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Q8N807

- PDILT_HUMAN

UniProt

Q8N807 - PDILT_HUMAN

Protein

Protein disulfide-isomerase-like protein of the testis

Gene

PDILT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.1 Publication

    GO - Molecular functioni

    1. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. cell redox homeostasis Source: InterPro
    3. multicellular organismal development Source: UniProtKB-KW
    4. protein folding Source: RefGenome
    5. spermatogenesis Source: UniProtKB-KW

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:27338. PDILT.

    Subcellular locationi

    Endoplasmic reticulum 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: RefGenome

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1351C → A: Does not affect homodimerization; when associated with A-420. 1 Publication
    Mutagenesisi420 – 4201C → A: Does not affect homodimerization; when associated with A-135. 1 Publication

    Organism-specific databases

    PharmGKBiPA164724442.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 584564Protein disulfide-isomerase-like protein of the testisPRO_0000325849Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi540 – 5401N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8N807.
    PRIDEiQ8N807.

    PTM databases

    PhosphoSiteiQ8N807.

    Expressioni

    Tissue specificityi

    Testis-specific.2 Publications

    Gene expression databases

    ArrayExpressiQ8N807.
    BgeeiQ8N807.
    GenevestigatoriQ8N807.

    Organism-specific databases

    HPAiHPA041913.

    Interactioni

    Subunit structurei

    Homodimer. The homodimer is not disulfide-linked. Interacts with ERO1L and CLGN.2 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000305465.

    Structurei

    Secondary structure

    1
    584
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi258 – 2603
    Helixi267 – 2704
    Beta strandi275 – 2828
    Helixi289 – 30012
    Helixi301 – 3033
    Turni304 – 3063
    Beta strandi308 – 3136
    Helixi317 – 3193
    Helixi320 – 3256
    Beta strandi334 – 3407
    Turni341 – 3433
    Beta strandi346 – 3483
    Helixi356 – 36712
    Helixi370 – 3745

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NWYX-ray2.00A/B/C/D258-386[»]
    ProteinModelPortaliQ8N807.
    SMRiQ8N807. Positions 41-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini388 – 45164ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi581 – 5844Prevents secretion from ERPROSITE-ProRule annotation

    Domaini

    The thioredoxin domain lacks the conserved redox-active Cys at position 417 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.
    HOGENOMiHOG000115479.
    HOVERGENiHBG108240.
    InParanoidiQ8N807.
    OMAiQKAFLFN.
    OrthoDBiEOG7VHSX1.
    PhylomeDBiQ8N807.
    TreeFamiTF106381.

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [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.

    Q8N807-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLLWMPLLL VAACVSAVHS SPEVNAGVSS IHITKPVHIL EERSLLVLTP    50
    AGLTQMLNQT RFLMVLFHNP SSKQSRNLAE ELGKAVEIMG KGKNGIGFGK 100
    VDITIEKELQ QEFGITKAPE LKLFFEGNRS EPISCKGVVE SAALVVWLRR 150
    QISQKAFLFN SSEQVAEFVI SRPLVIVGFF QDLEEEVAEL FYDVIKDFPE 200
    LTFGVITIGN VIGRFHVTLD SVLVFKKGKI VNRQKLINDS TNKQELNRVI 250
    KQHLTDFVIE YNTENKDLIS ELHIMSHMLL FVSKSSESYG IIIQHYKLAS 300
    KEFQNKILFI LVDADEPRNG RVFKYFRVTE VDIPSVQILN LSSDARYKMP 350
    SDDITYESLK KFGRSFLSKN ATKHQSSEEI PKYWDQGLVK QLVGKNFNVV 400
    VFDKEKDVFV MFYAPWSKKC KMLFPLLEEL GRKYQNHSTI IIAKIDVTAN 450
    DIQLMYLDRY PFFRLFPSGS QQAVLYKGEH TLKGFSDFLE SHIKTKIEDE 500
    DELLSVEQNE VIEEEVLAEE KEVPMMRKGL PEQQSPELEN MTKYVSKLEE 550
    PAGKKKTSEE VVVVVAKPKG PPVQKKKPKV KEEL 584
    Length:584
    Mass (Da):66,657
    Last modified:March 18, 2008 - v2
    Checksum:i03F7EAD418B3494C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti561 – 5611V → E in BAC05068. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261A → T.
    Corresponds to variant rs9926580 [ dbSNP | Ensembl ].
    VAR_039937
    Natural varianti106 – 1061E → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_039938
    Natural varianti446 – 4461D → N.
    Corresponds to variant rs11648131 [ dbSNP | Ensembl ].
    VAR_039939
    Natural varianti447 – 4471V → I.
    Corresponds to variant rs11865916 [ dbSNP | Ensembl ].
    VAR_039940
    Natural varianti475 – 4751L → R.
    Corresponds to variant rs4500734 [ dbSNP | Ensembl ].
    VAR_039941
    Natural varianti527 – 5271R → K.1 Publication
    Corresponds to variant rs9652589 [ dbSNP | Ensembl ].
    VAR_039942
    Natural varianti529 – 5291G → E.1 Publication
    Corresponds to variant rs9652588 [ dbSNP | Ensembl ].
    VAR_039943

