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Database: UniProt
Entry: H2QZP4_PANTR
LinkDB: H2QZP4_PANTR
Original site: H2QZP4_PANTR 
ID   H2QZP4_PANTR            Unreviewed;       432 AA.
AC   H2QZP4; K7AS92;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN   Name=TXNDC5 {ECO:0000313|EMBL:JAA20826.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000039310.5,
GN   ECO:0000313|VGNC:VGNC:13043};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000039310.5, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000039310.5, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA20826.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Smooth vascular {ECO:0000313|EMBL:JAA20826.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000039310.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000256|ARBA:ARBA00004319}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR   EMBL; AACZ04065936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABF01001319; JAA20826.1; -; mRNA.
DR   RefSeq; XP_016810363.1; XM_016954874.1.
DR   PaxDb; 9598-ENSPTRP00000039310; -.
DR   Ensembl; ENSPTRT00000032719.5; ENSPTRP00000039310.5; ENSPTRG00000017708.6.
DR   GeneID; 100615889; -.
DR   KEGG; ptr:100615889; -.
DR   CTD; 81567; -.
DR   VGNC; VGNC:13043; TXNDC5.
DR   eggNOG; KOG0191; Eukaryota.
DR   GeneTree; ENSGT00940000156920; -.
DR   HOGENOM; CLU_066321_0_0_1; -.
DR   OrthoDB; 52245at2759; -.
DR   TreeFam; TF106379; -.
DR   Proteomes; UP000002277; Chromosome 6.
DR   Bgee; ENSPTRG00000017708; Expressed in fibroblast and 20 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03005; PDI_a_ERp46; 3.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01126; pdi_dom; 1.
DR   PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR   PANTHER; PTHR45672:SF3; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 5; 1.
DR   Pfam; PF00085; Thioredoxin; 3.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 3.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..432
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014304835"
FT   DOMAIN          36..169
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          170..295
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          304..429
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          40..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  47557 MW;  A1592146396431B1 CRC64;
     MPARPGRLLP LLARPSALTA LLLLLLGHGG GGRWGARAQE AAAAAADGPP AADGEDGQDP
     HSKHLYTADM FTHGIQSAAH FVMFFAPWCG HCQRLQPTWN DLGDKYNSME DAKVYVAKVD
     CTAHSDVCSA QGVRGYPTLK LFKPGQEAVK YQGPRDFQTL ENWMLQTLNE EPVTPEPEVE
     PPSAPELKQG LYELSASNFE LHVAQGDHFI KFFAPWCGHC KALAPTWEQL ALGLEHSETV
     KIGKVDCTQH YELCSGNQVR GYPTLLWFRD GKKVDQYKGK RDLESLREYV ESQLQRTATG
     ATETVTPSEA PVLAAEPEAD KGTVLALTEN NFDDTIAEGI TFIKFYAPWC GHCKTLAPTW
     EELSKKEFPG LAGVKIAEVD CTAERNICSK YSVRGYPTLL LFRGGKKVSE HSGGRDLDSL
     HRFVLGQAKD EL
//
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