PDILT_HUMAN
ID PDILT_HUMAN Reviewed; 584 AA.
AC Q8N807; Q8IVQ5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein disulfide-isomerase-like protein of the testis;
DE Flags: Precursor;
GN Name=PDILT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LYS-527 AND GLU-529.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH ERO1A.
RX PubMed=15475357; DOI=10.1074/jbc.m408651200;
RA van Lith M., Hartigan N., Hatch J., Benham A.M.;
RT "PDILT, a divergent testis-specific protein disulfide isomerase with a non-
RT classical SXXC motif that engages in disulfide-dependent interactions in
RT the endoplasmic reticulum.";
RL J. Biol. Chem. 280:1376-1383(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, SUBUNIT, INTERACTION WITH CLGN,
RP AND MUTAGENESIS OF CYS-135 AND CYS-420.
RX PubMed=17507649; DOI=10.1091/mbc.e07-02-0147;
RA van Lith M., Karala A.R., Bown D., Gatehouse J.A., Ruddock L.W.,
RA Saunders P.T.K., Benham A.M.;
RT "A developmentally regulated chaperone complex for the endoplasmic
RT reticulum of male haploid germ cells.";
RL Mol. Biol. Cell 18:2795-2804(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 258-386.
RX PubMed=24662985; DOI=10.1038/srep04464;
RA Bastos-Aristizabal S., Kozlov G., Gehring K.;
RT "Structure of the substrate-binding b' domain of the protein disulfide
RT isomerase-like protein of the testis.";
RL Sci. Rep. 4:4464-4464(2014).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-106.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probable redox-inactive chaperone involved in
CC spermatogenesis. {ECO:0000269|PubMed:17507649}.
CC -!- SUBUNIT: Homodimer. The homodimer is not disulfide-linked. Interacts
CC with ERO1A and CLGN. {ECO:0000269|PubMed:15475357,
CC ECO:0000269|PubMed:17507649}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:15475357}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:15475357,
CC ECO:0000269|PubMed:17507649}.
CC -!- DOMAIN: The thioredoxin domain lacks the conserved redox-active Cys at
CC position 417 which is replaced by a Ser residue, suggesting that it
CC lacks thioredoxin activity.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15475357}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK097476; BAC05068.1; -; mRNA.
DR EMBL; CH471186; EAW50316.1; -; Genomic_DNA.
DR EMBL; BC042607; AAH42607.1; -; mRNA.
DR EMBL; BC044936; AAH44936.1; -; mRNA.
DR CCDS; CCDS10584.1; -.
DR RefSeq; NP_777584.1; NM_174924.1.
DR PDB; 4NWY; X-ray; 2.00 A; A/B/C/D=258-386.
DR PDB; 5XF7; X-ray; 2.38 A; A=21-584.
DR PDBsum; 4NWY; -.
DR PDBsum; 5XF7; -.
DR AlphaFoldDB; Q8N807; -.
DR SMR; Q8N807; -.
DR BioGRID; 128486; 4.
DR STRING; 9606.ENSP00000305465; -.
DR GlyGen; Q8N807; 5 sites.
DR iPTMnet; Q8N807; -.
DR PhosphoSitePlus; Q8N807; -.
DR BioMuta; PDILT; -.
DR DMDM; 172045780; -.
DR jPOST; Q8N807; -.
DR MassIVE; Q8N807; -.
DR PaxDb; Q8N807; -.
DR PeptideAtlas; Q8N807; -.
DR PRIDE; Q8N807; -.
DR ProteomicsDB; 72354; -.
DR Antibodypedia; 52595; 92 antibodies from 18 providers.
DR DNASU; 204474; -.
DR Ensembl; ENST00000302451.9; ENSP00000305465.4; ENSG00000169340.10.
DR GeneID; 204474; -.
DR KEGG; hsa:204474; -.
DR MANE-Select; ENST00000302451.9; ENSP00000305465.4; NM_174924.2; NP_777584.1.
DR UCSC; uc002dhc.2; human.
DR CTD; 204474; -.
DR DisGeNET; 204474; -.
DR GeneCards; PDILT; -.
DR HGNC; HGNC:27338; PDILT.
DR HPA; ENSG00000169340; Tissue enriched (stomach).
DR MIM; 618588; gene.
DR neXtProt; NX_Q8N807; -.