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK097476 mRNA. Translation: BAC05068.1.
    CH471186 Genomic DNA. Translation: EAW50316.1.
    BC042607 mRNA. Translation: AAH42607.1.
    BC044936 mRNA. Translation: AAH44936.1.
    CCDSiCCDS10584.1.
    RefSeqiNP_777584.1. NM_174924.1.
    UniGeneiHs.376025.

    Genome annotation databases

    EnsembliENST00000302451; ENSP00000305465; ENSG00000169340.
    GeneIDi204474.
    KEGGihsa:204474.
    UCSCiuc002dhc.1. human.

    Polymorphism databases

    DMDMi172045780.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK097476 mRNA. Translation: BAC05068.1 .
    CH471186 Genomic DNA. Translation: EAW50316.1 .
    BC042607 mRNA. Translation: AAH42607.1 .
    BC044936 mRNA. Translation: AAH44936.1 .
    CCDSi CCDS10584.1.
    RefSeqi NP_777584.1. NM_174924.1.
    UniGenei Hs.376025.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NWY X-ray 2.00 A/B/C/D 258-386 [» ]
    ProteinModelPortali Q8N807.
    SMRi Q8N807. Positions 41-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000305465.

    PTM databases

    PhosphoSitei Q8N807.

    Polymorphism databases

    DMDMi 172045780.

    Proteomic databases

    PaxDbi Q8N807.
    PRIDEi Q8N807.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302451 ; ENSP00000305465 ; ENSG00000169340 .
    GeneIDi 204474.
    KEGGi hsa:204474.
    UCSCi uc002dhc.1. human.

    Organism-specific databases

    CTDi 204474.
    GeneCardsi GC16M020370.
    H-InvDB HIX0019226.
    HGNCi HGNC:27338. PDILT.
    HPAi HPA041913.
    neXtProti NX_Q8N807.
    PharmGKBi PA164724442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000115479.
    HOVERGENi HBG108240.
    InParanoidi Q8N807.
    OMAi QKAFLFN.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi Q8N807.
    TreeFami TF106381.

    Miscellaneous databases

    GenomeRNAii 204474.
    NextBioi 90472.
    PROi Q8N807.

    Gene expression databases

    ArrayExpressi Q8N807.
    Bgeei Q8N807.
    Genevestigatori Q8N807.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LYS-527 AND GLU-529.
      Tissue: Testis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Brain.
    4. "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: SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, INTERACTION WITH ERO1L.
    5. "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: FUNCTION, TISSUE SPECIFICITY, INDUCTION, SUBUNIT, INTERACTION WITH CLGN, MUTAGENESIS OF CYS-135 AND CYS-420.
    6. "Structure of the substrate-binding b' domain of the protein disulfide isomerase-like protein of the testis."
      Bastos-Aristizabal S., Kozlov G., Gehring K.
      Sci. Rep. 4:4464-4464(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 258-386.
    7. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-106.

    Entry informationi

    Entry nameiPDILT_HUMAN
    AccessioniPrimary (citable) accession number: Q8N807
    Secondary accession number(s): Q8IVQ5
    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
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3