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Protein

Protein disulfide-isomerase-like protein of the testis

Gene

PDILT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable redox-inactive chaperone involved in spermatogenesis.1 Publication

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

Organism-specific databases

HGNCiHGNC:27338. PDILT.

Subcellular locationi

  1. Endoplasmic reticulum PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

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

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.

Polymorphism and mutation databases

BioMutaiPDILT.
DMDMi172045780.

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

BgeeiQ8N807.
ExpressionAtlasiQ8N807. baseline.
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 – 2603Combined sources
Helixi267 – 2704Combined sources
Beta strandi275 – 2828Combined sources
Helixi289 – 30012Combined sources
Helixi301 – 3033Combined sources
Turni304 – 3063Combined sources
Beta strandi308 – 3136Combined sources
Helixi317 – 3193Combined sources
Helixi320 – 3256Combined sources
Beta strandi334 – 3407Combined sources
Turni341 – 3433Combined sources
Beta strandi346 – 3483Combined sources
Helixi356 – 36712Combined sources
Helixi370 – 3745Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119201.
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

        10         20         30         40         50
MDLLWMPLLL VAACVSAVHS SPEVNAGVSS IHITKPVHIL EERSLLVLTP
60 70 80 90 100
AGLTQMLNQT RFLMVLFHNP SSKQSRNLAE ELGKAVEIMG KGKNGIGFGK
110 120 130 140 150
VDITIEKELQ QEFGITKAPE LKLFFEGNRS EPISCKGVVE SAALVVWLRR
160 170 180 190 200
QISQKAFLFN SSEQVAEFVI SRPLVIVGFF QDLEEEVAEL FYDVIKDFPE
210 220 230 240 250
LTFGVITIGN VIGRFHVTLD SVLVFKKGKI VNRQKLINDS TNKQELNRVI
260 270 280 290 300
KQHLTDFVIE YNTENKDLIS ELHIMSHMLL FVSKSSESYG IIIQHYKLAS
310 320 330 340 350
KEFQNKILFI LVDADEPRNG RVFKYFRVTE VDIPSVQILN LSSDARYKMP
360 370 380 390 400
SDDITYESLK KFGRSFLSKN ATKHQSSEEI PKYWDQGLVK QLVGKNFNVV
410 420 430 440 450
VFDKEKDVFV MFYAPWSKKC KMLFPLLEEL GRKYQNHSTI IIAKIDVTAN
460 470 480 490 500
DIQLMYLDRY PFFRLFPSGS QQAVLYKGEH TLKGFSDFLE SHIKTKIEDE
510 520 530 540 550
DELLSVEQNE VIEEEVLAEE KEVPMMRKGL PEQQSPELEN MTKYVSKLEE
560 570 580
PAGKKKTSEE VVVVVAKPKG PPVQKKKPKV KEEL
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiPDILT.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi9606.ENSP00000305465.

PTM databases

PhosphoSiteiQ8N807.

Polymorphism and mutation databases

BioMutaiPDILT.
DMDMi172045780.

Proteomic databases

PaxDbiQ8N807.
PRIDEiQ8N807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi204474.
GeneCardsiGC16M020370.
H-InvDBHIX0019226.
HGNCiHGNC:27338. PDILT.
HPAiHPA041913.
neXtProtiNX_Q8N807.
PharmGKBiPA164724442.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000115479.
HOVERGENiHBG108240.
InParanoidiQ8N807.
OMAiQKAFLFN.
OrthoDBiEOG7VHSX1.
PhylomeDBiQ8N807.
TreeFamiTF106381.

Miscellaneous databases

ChiTaRSiPDILT. human.
GenomeRNAii204474.
NextBioi90472.
PROiQ8N807.

Gene expression databases

BgeeiQ8N807.
ExpressionAtlasiQ8N807. baseline.
GenevestigatoriQ8N807.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 104 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

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.