PDILT_MOUSE
ID PDILT_MOUSE Reviewed; 588 AA.
AC Q9DAN1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein disulfide-isomerase-like protein of the testis;
DE Flags: Precursor;
GN Name=Pdilt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP TISSUE SPECIFICITY.
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 [3]
RP TISSUE SPECIFICITY.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable redox-inactive chaperone involved in
CC spermatogenesis. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. The homodimer is not disulfide-linked. Interacts
CC with CLGN and ERO1A (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9DAN1; Q62287: Adam3; NbExp=2; IntAct=EBI-15971896, EBI-15971963;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- TISSUE SPECIFICITY: Testis-specific (at protein level).
CC {ECO:0000269|PubMed:15475357, ECO:0000269|PubMed:17507649}.
CC -!- DOMAIN: The thioredoxin domain lacks the conserved redox-active Cys at
CC position 414 which is replaced by a Ser residue, suggesting that it
CC lacks thioredoxin activity.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK005692; BAB24190.1; ALT_INIT; mRNA.
DR CCDS; CCDS52378.1; -.
DR RefSeq; NP_082219.1; NM_027943.1.
DR RefSeq; XP_006508276.2; XM_006508213.3.
DR RefSeq; XP_006508277.1; XM_006508214.1.
DR AlphaFoldDB; Q9DAN1; -.
DR SMR; Q9DAN1; -.
DR DIP; DIP-60024N; -.
DR IntAct; Q9DAN1; 3.
DR STRING; 10090.ENSMUSP00000033267; -.
DR GlyGen; Q9DAN1; 3 sites.
DR PhosphoSitePlus; Q9DAN1; -.
DR PaxDb; Q9DAN1; -.
DR PeptideAtlas; Q9DAN1; -.
DR PRIDE; Q9DAN1; -.
DR ProteomicsDB; 288021; -.
DR Antibodypedia; 52595; 92 antibodies from 18 providers.
DR Ensembl; ENSMUST00000033267; ENSMUSP00000033267; ENSMUSG00000030968.
DR GeneID; 71830; -.
DR KEGG; mmu:71830; -.
DR UCSC; uc009jld.1; mouse.
DR CTD; 204474; -.
DR MGI; MGI:1919080; Pdilt.
DR VEuPathDB; HostDB:ENSMUSG00000030968; -.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00940000160939; -.
DR HOGENOM; CLU_025879_1_1_1; -.
DR InParanoid; Q9DAN1; -.
DR OMA; RYKMPSD; -.
DR OrthoDB; 462118at2759; -.
DR PhylomeDB; Q9DAN1; -.
DR TreeFam; TF106381; -.
DR BioGRID-ORCS; 71830; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Pdilt; mouse.
DR PRO; PR:Q9DAN1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DAN1; protein.
DR Bgee; ENSMUSG00000030968; Expressed in spermatid and 88 other tissues.
DR ExpressionAtlas; Q9DAN1; baseline and differential.
DR Genevisible; Q9DAN1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IMP:MGI.
DR GO; GO:0008354; P:germ cell migration; IMP:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 4.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Developmental protein; Differentiation; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Isomerase; Reference proteome; Signal;
KW Spermatogenesis.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..588
FT /note="Protein disulfide-isomerase-like protein of the
FT testis"
FT /id="PRO_0000325851"
FT DOMAIN 385..448
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 531..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 585..588
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 588 AA; 67759 MW; 1B0A73E5DBDF6187 CRC64;
MELLWTPLLL VAACLSEVLG SPEIDTGINI SQPLHILEDH NLMVLTPAGL TQTLNETRFL
MVIFHNPSLK QSRKLAKELG KAAEIFGKGK NGLGFGKVDI TKETELQQEF DITHAPELKL
FFEGNRLKPI SCKDVVESTA LVVWLRRQIS KKALLFNNSD EVADFVKSRP LVIVGFFQDL
EEEVAELFYD TIKDFPELTF GAIQIKNSFG RFHVILDSVL VFKKGKIVKR QELINDSTNK
DHLNQVIKQQ LTGFVIELNP ENKDLIYELN ILNHMLLFIS KSSEPYSTIS RHYRQIAKEF
QNKILFVLVN ADEPKNKRIF EYFQISRVNV PSVQILNLSS DGRYKMPTDD INFESLKKFC
NSFLSKTAKK HKASEEIPKY WDQGPVKKLV GKNFNVVVLD KEKDVFVMFY APWSEKCRVL
LPLLEELGIK YQNHSTVIIA KIDITANDIQ LANPEQYPFF RLFPTDSQEA VMYKGEHTMK
GFCDFLESHV KVRIEEEDEL LYIEQNEEEE VLAEPEIQLI EKLPENPLLK IEDTSKQDRP
VKESPVLDSI RKPEEPERRK ETAEREAAAA QPKEQPKPER KLEVKEEL
