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Q6PKC3

- TXD11_HUMAN

UniProt

Q6PKC3 - TXD11_HUMAN

Protein

Thioredoxin domain-containing protein 11

Gene

TXNDC11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H2O2 generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H2O2 generation.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. protein folding Source: RefGenome
    3. response to endoplasmic reticulum stress Source: RefGenome

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin domain-containing protein 11
    Alternative name(s):
    EF-hand-binding protein 1
    Gene namesi
    Name:TXNDC11
    Synonyms:EFP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:28030. TXNDC11.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: RefGenome
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134915251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 985985Thioredoxin domain-containing protein 11PRO_0000120173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi469 ↔ 472Redox-activePROSITE-ProRule annotation
    Disulfide bondi719 ↔ 722Redox-activePROSITE-ProRule annotation
    Modified residuei828 – 8281Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ6PKC3.
    PaxDbiQ6PKC3.
    PRIDEiQ6PKC3.

    PTM databases

    PhosphoSiteiQ6PKC3.

    Expressioni

    Tissue specificityi

    Widely expressed at low level. Expressed at higher level in thyroid and prostate.1 Publication

    Gene expression databases

    ArrayExpressiQ6PKC3.
    BgeeiQ6PKC3.
    CleanExiHS_TXNDC11.
    GenevestigatoriQ6PKC3.

    Organism-specific databases

    HPAiHPA041174.
    HPA041390.

    Interactioni

    Subunit structurei

    Interacts with the cytoplasmic part of DUOX1 and DUOX2. Interacts with TPO and CYBA.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-749812,EBI-6863748From a different organism.

    Protein-protein interaction databases

    BioGridi119253. 18 interactions.
    IntActiQ6PKC3. 43 interactions.
    MINTiMINT-2872884.
    STRINGi9606.ENSP00000283033.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PKC3.
    SMRiQ6PKC3. Positions 127-245, 569-827.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei65 – 8521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 214123Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini649 – 799151Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili821 – 91999Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 2 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Redox-active center, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000132983.
    HOVERGENiHBG082866.
    InParanoidiQ6PKC3.
    OMAiNFSVLYS.
    OrthoDBiEOG7ZSHSG.
    PhylomeDBiQ6PKC3.
    TreeFamiTF323602.

    Family and domain databases

    Gene3Di3.40.30.10. 2 hits.
    InterProiIPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 2 hits.
    PROSITEiPS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6PKC3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSECGGRGGG SSSSEDAEDE GGGGGGPAGS DCLSSSPTLA TASSAGRLRR    50
    GLRGAFLMAR QRPELLCGAV ALGCALLLAL KFTCSRAKDV IIPAKPPVSF 100
    FSLRSPVLDL FQGQLDYAEY VRRDSEVVLL FFYAPWCGQS IAARAEIEQA 150
    ASRLSDQVLF VAINCWWNQG KCRKQKHFFY FPVIYLYHRS FGPIEYKGPM 200
    SAVYIEKFVR RVMKPLLYIP SQSELLDFLS NYEPGVLGYF EFSGSPQPPG 250
    YLTFFTSALH SLKKALESTS SPRALVSFTG EWHLETKIYV LDYLGTVRFG 300
    VITNKHLAKL VSLVHSGSVY LHRHFNTSLV FPREVLNYTA ENICKWALEN 350
    QETLFRWLRP HGGKSLLLNN ELKKGPALFL FIPFNPLAES HPLIDEITEV 400
    ALEYNNCHGD QVVERLLQHL RRVDAPVLES LALEVPAQLP DPPTITASPC 450
    CNTVVLPQWH SFSRTHNVCE LCVNQTSGGM KPSSVSVPQC SFFEMAAALD 500
    SFYLKEQTFY HVASDSIECS NFLTSYSPFS YYTACCRTIS RGVSGFIDSE 550
    QGVFEAPTVA FSSLEKKCEV DAPSSVPHIE ENRYLFPEVD MTSTNFTGLS 600
    CRTNKTLNIY LLDSNLFWLY AERLGAPSST QVKEFAAIVD VKEESHYILD 650
    PKQALMKLTL ESFIQNFSVL YSPLKRHLIG SGSAQFPSQH LITEVTTDTF 700
    WEVVLQKQDV LLLYYAPWCG FCPSLNHIFI QLARNLPMDT FTVARIDVSQ 750
    NDLPWEFMVD RLPTVLFFPC NRKDLSVKYP EDVPITLPNL LRFILHHSDP 800
    ASSPQNVANS PTKECLQSEA VLQRGHISHL EREIQKLRAE ISSLQRAQVQ 850
    VESQLSSARR DEHRLRQQQR ALEEQHSLLH AHSEQLQALY EQKTRELQEL 900
    ARKLQELADA SENLLTENTW LKILVATMER KLEGRDGAES LAAQREVHPK 950
    QPEPSATPQL PGSSPPPANV SATLVSERNK ENRTD 985
    Length:985
    Mass (Da):110,529
    Last modified:July 5, 2005 - v2
    Checksum:i4A8C852F8E81B8BC
    GO
    Isoform 2 (identifier: Q6PKC3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         265-291: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:958
    Mass (Da):107,512
    Checksum:i7E051E7BFA61B4F8
    GO
    Isoform 3 (identifier: Q6PKC3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         265-278: ALESTSSPRALVSF → DGVSPCRPGWSAVA
         279-985: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:278
    Mass (Da):30,375
    Checksum:iC89C635153ADE9F9
    GO

