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Q9DAN1 (PDILT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length588 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 CLGN and ERO1L By similarity.

Subcellular location

Endoplasmic reticulum By similarity.

Tissue specificity

Testis-specific (at protein level). Ref.2 Ref.3

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.

Sequence caution

The sequence BAB24190.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 588568Protein disulfide-isomerase-like protein of the testis
PRO_0000325851

Regions

Domain385 – 44864Thioredoxin
Motif585 – 5884Prevents secretion from ER Potential

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9DAN1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 1B0A73E5DBDF6187

FASTA58867,759
        10         20         30         40         50         60 
MELLWTPLLL VAACLSEVLG SPEIDTGINI SQPLHILEDH NLMVLTPAGL TQTLNETRFL 

        70         80         90        100        110        120 
MVIFHNPSLK QSRKLAKELG KAAEIFGKGK NGLGFGKVDI TKETELQQEF DITHAPELKL 

       130        140        150        160        170        180 
FFEGNRLKPI SCKDVVESTA LVVWLRRQIS KKALLFNNSD EVADFVKSRP LVIVGFFQDL 

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

       250        260        270        280        290        300 
DHLNQVIKQQ LTGFVIELNP ENKDLIYELN ILNHMLLFIS KSSEPYSTIS RHYRQIAKEF 

       310        320        330        340        350        360 
QNKILFVLVN ADEPKNKRIF EYFQISRVNV PSVQILNLSS DGRYKMPTDD INFESLKKFC 

       370        380        390        400        410        420 
NSFLSKTAKK HKASEEIPKY WDQGPVKKLV GKNFNVVVLD KEKDVFVMFY APWSEKCRVL 

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

       490        500        510        520        530        540 
GFCDFLESHV KVRIEEEDEL LYIEQNEEEE VLAEPEIQLI EKLPENPLLK IEDTSKQDRP 

       550        560        570        580 
VKESPVLDSI RKPEEPERRK ETAEREAAAA QPKEQPKPER KLEVKEEL 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[2]"PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum."
van Lith M., Hartigan N., Hatch J., Benham A.M.
J. Biol. Chem. 280:1376-1383(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK005692 mRNA. Translation: BAB24190.1. Different initiation.
CCDSCCDS52378.1.
RefSeqNP_082219.1. NM_027943.1.
XP_006508277.1. XM_006508214.1.
UniGeneMm.84631.

3D structure databases

ProteinModelPortalQ9DAN1.
SMRQ9DAN1. Positions 30-488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60024N.
STRING10090.ENSMUSP00000033267.

PTM databases

PhosphoSiteQ9DAN1.

Proteomic databases

PaxDbQ9DAN1.
PRIDEQ9DAN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033267; ENSMUSP00000033267; ENSMUSG00000030968.
GeneID71830.
KEGGmmu:71830.
UCSCuc009jld.1. mouse.

Organism-specific databases

CTD204474.
MGIMGI:1919080. Pdilt.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00740000115202.
HOGENOMHOG000115479.
HOVERGENHBG108240.
InParanoidQ9DAN1.
OMAQKAFLFN.
OrthoDBEOG7VHSX1.
PhylomeDBQ9DAN1.
TreeFamTF106381.

Gene expression databases

BgeeQ9DAN1.
CleanExMM_1700007B13RIK.
GenevestigatorQ9DAN1.

Family and domain databases

Gene3D3.40.30.10. 4 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

NextBio334632.
PROQ9DAN1.
SOURCESearch...

Entry information

Entry namePDILT_MOUSE
AccessionPrimary (citable) accession number: Q9DAN1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 9, 2014
This is version 98 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot