Full text data of ZZZZ
Q6ZR44
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00472175
IPI00472175 Thioredoxin reductase 1, cytoplasmic thioredoxin-disulfide reductase activity, signal transduction soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00472175 Thioredoxin reductase 1, cytoplasmic thioredoxin-disulfide reductase activity, signal transduction soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q6ZR44
ID Q6ZR44_HUMAN Unreviewed; 581 AA.
AC Q6ZR44;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
read moreDT 22-JAN-2014, entry version 73.
DE SubName: Full=cDNA FLJ46672 fis, clone TRACH3009008, highly similar to Thioredoxin reductase (EC 1.6.4.5);
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Trachea;
RA Ninomiya K., Wagatsuma M., Kanda K., Kondo H., Yokoi T., Kodaira H.,
RA Furuya T., Takahashi M., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Sugiyama T., Irie R.,
RA Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J.,
RA Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K.,
RA Yamashita H., Matsuo K., Nakamura Y., Sekine M., Kikuchi H.,
RA Murakawa K., Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A.,
RA Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K.,
RA Isogai T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK128515; BAC87474.1; -; mRNA.
DR UniGene; Hs.654922; -.
DR ProteinModelPortal; Q6ZR44; -.
DR SMR; Q6ZR44; 50-579.
DR MINT; MINT-1422693; -.
DR PRIDE; Q6ZR44; -.
DR HOGENOM; HOG000276712; -.
DR HOVERGEN; HBG004959; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR PANTHER; PTHR22912:SF23; PTHR22912:SF23; 1.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Oxidoreductase; Redox-active center.
SQ SEQUENCE 581 AA; 63965 MW; 84EF4E9B6CE371B2 CRC64;
MQQVMLTCKG VNRGHAVPAG PGRKPRPRRS SRLLAGEKHL TRSALLLCHT EDGRALEGTL
SELAAETDLP VVFVKQRKIG GHGPTLKAYQ EGRLQKLLKM NGPEDLPKSY DYDLIIIGGG
SGGLAAAKEA AQYGKKVMVL VFVTPTPLGT RWGLGGTCVN VGCIPKKLMH QAALLGQALQ
DSRNYGWKVE ETVKHDWDRM IEAVQNHIGS LNWGYRVALR EKKVVYENAY GQFIGPHRIK
ATNNKGKEKI YSAERFLIAT GERPRYLGIP GDKEYCISSD DLFSLPYCPG KTLVVGASYV
ALECAGFLAG IGLDVTVMVR SILLRGFDQD MANKIGEHME EHGIKFIRQF VPIKVEQIEA
GTPGRLRVVA QSTNSEEIIE GEYNTVMLAI GRDACTRKIG LETVGVKINE KTGKIPVTDE
EQTNVPYIYA IGDILEDKVE LTPVAIQAGR LLAQRLYAGS TVKCDYENVP TTVFTPLEYG
ACGLSEEKAV EKFGEENIEV YHSYFWPLEW TIPSRDNNKC YAKIICNTKD NERVVGFHVL
GPNAGEVTQG FAAALKCGLT KKQLDSTIGI HPVCAEFFSF I
//
ID Q6ZR44_HUMAN Unreviewed; 581 AA.
AC Q6ZR44;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
read moreDT 22-JAN-2014, entry version 73.
DE SubName: Full=cDNA FLJ46672 fis, clone TRACH3009008, highly similar to Thioredoxin reductase (EC 1.6.4.5);
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Trachea;
RA Ninomiya K., Wagatsuma M., Kanda K., Kondo H., Yokoi T., Kodaira H.,
RA Furuya T., Takahashi M., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Sugiyama T., Irie R.,
RA Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J.,
RA Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K.,
RA Yamashita H., Matsuo K., Nakamura Y., Sekine M., Kikuchi H.,
RA Murakawa K., Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A.,
RA Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K.,
RA Isogai T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK128515; BAC87474.1; -; mRNA.
DR UniGene; Hs.654922; -.
DR ProteinModelPortal; Q6ZR44; -.
DR SMR; Q6ZR44; 50-579.
DR MINT; MINT-1422693; -.
DR PRIDE; Q6ZR44; -.
DR HOGENOM; HOG000276712; -.
DR HOVERGEN; HBG004959; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR PANTHER; PTHR22912:SF23; PTHR22912:SF23; 1.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Oxidoreductase; Redox-active center.
SQ SEQUENCE 581 AA; 63965 MW; 84EF4E9B6CE371B2 CRC64;
MQQVMLTCKG VNRGHAVPAG PGRKPRPRRS SRLLAGEKHL TRSALLLCHT EDGRALEGTL
SELAAETDLP VVFVKQRKIG GHGPTLKAYQ EGRLQKLLKM NGPEDLPKSY DYDLIIIGGG
SGGLAAAKEA AQYGKKVMVL VFVTPTPLGT RWGLGGTCVN VGCIPKKLMH QAALLGQALQ
DSRNYGWKVE ETVKHDWDRM IEAVQNHIGS LNWGYRVALR EKKVVYENAY GQFIGPHRIK
ATNNKGKEKI YSAERFLIAT GERPRYLGIP GDKEYCISSD DLFSLPYCPG KTLVVGASYV
ALECAGFLAG IGLDVTVMVR SILLRGFDQD MANKIGEHME EHGIKFIRQF VPIKVEQIEA
GTPGRLRVVA QSTNSEEIIE GEYNTVMLAI GRDACTRKIG LETVGVKINE KTGKIPVTDE
EQTNVPYIYA IGDILEDKVE LTPVAIQAGR LLAQRLYAGS TVKCDYENVP TTVFTPLEYG
ACGLSEEKAV EKFGEENIEV YHSYFWPLEW TIPSRDNNKC YAKIICNTKD NERVVGFHVL
GPNAGEVTQG FAAALKCGLT KKQLDSTIGI HPVCAEFFSF I
//