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Protein

Protein disulfide-isomerase-like protein of the testis

Gene

Pdilt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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: MGI

GO - Biological processi

  1. cell migration Source: MGI
  2. cell redox homeostasis Source: InterPro
  3. multicellular organismal development Source: UniProtKB-KW
  4. protein folding Source: GOC
  5. spermatid development Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1919080. 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 – 588568Protein disulfide-isomerase-like protein of the testisPRO_0000325851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9DAN1.
PRIDEiQ9DAN1.

PTM databases

PhosphoSiteiQ9DAN1.

Expressioni

Tissue specificityi

Testis-specific (at protein level).2 Publications

Gene expression databases

BgeeiQ9DAN1.
CleanExiMM_1700007B13RIK.
GenevestigatoriQ9DAN1.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-60024N.
STRINGi10090.ENSMUSP00000033267.

Structurei

3D structure databases

ProteinModelPortaliQ9DAN1.
SMRiQ9DAN1. Positions 30-488.
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
Motifi585 – 5884Prevents 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.
InParanoidiQ9DAN1.
OMAiQKAFLFN.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ9DAN1.
TreeFamiTF106381.

Family and domain databases

Gene3Di3.40.30.10. 4 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.

Q9DAN1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELLWTPLLL VAACLSEVLG SPEIDTGINI SQPLHILEDH NLMVLTPAGL
60 70 80 90 100
TQTLNETRFL MVIFHNPSLK QSRKLAKELG KAAEIFGKGK NGLGFGKVDI
110 120 130 140 150
TKETELQQEF DITHAPELKL FFEGNRLKPI SCKDVVESTA LVVWLRRQIS
160 170 180 190 200
KKALLFNNSD EVADFVKSRP LVIVGFFQDL EEEVAELFYD TIKDFPELTF
210 220 230 240 250
GAIQIKNSFG RFHVILDSVL VFKKGKIVKR QELINDSTNK DHLNQVIKQQ
260 270 280 290 300
LTGFVIELNP ENKDLIYELN ILNHMLLFIS KSSEPYSTIS RHYRQIAKEF
310 320 330 340 350
QNKILFVLVN ADEPKNKRIF EYFQISRVNV PSVQILNLSS DGRYKMPTDD
360 370 380 390 400
INFESLKKFC NSFLSKTAKK HKASEEIPKY WDQGPVKKLV GKNFNVVVLD
410 420 430 440 450
KEKDVFVMFY APWSEKCRVL LPLLEELGIK YQNHSTVIIA KIDITANDIQ
460 470 480 490 500
LANPEQYPFF RLFPTDSQEA VMYKGEHTMK GFCDFLESHV KVRIEEEDEL
510 520 530 540 550
LYIEQNEEEE VLAEPEIQLI EKLPENPLLK IEDTSKQDRP VKESPVLDSI
560 570 580
RKPEEPERRK ETAEREAAAA QPKEQPKPER KLEVKEEL
Length:588
Mass (Da):67,759
Last modified:March 18, 2008 - v2
Checksum:i1B0A73E5DBDF6187
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005692 mRNA. Translation: BAB24190.1. Different initiation.
CCDSiCCDS52378.1.
RefSeqiNP_082219.1. NM_027943.1.
XP_006508277.1. XM_006508214.1.
UniGeneiMm.84631.

Genome annotation databases

EnsembliENSMUST00000033267; ENSMUSP00000033267; ENSMUSG00000030968.
GeneIDi71830.
KEGGimmu:71830.
UCSCiuc009jld.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005692 mRNA. Translation: BAB24190.1. Different initiation.
CCDSiCCDS52378.1.
RefSeqiNP_082219.1. NM_027943.1.
XP_006508277.1. XM_006508214.1.
UniGeneiMm.84631.

3D structure databases

ProteinModelPortaliQ9DAN1.
SMRiQ9DAN1. Positions 30-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60024N.
STRINGi10090.ENSMUSP00000033267.

PTM databases

PhosphoSiteiQ9DAN1.

Proteomic databases

PaxDbiQ9DAN1.
PRIDEiQ9DAN1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033267; ENSMUSP00000033267; ENSMUSG00000030968.
GeneIDi71830.
KEGGimmu:71830.
UCSCiuc009jld.1. mouse.

Organism-specific databases

CTDi204474.
MGIiMGI:1919080. Pdilt.

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000115479.
HOVERGENiHBG108240.
InParanoidiQ9DAN1.
OMAiQKAFLFN.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ9DAN1.
TreeFamiTF106381.

Miscellaneous databases

NextBioi334632.
PROiQ9DAN1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAN1.
CleanExiMM_1700007B13RIK.
GenevestigatoriQ9DAN1.

Family and domain databases

Gene3Di3.40.30.10. 4 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 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.
    , 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.

Entry informationi

Entry nameiPDILT_MOUSE
AccessioniPrimary (citable) accession number: Q9DAN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: February 4, 2015
This is version 102 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.