ID   TXD11_HUMAN             Reviewed;         985 AA.
AC   Q6PKC3; O95887; Q6PJA6; Q8N2Q4; Q96K45; Q96K53;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   10-JUN-2026, entry version 184.
DE   RecName: Full=Thioredoxin domain-containing protein 11;
DE   AltName: Full=EF-hand-binding protein 1;
GN   Name=TXNDC11; Synonyms=EFP1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo, and Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP   LEU-783.
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-985.
RC   TISSUE=Brain;
RA   Mei G., Yu W., Gibbs R.A.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 656-985.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH DUOX1; DUOX2; TPO AND CYBA.
RX   PubMed=15561711; DOI=10.1074/jbc.m407709200;
RA   Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E.,
RA   Miot F.;
RT   "Identification of a novel partner of duox: EFP1, a thioredoxin-related
RT   protein.";
RL   J. Biol. Chem. 280:3096-3103(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA   Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA   Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT   "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT   network: indicating the involvement of ribonucleoside-diphosphate reductase
RT   M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT   transduction.";
RL   Mol. Cell. Proteomics 6:1952-1967(2007).
CC   -!- FUNCTION: May act as a redox regulator involved in DUOX proteins
CC       folding. The interaction with DUOX1 and DUOX2 suggest that it belongs
CC       to a multiprotein complex constituting the thyroid H(2)O(2) generating
CC       system. It is however not sufficient to assist DUOX1 and DUOX2 in
CC       H(2)O(2) generation.
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of DUOX1 and DUOX2.
CC       Interacts with TPO and CYBA. {ECO:0000269|PubMed:15561711}.
CC   -!- INTERACTION:
CC       Q6PKC3; P42858: HTT; NbExp=7; IntAct=EBI-749812, EBI-466029;
CC       Q6PKC3; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-749812, EBI-6426443;
CC       Q6PKC3; Q13064: MKRN3; NbExp=3; IntAct=EBI-749812, EBI-2340269;
CC       Q6PKC3; Q99633: PRPF18; NbExp=3; IntAct=EBI-749812, EBI-2798416;
CC       Q6PKC3; Q8WUD1: RAB2B; NbExp=3; IntAct=EBI-749812, EBI-5542466;
CC       Q6PKC3; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-749812, EBI-740727;
CC       Q6PKC3; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-749812, EBI-6863748;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PKC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PKC3-2; Sequence=VSP_014335;
CC       Name=3;
CC         IsoId=Q6PKC3-3; Sequence=VSP_014336, VSP_014337;
CC   -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed at higher
CC       level in thyroid and prostate. {ECO:0000269|PubMed:15561711}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20043.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH13727.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB55129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC11044.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AK027464; BAB55129.1; ALT_INIT; mRNA.
DR   EMBL; AK027646; BAB55262.1; -; mRNA.
DR   EMBL; AK074534; BAC11044.1; ALT_SEQ; mRNA.
DR   EMBL; BC002856; AAH02856.1; -; mRNA.
DR   EMBL; BC013727; AAH13727.1; ALT_INIT; mRNA.
DR   EMBL; BC018635; AAH18635.1; -; mRNA.
DR   EMBL; AF131780; AAD20043.1; ALT_FRAME; mRNA.
DR   EMBL; CR457152; CAG33433.1; -; mRNA.
DR   CCDS; CCDS32387.1; -. [Q6PKC3-2]
DR   CCDS; CCDS76822.1; -. [Q6PKC3-1]
DR   RefSeq; NP_001290376.1; NM_001303447.2. [Q6PKC3-1]
DR   RefSeq; NP_001310953.1; NM_001324024.1.
DR   RefSeq; NP_001310954.1; NM_001324025.1.
DR   RefSeq; NP_056998.4; NM_015914.6. [Q6PKC3-2]
DR   AlphaFoldDB; Q6PKC3; -.
DR   BioGRID; 119253; 120.
DR   CORUM; Q6PKC3; -.
DR   FunCoup; Q6PKC3; 1620.
DR   IntAct; Q6PKC3; 115.
DR   MINT; Q6PKC3; -.
DR   NDEx; IQUERY-CP-TXNDC11; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000349439; -.
DR   ChEMBL; CHEMBL4630840; -.
DR   GlyConnect; Q6PKC3; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q6PKC3; 2 sites, 2 glycans.
DR   GlyGen; Q6PKC3; 8 sites, 12 N-linked glycans (5 sites), 2 O-linked glycans (3 sites).
DR   iPTMnet; Q6PKC3; -.
DR   PhosphoSitePlus; Q6PKC3; -.
DR   BioMuta; TXNDC11; -.
DR   DMDM; 68566185; -.
DR   jPOST; Q6PKC3; -.
DR   MassIVE; Q6PKC3; -.
DR   PaxDb; 9606-ENSP00000349439; -.
DR   PeptideAtlas; Q6PKC3; -.
DR   ProteomicsDB; 67239; -. [Q6PKC3-1]
DR   ProteomicsDB; 67240; -. [Q6PKC3-2]
DR   ProteomicsDB; 67241; -. [Q6PKC3-3]
DR   Pumba; Q6PKC3; -.
DR   Antibodypedia; 49688; 115 antibodies from 24 providers.
DR   DNASU; 51061; -.
DR   Ensembl; ENST00000283033.10; ENSP00000283033.5; ENSG00000153066.14. [Q6PKC3-2]
DR   Ensembl; ENST00000356957.7; ENSP00000349439.3; ENSG00000153066.14. [Q6PKC3-1]
DR   GeneID; 51061; -.
