TXD11_HUMAN
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 03-AUG-2022, entry version 166.
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_001303447.1. [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; 117.
DR IntAct; Q6PKC3; 76.
DR MINT; Q6PKC3; -.
DR STRING; 9606.ENSP00000283033; -.
DR ChEMBL; CHEMBL4630840; -.
DR GlyConnect; 1800; 1 N-Linked glycan (1 site).
DR GlyGen; Q6PKC3; 5 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (2 sites).
DR iPTMnet; Q6PKC3; -.
DR PhosphoSitePlus; Q6PKC3; -.
DR BioMuta; TXNDC11; -.
DR DMDM; 68566185; -.
DR EPD; Q6PKC3; -.
DR jPOST; Q6PKC3; -.
DR MassIVE; Q6PKC3; -.
DR MaxQB; Q6PKC3; -.
DR PaxDb; Q6PKC3; -.
DR PeptideAtlas; Q6PKC3; -.
DR PRIDE; Q6PKC3; -.
DR ProteomicsDB; 67239; -. [Q6PKC3-1]
DR ProteomicsDB; 67240; -. [Q6PKC3-2]
DR ProteomicsDB; 67241; -. [Q6PKC3-3]
DR Antibodypedia; 49688; 124 antibodies from 25 providers.
DR DNASU; 51061; -.
DR Ensembl; ENST00000283033.10; ENSP00000283033.5; ENSG00000153066.13. [Q6PKC3-2]
DR Ensembl; ENST00000356957.7; ENSP00000349439.3; ENSG00000153066.13. [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 CTD; 51061; -.
DR DisGeNET; 51061; -.
DR GeneCards; TXNDC11; -.
DR HGNC; HGNC:28030; TXNDC11.
DR HPA; ENSG00000153066; Low tissue specificity.
DR MIM; 617792; gene.
DR neXtProt; NX_Q6PKC3; -.
DR OpenTargets; ENSG00000153066; -.
DR PharmGKB; PA134915251; -.
DR VEuPathDB; HostDB:ENSG00000153066; -.
DR eggNOG; KOG0190; Eukaryota.
DR GeneTree; ENSGT00390000016020; -.
DR HOGENOM; CLU_010764_1_0_1; -.
DR InParanoid; Q6PKC3; -.
DR OMA; ANDLPWE; -.
DR OrthoDB; 860125at2759; -.
DR PhylomeDB; Q6PKC3; -.
DR TreeFam; TF323602; -.
DR PathwayCommons; Q6PKC3; -.
DR SignaLink; Q6PKC3; -.
DR BioGRID-ORCS; 51061; 10 hits in 1078 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 176 other tissues.
DR ExpressionAtlas; Q6PKC3; baseline and differential.
DR Genevisible; Q6PKC3; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 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; Redox-active center; Reference proteome; Repeat;
KW 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 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
