKDLIYEMN ILNHMLLFIS KNSEPYSTII RHYRQISKEF
310 320 330 340 350
QNKILFVLVN SDEPKNKRIF EYFQISRVNV PSVQILNLSS DARYKMPTDN
360 370 380 390 400
ITFESLKKFC NSFLSRTAKK HKSSEEIPKY WDQEPVKKLV GKNFNVVVFD
410 420 430 440 450
KEKDVFVMFY APWSEKCRVL LPLLEELGIK YQNHSTVIIA KIDITANDIQ
460 470 480 490 500
LANPEQYPFF RLFPTDSQEA VMYKGEHTMK GFCDFLESHV KVRIEEDDEL
510 520 530 540 550
LYIEQNEVAE EEVLAEPEMQ HIDKLPEKPP LKVEDTSKQD RPAKESPALG
560 570 580 590
SISQPEELER RKETAEKEKK VAQPKEQPKP ERKLDIKEEL
Length:590
Mass (Da):68,267
Last modified:November 23, 2004 - v1
Checksum:i6F73FA1B8CD304DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083897 mRNA. Translation: AAH83897.1.
RefSeqiNP_001013924.1. NM_001013902.1.
UniGeneiRn.146183.

Genome annotation databases

EnsembliENSRNOT00000020817; ENSRNOP00000020817; ENSRNOG00000015368.
GeneIDi293544.
KEGGirno:293544.
UCSCiRGD:1307822. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083897 mRNA. Translation: AAH83897.1.
RefSeqiNP_001013924.1. NM_001013902.1.
UniGeneiRn.146183.

3D structure databases

ProteinModelPortaliQ5XI02.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020817.

PTM databases

PhosphoSiteiQ5XI02.

Proteomic databases

PRIDEiQ5XI02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020817; ENSRNOP00000020817; ENSRNOG00000015368.
GeneIDi293544.
KEGGirno:293544.
UCSCiRGD:1307822. rat.

Organism-specific databases

CTDi204474.
RGDi1307822. Pdilt.

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000115479.
HOVERGENiHBG108240.
InParanoidiQ5XI02.
OMAiQKAFLFN.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ5XI02.
TreeFamiTF106381.

Miscellaneous databases

NextBioi636364.

Gene expression databases

GenevestigatoriQ5XI02.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 4 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPDILT_RAT
AccessioniPrimary (citable) accession number: Q5XI02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 23, 2004
Last modified: February 4, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.