PDILT_MACFA
ID PDILT_MACFA Reviewed; 583 AA.
AC Q95LM0; Q95LX8; Q95LZ9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Protein disulfide-isomerase-like protein of the testis;
DE Flags: Precursor;
GN Name=PDILT; ORFNames=QtsA-10382, QtsA-15920, QtsA-20110;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Testis;
RA Hashimoto K., Osada N., Hida M., Kusuda J., Tanuma R., Hirai M., Terao K.,
RA Sugano S.;
RT "Isolation of novel full-length cDNA clones from macaque testis cDNA
RT libraries.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q95LM0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95LM0-2; Sequence=VSP_032448;
CC Name=3;
CC IsoId=Q95LM0-3; Sequence=VSP_032447;
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:0000250}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; AB071042; BAB64435.1; -; mRNA.
DR EMBL; AB071063; BAB64456.1; -; mRNA.
DR EMBL; AB072768; BAB69737.1; -; mRNA.
DR AlphaFoldDB; Q95LM0; -.
DR SMR; Q95LM0; -.
DR STRING; 9541.XP_005591450.1; -.
DR PRIDE; Q95LM0; -.
DR eggNOG; KOG0191; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative splicing; Chaperone; Developmental protein; Differentiation;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Reference proteome; Signal; Spermatogenesis.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..583
FT /note="Protein disulfide-isomerase-like protein of the
FT testis"
FT /id="PRO_0000325850"
FT DOMAIN 388..451
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 522..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 580..583
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 542..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032447"
FT VAR_SEQ 527..553
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032448"
FT CONFLICT 375
FT /note="Q -> R (in Ref. 2; BAB64435)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="E -> G (in Ref. 2; BAB64435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 66848 MW; CAC54CF9A5F6369C CRC64;
MDLLWMPLLL VAARISAVHS SPEVNAGVSS IHITKPVHIL EERNLLVLTP AGLTQMLNQT
RFLMVLFHNP SSKQSRNLAE ELGKAVEIMG KGKNGIGFGK VDITVEKELQ QEFGITKAPQ
LKLFFEGNRS EPISCKGVVE STALVVWLRR QISQKAFLFN SSLQVAEFVT SRPLVIVGFF
QDLEEEVAEL FYDVIKDFPE LTFGVITIGN AIGRFHVTLD SILVFKKGKI VNRQELINDS
TNKQELNRVI KQHLTDFVIE YNAENKDLIY ELYIMSHMLL FVSKSSESFG IIIQHYKLAS
KEFQNKILFI LVNADEPRNR RVIEYFRVTE VDIPSVQILN LSSDARYKMP SDDITYENLK
KFGRSFLSKN AKKHQSSEEI PKHWDQGLVK QLVGKNFNIV VFDKEKDVFV MFYAPWSKKC
KMLFPLLEEL GRKYQNHSTI IIAKIDITAN DIQLVYLDRY PFFRLFPTDS QQAVLYKGEH
TLKGFSDFLE SYIKTSIEDE DELLSVEQNE VIEEEVRAKE KEVPMMKKEL PEQQSPELEN
VTKHVSKLEE SAGKKKTSEE VVVVAKPKGP PTQKKKPKVK EEL
