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Database: UniProt
Entry: H7BZ94_HUMAN
LinkDB: H7BZ94_HUMAN
Original site: H7BZ94_HUMAN 
ID   H7BZ94_HUMAN            Unreviewed;       464 AA.
AC   H7BZ94;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN   Name=P4HB {ECO:0000313|Ensembl:ENSP00000388374.2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000388374.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000388374.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [2] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [3] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [4] {ECO:0007829|PubMed:25944712}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [5] {ECO:0000313|Ensembl:ENSP00000388374.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}. Melanosome
CC       {ECO:0000256|ARBA:ARBA00004223}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR   EMBL; AC145207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC174470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H7BZ94; -.
DR   SMR; H7BZ94; -.
DR   EPD; H7BZ94; -.
DR   MassIVE; H7BZ94; -.
DR   MaxQB; H7BZ94; -.
DR   PeptideAtlas; H7BZ94; -.
DR   ProteomicsDB; 43877; -.
DR   Antibodypedia; 3250; 639 antibodies from 43 providers.
DR   Ensembl; ENST00000439918.7; ENSP00000388374.2; ENSG00000185624.16.
DR   UCSC; uc060loc.1; human.
DR   HGNC; HGNC:8548; P4HB.
DR   VEuPathDB; HostDB:ENSG00000185624; -.
DR   GeneTree; ENSGT00940000157351; -.
DR   HOGENOM; CLU_025879_1_0_1; -.
DR   ChiTaRS; P4HB; human.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000185624; Expressed in stromal cell of endometrium and 207 other cell types or tissues.
DR   ExpressionAtlas; H7BZ94; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
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; 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; 2.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF101; PROTEIN DISULFIDE-ISOMERASE; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Proteomics identification {ECO:0007829|EPD:H7BZ94,
KW   ECO:0007829|MaxQB:H7BZ94};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..464
FT                   /note="protein disulfide-isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003608316"
FT   DOMAIN          8..190
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          305..431
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          427..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..464
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  52502 MW;  5A9AD45C0CA46796 CRC64;
     MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA
     PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP TIKFFRNGDT ASPKEYTGDV
     ESDSAKQFLQ AAEAIDDIPF GITSNSDVFS KYQLDKDGVV LFKKFDEGRN NFEGEVTKEN
     LLDFIKHNQL PLVIEFTEQT APKIFGGEIK THILLFLPKS VSDYDGKLSN FKTAAESFKG
     KILFIFIDSD HTDNQRILEF FGLKKEECPA VRLITLEEEM TKYKPESEEL TAERITEFCH
     RFLEGKIKPH LMSQELPEDW DKQPVKVLVG KNFEDVAFDE KKNVFVEFYA PWCGHCKQLA
     PIWDKLGETY KDHENIVIAK MDSTANEVEA VKVHSFPTLK FFPASADRTV IDYNGERTLD
     GFKKFLESGG QDGAGDDDDL EDLEEAEEPD MEEDDDQKAV KDEL
//
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