    Sequence cautioni

    The sequence BAC11044.1 differs from that shown. Reason: Intron retention.
    The sequence AAD20043.1 differs from that shown. Reason: Frameshift at position 618.
    The sequence AAH13727.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB55129.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti783 – 7831V → L.1 Publication
    Corresponds to variant rs3190321 [ dbSNP | Ensembl ].
    VAR_022767

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei265 – 29127Missing in isoform 2. 1 PublicationVSP_014335Add
    BLAST
    Alternative sequencei265 – 27814ALEST…ALVSF → DGVSPCRPGWSAVA in isoform 3. 1 PublicationVSP_014336Add
    BLAST
    Alternative sequencei279 – 985707Missing in isoform 3. 1 PublicationVSP_014337Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027464 mRNA. Translation: BAB55129.1. Different initiation.
    AK027646 mRNA. Translation: BAB55262.1.
    AK074534 mRNA. Translation: BAC11044.1. Sequence problems.
    BC002856 mRNA. Translation: AAH02856.1.
    BC013727 mRNA. Translation: AAH13727.1. Different initiation.
    BC018635 mRNA. Translation: AAH18635.1.
    AF131780 mRNA. Translation: AAD20043.1. Frameshift.
    CR457152 mRNA. Translation: CAG33433.1.
    CCDSiCCDS32387.1. [Q6PKC3-2]
    RefSeqiNP_056998.4. NM_015914.5. [Q6PKC3-2]
    UniGeneiHs.313847.

    Genome annotation databases

    EnsembliENST00000283033; ENSP00000283033; ENSG00000153066. [Q6PKC3-2]
    ENST00000356957; ENSP00000349439; ENSG00000153066. [Q6PKC3-1]
    GeneIDi51061.
    KEGGihsa:51061.
    UCSCiuc002dbg.1. human. [Q6PKC3-2]
    uc010buu.1. human. [Q6PKC3-1]

    Polymorphism databases

    DMDMi68566185.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK027464 mRNA. Translation: BAB55129.1 . Different initiation.
    AK027646 mRNA. Translation: BAB55262.1 .
    AK074534 mRNA. Translation: BAC11044.1 . Sequence problems.
    BC002856 mRNA. Translation: AAH02856.1 .
    BC013727 mRNA. Translation: AAH13727.1 . Different initiation.
    BC018635 mRNA. Translation: AAH18635.1 .
    AF131780 mRNA. Translation: AAD20043.1 . Frameshift.
    CR457152 mRNA. Translation: CAG33433.1 .
    CCDSi CCDS32387.1. [Q6PKC3-2 ]
    RefSeqi NP_056998.4. NM_015914.5. [Q6PKC3-2 ]
    UniGenei Hs.313847.

    3D structure databases

    ProteinModelPortali Q6PKC3.
    SMRi Q6PKC3. Positions 127-245, 569-827.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119253. 18 interactions.
    IntActi Q6PKC3. 43 interactions.
    MINTi MINT-2872884.
    STRINGi 9606.ENSP00000283033.

    PTM databases

    PhosphoSitei Q6PKC3.

    Polymorphism databases

    DMDMi 68566185.

    Proteomic databases

    MaxQBi Q6PKC3.
    PaxDbi Q6PKC3.
    PRIDEi Q6PKC3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000283033 ; ENSP00000283033 ; ENSG00000153066 . [Q6PKC3-2 ]
    ENST00000356957 ; ENSP00000349439 ; ENSG00000153066 . [Q6PKC3-1 ]
    GeneIDi 51061.
    KEGGi hsa:51061.
    UCSCi uc002dbg.1. human. [Q6PKC3-2 ]
    uc010buu.1. human. [Q6PKC3-1 ]

    Organism-specific databases

    CTDi 51061.
    GeneCardsi GC16M011772.
    H-InvDB HIX0017349.
    HGNCi HGNC:28030. TXNDC11.
    HPAi HPA041174.
    HPA041390.
    neXtProti NX_Q6PKC3.
    PharmGKBi PA134915251.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000132983.
    HOVERGENi HBG082866.
    InParanoidi Q6PKC3.
    OMAi NFSVLYS.
    OrthoDBi EOG7ZSHSG.
    PhylomeDBi Q6PKC3.
    TreeFami TF323602.

    Miscellaneous databases

    GenomeRNAii 51061.
    NextBioi 53645.
    PROi Q6PKC3.

    Gene expression databases

    ArrayExpressi Q6PKC3.
    Bgeei Q6PKC3.
    CleanExi HS_TXNDC11.
    Genevestigatori Q6PKC3.

    Family and domain databases

    Gene3Di 3.40.30.10. 2 hits.
    InterProi IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 2 hits.
    PROSITEi PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 2).
      Tissue: Embryo and Teratocarcinoma.
    2. "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] (ISOFORMS 1 AND 3), VARIANT LEU-783.
      Tissue: Placenta.
    3. Mei G., Yu W., Gibbs R.A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-985.
      Tissue: Brain.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 656-985.
    5. "Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
      Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
      J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH DUOX1; DUOX2; TPO AND CYBA.
    6. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.

    Entry informationi

    Entry nameiTXD11_HUMAN
    AccessioniPrimary (citable) accession number: Q6PKC3
    Secondary accession number(s): O95887
    , Q6PJA6, Q8N2Q4, Q96K45, Q96K53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3