ID   PDILT_RAT               Reviewed;         590 AA.
AC   Q5XI02;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Protein disulfide-isomerase-like protein of the testis;
DE   Flags: Precursor;
GN   Name=Pdilt;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
CC   -!- FUNCTION: Probable redox-inactive chaperone involved in
CC       spermatogenesis. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. The homodimer is not disulfide-linked. Interacts
CC       with ERO1A and CLGN (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- TISSUE SPECIFICITY: Testis-specific. Expressed exclusively in
CC       postmeiotic male germ cells (at protein level).
CC       {ECO:0000269|PubMed:17507649}.
CC   -!- DEVELOPMENTAL STAGE: Induced during puberty.
CC       {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}.
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DR   EMBL; BC083897; AAH83897.1; -; mRNA.
DR   RefSeq; NP_001013924.1; NM_001013902.1.
DR   AlphaFoldDB; Q5XI02; -.
DR   SMR; Q5XI02; -.
DR   STRING; 10116.ENSRNOP00000020817; -.
DR   GlyCosmos; Q5XI02; 2 sites, No reported glycans.
DR   GlyGen; Q5XI02; 2 sites.
DR   iPTMnet; Q5XI02; -.
DR   PhosphoSitePlus; Q5XI02; -.
DR   jPOST; Q5XI02; -.
DR   PaxDb; 10116-ENSRNOP00000020817; -.
DR   Ensembl; ENSRNOT00000020817.5; ENSRNOP00000020817.4; ENSRNOG00000015368.5.
DR   GeneID; 293544; -.
DR   KEGG; rno:293544; -.
DR   UCSC; RGD:1307822; rat.
DR   AGR; RGD:1307822; -.
DR   CTD; 204474; -.
DR   RGD; 1307822; Pdilt.
DR   eggNOG; KOG0190; Eukaryota.
DR   GeneTree; ENSGT00940000160939; -.
DR   HOGENOM; CLU_025879_1_1_1; -.
DR   InParanoid; Q5XI02; -.
DR   OMA; APWSKKC; -.
DR   OrthoDB; 5399045at2759; -.
DR   PhylomeDB; Q5XI02; -.
DR   TreeFam; TF106381; -.
DR   PRO; PR:Q5XI02; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015368; Expressed in testis and 3 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; ISO:RGD.
DR   GO; GO:0008354; P:germ cell migration; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007286; P:spermatid development; ISO:RGD.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF58; PROTEIN DISULFIDE-ISOMERASE-LIKE PROTEIN OF THE TESTIS; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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..590
FT                   /note="Protein disulfide-isomerase-like protein of the
FT                   testis"
FT                   /id="PRO_0000325852"
FT   DOMAIN          385..448
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          514..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           587..590
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   COMPBIAS        514..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        55
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   590 AA;  68267 MW;  6F73FA1B8CD304DD CRC64;
     MELLWTPLLL LAACLSEVLG SPEMDTGINI SQPLHILEDH NLMVLTPAGL TQTLNETRFL
     MVIFHNPTLK QSRKLAKELG KAAEIFGKGK NGLGFGKVDI TMETELKQEF DITHAPELKL
     FYEGNRLEPI SCKDVVESTA LVVWLRRQIS KKALLFNNSN EVADFVKSRP LVIVGFFQDL
     EEEVAELFYD TIKDFPELTF GAIQIKNSFG RFHVILDSVL VFKKGRVVKR QELINDSTNK
     DYLNQVIKQQ LTGFVIEFNP ENKDLIYEMN ILNHMLLFIS KNSEPYSTII RHYRQISKEF
     QNKILFVLVN SDEPKNKRIF EYFQISRVNV PSVQILNLSS DARYKMPTDN ITFESLKKFC
     NSFLSRTAKK HKSSEEIPKY WDQEPVKKLV GKNFNVVVFD KEKDVFVMFY APWSEKCRVL
     LPLLEELGIK YQNHSTVIIA KIDITANDIQ LANPEQYPFF RLFPTDSQEA VMYKGEHTMK
     GFCDFLESHV KVRIEEDDEL LYIEQNEVAE EEVLAEPEMQ HIDKLPEKPP LKVEDTSKQD
     RPAKESPALG SISQPEELER RKETAEKEKK VAQPKEQPKP ERKLDIKEEL
//