Q8N807 (PDILT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase-like protein of the testis

Gene names

Name:

PDILT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	584 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable redox-inactive chaperone involved in spermatogenesis. Ref.5
Subunit structure	Homodimer. The homodimer is not disulfide-linked. Interacts with ERO1L and CLGN. Ref.4 Ref.5
Subcellular location	Endoplasmic reticulum Ref.4.
Tissue specificity	Testis-specific. Ref.4 Ref.5
Domain	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.
Post-translational modification	N-glycosylated. Ref.4
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Chaperone Developmental protein Isomerase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell redox homeostasis Inferred from electronic annotation. Source: InterPro multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 584	564	Protein disulfide-isomerase-like protein of the testis		PRO_0000325849
Regions
	Domain	388 – 451	64	Thioredoxin
	Motif	581 – 584	4	Prevents secretion from ER Potential
Amino acid modifications
	Glycosylation	58	1	N-linked (GlcNAc...) Potential
	Glycosylation	128	1	N-linked (GlcNAc...) Potential
	Glycosylation	160	1	N-linked (GlcNAc...) Potential
	Glycosylation	340	1	N-linked (GlcNAc...) Potential
	Glycosylation	540	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	26	1	A → T. Corresponds to variant rs9926580 [ dbSNP | Ensembl ].		VAR_039937
	Natural variant	106	1	E → Q in a colorectal cancer sample; somatic mutation. Ref.6		VAR_039938
	Natural variant	446	1	D → N. Corresponds to variant rs11648131 [ dbSNP | Ensembl ].		VAR_039939
	Natural variant	447	1	V → I. Corresponds to variant rs11865916 [ dbSNP | Ensembl ].		VAR_039940
	Natural variant	475	1	L → R. Corresponds to variant rs4500734 [ dbSNP | Ensembl ].		VAR_039941
	Natural variant	527	1	R → K. Ref.1 Corresponds to variant rs9652589 [ dbSNP | Ensembl ].		VAR_039942
	Natural variant	529	1	G → E. Ref.1 Corresponds to variant rs9652588 [ dbSNP | Ensembl ].		VAR_039943
Experimental info
	Mutagenesis	135	1	C → A: Does not affect homodimerization; when associated with A-420. Ref.5
	Mutagenesis	420	1	C → A: Does not affect homodimerization; when associated with A-135. Ref.5
	Sequence conflict	561	1	V → E in BAC05068. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8N807 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: 03F7EAD418B3494C	FASTA	584	66,657
	10 20 30 40 50 60 MDLLWMPLLL VAACVSAVHS SPEVNAGVSS IHITKPVHIL EERSLLVLTP AGLTQMLNQT 70 80 90 100 110 120 RFLMVLFHNP SSKQSRNLAE ELGKAVEIMG KGKNGIGFGK VDITIEKELQ QEFGITKAPE 130 140 150 160 170 180 LKLFFEGNRS EPISCKGVVE SAALVVWLRR QISQKAFLFN SSEQVAEFVI SRPLVIVGFF 190 200 210 220 230 240 QDLEEEVAEL FYDVIKDFPE LTFGVITIGN VIGRFHVTLD SVLVFKKGKI VNRQKLINDS 250 260 270 280 290 300 TNKQELNRVI KQHLTDFVIE YNTENKDLIS ELHIMSHMLL FVSKSSESYG IIIQHYKLAS 310 320 330 340 350 360 KEFQNKILFI LVDADEPRNG RVFKYFRVTE VDIPSVQILN LSSDARYKMP SDDITYESLK 370 380 390 400 410 420 KFGRSFLSKN ATKHQSSEEI PKYWDQGLVK QLVGKNFNVV VFDKEKDVFV MFYAPWSKKC 430 440 450 460 470 480 KMLFPLLEEL GRKYQNHSTI IIAKIDVTAN DIQLMYLDRY PFFRLFPSGS QQAVLYKGEH 490 500 510 520 530 540 TLKGFSDFLE SHIKTKIEDE DELLSVEQNE VIEEEVLAEE KEVPMMRKGL PEQQSPELEN 550 560 570 580 MTKYVSKLEE PAGKKKTSEE VVVVVAKPKG PPVQKKKPKV KEEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-106.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK097476 mRNA. Translation: BAC05068.1. CH471186 Genomic DNA. Translation: EAW50316.1. BC042607 mRNA. Translation: AAH42607.1. BC044936 mRNA. Translation: AAH44936.1.
IPI	IPI00646007.
RefSeq	NP_777584.1. NM_174924.1.
UniGene	Hs.376025.
3D structure databases
HSSP	HSSP built from PDB template 1X5C based on UniProtKB P07237.
ProteinModelPortal	Q8N807.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000305465.
PTM databases
PhosphoSite	Q8N807.
Polymorphism databases
DMDM	172045780.
Proteomic databases
PaxDb	Q8N807.
PRIDE	Q8N807.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302451; ENSP00000305465; ENSG00000169340.
GeneID	204474.
KEGG	hsa:204474.
UCSC	uc002dhc.1. human.
Organism-specific databases
CTD	204474.
GeneCards	GC16M020370.
H-InvDB	HIX0019226.
HGNC	HGNC:27338. PDILT.
HPA	HPA041913.
neXtProt	NX_Q8N807.
PharmGKB	PA164724442.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0526.
HOGENOM	HOG000115479.
HOVERGEN	HBG108240.
InParanoid	Q8N807.
OMA	QKAFLFN.
OrthoDB	EOG4RFKSG.
PhylomeDB	Q8N807.
Gene expression databases
ArrayExpress	Q8N807.
Bgee	Q8N807.
Genevestigator	Q8N807.
Family and domain databases
Gene3D	3.40.30.10. 3 hits.
InterPro	IPR012336. Thioredoxin-like_fold. IPR013766. Thioredoxin_domain. [Graphical view]
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
SUPFAM	SSF52833. Thiordxn-like_fd. 4 hits.
PROSITE	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. False negative. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	204474.
NextBio	90472.

Entry information

Entry name

PDILT_HUMAN

Accession

Primary (citable) accession number: Q8N807
Secondary accession number(s): Q8IVQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.