F5H780 (F5H780_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Thioredoxin reductase 1, cytoplasmic Ensembl ENSP00000442709

Gene names

Name:

TXNRD1 Ensembl ENSP00000442709

Organism

Homo sapiens (Human) [Reference proteome] Ensembl ENSP00000442709

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	459 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. RuleBase RU003691
Caution	The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000442709

Ontologies

Keywords
Domain	Redox-active center RuleBase RU003691
Ligand	FAD RuleBase RU003691 Flavoprotein RuleBase RU003691
Molecular function	Oxidoreductase RuleBase RU003691
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from electronic annotation. Source: Compara benzene-containing compound metabolic process Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to copper ion Inferred from electronic annotation. Source: Compara cellular response to hyperoxia Inferred from electronic annotation. Source: Compara glutathione metabolic process Inferred from electronic annotation. Source: Compara halogen metabolic process Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from electronic annotation. Source: Compara mesoderm formation Inferred from electronic annotation. Source: Compara methylmercury metabolic process Inferred from electronic annotation. Source: Compara placenta development Inferred from electronic annotation. Source: Compara positive regulation of cell death Inferred from electronic annotation. Source: Compara protein tetramerization Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to selenium ion Inferred from electronic annotation. Source: Compara selenocysteine metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	NAD(P)H oxidase activity Inferred from electronic annotation. Source: Compara NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro mercury ion binding Inferred from electronic annotation. Source: Compara selenate reductase activity Inferred from electronic annotation. Source: Compara thioredoxin-disulfide reductase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	F5H780 [UniParc]. Last modified June 28, 2011. Version 1. Checksum: 9620A6BD82EA428C	FASTA	459	50,666
	10 20 30 40 50 60 MVLDFVTPTP LGTRWGLGGT CVNVGCIPKK LMHQAALLGQ ALQDSRNYGW KVEETVKHDW 70 80 90 100 110 120 DRMIEAVQNH IGSLNWGYRV ALREKKVVYE NAYGQFIGPH RIKATNNKGK EKIYSAERFL 130 140 150 160 170 180 IATGERPRYL GIPGDKEYCI SSDDLFSLPY CPGKTLVVGA SYVALECAGF LAGIGLDVTV 190 200 210 220 230 240 MVRSILLRGF DQDMANKIGE HMEEHGIKFI RQFVPIKVEQ IEAGTPGRLR VVAQSTNSEE 250 260 270 280 290 300 IIEGEYNTVM LAIGRDACTR KIGLETVGVK INEKTGKIPV TDEEQTNVPY IYAIGDILED 310 320 330 340 350 360 KVELTPVAIQ AGRLLAQRLY AGSTVKCDYE NVPTTVFTPL EYGACGLSEE KAVEKFGEEN 370 380 390 400 410 420 IEVYHSYFWP LEWTIPSRDN NKCYAKIICN TKDNERVVGF HVLGPNAGEV TQGFAAALKC 430 440 450 GLTKKQLDST IGIHPVCAEV FTTLSVTKRS GASILQAGC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The finished DNA sequence of human chromosome 12." Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A., null. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Ensembl Submitted (JUL-2011) to UniProtKB Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC089983 Genomic DNA. No translation available. AC090107 Genomic DNA. No translation available.
IPI	IPI00977771.
3D structure databases
ProteinModelPortal	F5H780.
SMR	F5H780. Positions 1-458.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000540716; ENSP00000442709; ENSG00000198431.
Organism-specific databases
HGNC	HGNC:12437. TXNRD1.
GenAtlas	Search...
Gene expression databases
ArrayExpress	F5H780.
Bgee	F5H780.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR006338. Thioredoxin/glutathione_Rdtase. [Graphical view]
PANTHER	PTHR22912:SF23. PTHR22912:SF23. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TXNRD1. human.
NextBio	35509326.

Entry information

Entry name

F5H780_HUMAN

Accession

Primary (citable) accession number: F5H780

Entry history

Integrated into UniProtKB/TrEMBL:	June 28, 2011
Last sequence update:	June 28, 2011
Last modified:	April 3, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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.