DR OpenTargets; ENSG00000169340; -.
DR PharmGKB; PA164724442; -.
DR VEuPathDB; HostDB:ENSG00000169340; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000160939; -.
DR HOGENOM; CLU_025879_1_1_1; -.
DR InParanoid; Q8N807; -.
DR OMA; RYKMPSD; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q8N807; -.
DR TreeFam; TF106381; -.
DR PathwayCommons; Q8N807; -.
DR SignaLink; Q8N807; -.
DR BioGRID-ORCS; 204474; 7 hits in 1062 CRISPR screens.
DR ChiTaRS; PDILT; human.
DR GenomeRNAi; 204474; -.
DR Pharos; Q8N807; Tdark.
DR PRO; PR:Q8N807; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8N807; protein.
DR Bgee; ENSG00000169340; Expressed in left testis and 32 other tissues.
DR ExpressionAtlas; Q8N807; baseline and differential.
DR Genevisible; Q8N807; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:Ensembl.
DR GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Developmental protein; Differentiation;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Reference proteome; Signal; Spermatogenesis.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..584
FT /note="Protein disulfide-isomerase-like protein of the
FT testis"
FT /id="PRO_0000325849"
FT DOMAIN 388..451
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 581..584
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 26
FT /note="A -> T (in dbSNP:rs9926580)"
FT /id="VAR_039937"
FT VARIANT 106
FT /note="E -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs773495613)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039938"
FT VARIANT 446
FT /note="D -> N (in dbSNP:rs11648131)"
FT /id="VAR_039939"
FT VARIANT 447
FT /note="V -> I (in dbSNP:rs11865916)"
FT /id="VAR_039940"
FT VARIANT 475
FT /note="L -> R (in dbSNP:rs4500734)"
FT /id="VAR_039941"
FT VARIANT 527
FT /note="R -> K (in dbSNP:rs9652589)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039942"
FT VARIANT 529
FT /note="G -> E (in dbSNP:rs9652588)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039943"
FT MUTAGEN 135
FT /note="C->A: Does not affect homodimerization; when
FT associated with A-420."
FT /evidence="ECO:0000269|PubMed:17507649"
FT MUTAGEN 420
FT /note="C->A: Does not affect homodimerization; when
FT associated with A-135."
FT /evidence="ECO:0000269|PubMed:17507649"
FT CONFLICT 561
FT /note="V -> E (in Ref. 1; BAC05068)"
FT /evidence="ECO:0000305"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:5XF7"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:5XF7"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:4NWY"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4NWY"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:4NWY"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:4NWY"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:4NWY"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:4NWY"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:5XF7"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 438..450
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:5XF7"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:5XF7"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:5XF7"
FT HELIX 482..493
FT /evidence="ECO:0007829|PDB:5XF7"
SQ SEQUENCE 584 AA; 66657 MW; 03F7EAD418B3494C CRC64;
MDLLWMPLLL VAACVSAVHS SPEVNAGVSS IHITKPVHIL EERSLLVLTP AGLTQMLNQT
RFLMVLFHNP SSKQSRNLAE ELGKAVEIMG KGKNGIGFGK VDITIEKELQ QEFGITKAPE
LKLFFEGNRS EPISCKGVVE SAALVVWLRR QISQKAFLFN SSEQVAEFVI SRPLVIVGFF
QDLEEEVAEL FYDVIKDFPE LTFGVITIGN VIGRFHVTLD SVLVFKKGKI VNRQKLINDS
TNKQELNRVI KQHLTDFVIE YNTENKDLIS ELHIMSHMLL FVSKSSESYG IIIQHYKLAS
KEFQNKILFI LVDADEPRNG RVFKYFRVTE VDIPSVQILN LSSDARYKMP SDDITYESLK
KFGRSFLSKN ATKHQSSEEI PKYWDQGLVK QLVGKNFNVV VFDKEKDVFV MFYAPWSKKC
KMLFPLLEEL GRKYQNHSTI IIAKIDVTAN DIQLMYLDRY PFFRLFPSGS QQAVLYKGEH
TLKGFSDFLE SHIKTKIEDE DELLSVEQNE VIEEEVLAEE KEVPMMRKGL PEQQSPELEN
MTKYVSKLEE PAGKKKTSEE VVVVVAKPKG PPVQKKKPKV KEEL
