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Q9DAN1

- PDILT_MOUSE

UniProt

Q9DAN1 - PDILT_MOUSE

Protein

Protein disulfide-isomerase-like protein of the testis

Gene

Pdilt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (18 Mar 2008)
      Previous versions | rss
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    Functioni

    Probable redox-inactive chaperone involved in spermatogenesis.By similarity

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. 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

    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: RefGenome

    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.
    GeneTreeiENSGT00740000115202.
    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

    MELLWTPLLL VAACLSEVLG SPEIDTGINI SQPLHILEDH NLMVLTPAGL    50
    TQTLNETRFL MVIFHNPSLK QSRKLAKELG KAAEIFGKGK NGLGFGKVDI 100
    TKETELQQEF DITHAPELKL FFEGNRLKPI SCKDVVESTA LVVWLRRQIS 150
    KKALLFNNSD EVADFVKSRP LVIVGFFQDL EEEVAELFYD TIKDFPELTF 200
    GAIQIKNSFG RFHVILDSVL VFKKGKIVKR QELINDSTNK DHLNQVIKQQ 250
    LTGFVIELNP ENKDLIYELN ILNHMLLFIS KSSEPYSTIS RHYRQIAKEF 300
    QNKILFVLVN ADEPKNKRIF EYFQISRVNV PSVQILNLSS DGRYKMPTDD 350
    INFESLKKFC NSFLSKTAKK HKASEEIPKY WDQGPVKKLV GKNFNVVVLD 400
    KEKDVFVMFY APWSEKCRVL LPLLEELGIK YQNHSTVIIA KIDITANDIQ 450
    LANPEQYPFF RLFPTDSQEA VMYKGEHTMK GFCDFLESHV KVRIEEEDEL 500
    LYIEQNEEEE VLAEPEIQLI EKLPENPLLK IEDTSKQDRP VKESPVLDSI 550
    RKPEEPERRK ETAEREAAAA QPKEQPKPER KLEVKEEL 588
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK005692 mRNA. Translation: BAB24190.1 . Different initiation.
    CCDSi CCDS52378.1.
    RefSeqi NP_082219.1. NM_027943.1.
    XP_006508277.1. XM_006508214.1.
    UniGenei Mm.84631.

    3D structure databases

    ProteinModelPortali Q9DAN1.
    SMRi Q9DAN1. Positions 30-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60024N.
    STRINGi 10090.ENSMUSP00000033267.

    PTM databases

    PhosphoSitei Q9DAN1.

    Proteomic databases

    PaxDbi Q9DAN1.
    PRIDEi Q9DAN1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033267 ; ENSMUSP00000033267 ; ENSMUSG00000030968 .
    GeneIDi 71830.
    KEGGi mmu:71830.
    UCSCi uc009jld.1. mouse.

    Organism-specific databases

    CTDi 204474.
    MGIi MGI:1919080. Pdilt.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00740000115202.
    HOGENOMi HOG000115479.
    HOVERGENi HBG108240.
    InParanoidi Q9DAN1.
    OMAi QKAFLFN.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi Q9DAN1.
    TreeFami TF106381.

    Miscellaneous databases

    NextBioi 334632.
    PROi Q9DAN1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DAN1.
    CleanExi MM_1700007B13RIK.
    Genevestigatori Q9DAN1.

    Family and domain databases

    Gene3Di 3.40.30.10. 4 hits.
    InterProi IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 99 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