DR   KEGG; hsa:51061; -.
DR   MANE-Select; ENST00000283033.10; ENSP00000283033.5; NM_015914.7; NP_056998.4. [Q6PKC3-2]
DR   UCSC; uc002dbg.2; human. [Q6PKC3-1]
DR   AGR; HGNC:28030; -.
DR   ClinPGx; PA134915251; -.
DR   CTD; 51061; -.
DR   DisGeNET; 51061; -.
DR   GeneCards; TXNDC11; -.
DR   HGNC; HGNC:28030; TXNDC11.
DR   HPA; ENSG00000153066; Low tissue specificity.
DR   MIM; 617792; gene.
DR   OpenTargets; ENSG00000153066; -.
DR   VEuPathDB; HostDB:ENSG00000153066; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   GeneTree; ENSGT00390000016020; -.
DR   HOGENOM; CLU_010764_1_0_1; -.
DR   InParanoid; Q6PKC3; -.
DR   OMA; VIYLYHQ; -.
DR   OrthoDB; 1910803at2759; -.
DR   PAN-GO; Q6PKC3; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6PKC3; -.
DR   PathwayCommons; Q6PKC3; -.
DR   Reactome; R-HSA-209968; Thyroxine biosynthesis.
DR   SignaLink; Q6PKC3; -.
DR   Agora; ENSG00000153066; -.
DR   BioGRID-ORCS; 51061; 10 hits in 1156 CRISPR screens.
DR   ChiTaRS; TXNDC11; human.
DR   GenomeRNAi; 51061; -.
DR   Pharos; Q6PKC3; Tbio.
DR   PRO; PR:Q6PKC3; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q6PKC3; protein.
DR   Bgee; ENSG00000153066; Expressed in bone marrow cell and 178 other cell types or tissues.
DR   ExpressionAtlas; Q6PKC3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   CDD; cd03006; PDI_a_EFP1_N; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR052792; Thioredoxin_dom-contain_11.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR058777; TXNDC11_thioredoxin.
DR   PANTHER; PTHR46497; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 11; 1.
DR   PANTHER; PTHR46497:SF1; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 11; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF26234; TXNDC11_2nd; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disulfide bond; Endoplasmic reticulum;
KW   Membrane; Phosphoprotein; Proteomics identification; Redox-active center;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..985
FT                   /note="Thioredoxin domain-containing protein 11"
FT                   /id="PRO_0000120173"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          92..214
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          649..799
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          821..919
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..11
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..38
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         828
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17693683"
FT   DISULFID        469..472
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        719..722
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   VAR_SEQ         265..291
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_014335"
FT   VAR_SEQ         265..278
FT                   /note="ALESTSSPRALVSF -> DGVSPCRPGWSAVA (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014336"
FT   VAR_SEQ         279..985
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014337"
FT   VARIANT         783
FT                   /note="V -> L (in dbSNP:rs3190321)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_022767"
SQ   SEQUENCE   985 AA;  110529 MW;  4A8C852F8E81B8BC CRC64;
     MSECGGRGGG SSSSEDAEDE GGGGGGPAGS DCLSSSPTLA TASSAGRLRR GLRGAFLMAR
     QRPELLCGAV ALGCALLLAL KFTCSRAKDV IIPAKPPVSF FSLRSPVLDL FQGQLDYAEY
     VRRDSEVVLL FFYAPWCGQS IAARAEIEQA ASRLSDQVLF VAINCWWNQG KCRKQKHFFY
     FPVIYLYHRS FGPIEYKGPM SAVYIEKFVR RVMKPLLYIP SQSELLDFLS NYEPGVLGYF
     EFSGSPQPPG YLTFFTSALH SLKKALESTS SPRALVSFTG EWHLETKIYV LDYLGTVRFG
     VITNKHLAKL VSLVHSGSVY LHRHFNTSLV FPREVLNYTA ENICKWALEN QETLFRWLRP
     HGGKSLLLNN ELKKGPALFL FIPFNPLAES HPLIDEITEV ALEYNNCHGD QVVERLLQHL
     RRVDAPVLES LALEVPAQLP DPPTITASPC CNTVVLPQWH SFSRTHNVCE LCVNQTSGGM
     KPSSVSVPQC SFFEMAAALD SFYLKEQTFY HVASDSIECS NFLTSYSPFS YYTACCRTIS
     RGVSGFIDSE QGVFEAPTVA FSSLEKKCEV DAPSSVPHIE ENRYLFPEVD MTSTNFTGLS
     CRTNKTLNIY LLDSNLFWLY AERLGAPSST QVKEFAAIVD VKEESHYILD PKQALMKLTL
     ESFIQNFSVL YSPLKRHLIG SGSAQFPSQH LITEVTTDTF WEVVLQKQDV LLLYYAPWCG
     FCPSLNHIFI QLARNLPMDT FTVARIDVSQ NDLPWEFMVD RLPTVLFFPC NRKDLSVKYP
     EDVPITLPNL LRFILHHSDP ASSPQNVANS PTKECLQSEA VLQRGHISHL EREIQKLRAE
     ISSLQRAQVQ VESQLSSARR DEHRLRQQQR ALEEQHSLLH AHSEQLQALY EQKTRELQEL
     ARKLQELADA SENLLTENTW LKILVATMER KLEGRDGAES LAAQREVHPK QPEPSATPQL
     PGSSPPPANV SATLVSERNK ENRTD
//