TXN4A_HUMAN
ID TXN4A_HUMAN Reviewed; 142 AA.
AC P83876; B2RC18; O14834;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Thioredoxin-like protein 4A;
DE AltName: Full=DIM1 protein homolog {ECO:0000303|PubMed:11054566, ECO:0000303|Ref.1};
DE AltName: Full=Spliceosomal U5 snRNP-specific 15 kDa protein {ECO:0000303|PubMed:10610776};
DE AltName: Full=Thioredoxin-like U5 snRNP protein U5-15kD;
GN Name=TXNL4A; Synonyms=DIM1, TXNL4;
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 [MRNA].
RC TISSUE=Liver;
RA Larin D., Ross B.M., Gilliam T.C.;
RT "Human homologue of the S. pombe Dim1p gene.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY
RP (1.4 ANGSTROMS), PROBABLE FUNCTION, DISULFIDE BOND, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10610776; DOI=10.1006/jmbi.1999.3258;
RA Reuter K., Nottrott S., Fabrizio P., Luehrmann R., Ficner R.;
RT "Identification, characterization and crystal structure analysis of the
RT human spliceosomal U5 snRNP-specific 15kD protein.";
RL J. Mol. Biol. 294:515-525(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH HNRPF; HNRPH2; NEDD9 AND PQBP1, AND
RP MUTAGENESIS.
RX PubMed=11054566; DOI=10.1016/s0378-1119(00)00372-3;
RA Zhang Y.-Z., Lindblom T., Chang A., Sudol M., Sluder A.E., Golemis E.A.;
RT "Evidence that Dim1 associates with proteins involved in pre-mRNA splicing,
RT and delineation of residues essential for Dim1 interactions with hnRNP F
RT and Npw38/PQBP-1.";
RL Gene 257:33-43(2000).
RN [7]
RP SUBUNIT.
RX PubMed=16723661; DOI=10.1261/rna.55406;
RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT "The network of protein-protein interactions within the human U4/U6.U5 tri-
RT snRNP.";
RL RNA 12:1418-1430(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20858735; DOI=10.1158/1541-7786.mcr-10-0042;
RA Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
RT "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage
RT response pathways.";
RL Mol. Cancer Res. 8:1388-1398(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP INVOLVEMENT IN BMKS.
RX PubMed=25434003; DOI=10.1016/j.ajhg.2014.10.014;
RA Wieczorek D., Newman W.G., Wieland T., Berulava T., Kaffe M.,
RA Falkenstein D., Beetz C., Graf E., Schwarzmayr T., Douzgou S.,
RA Clayton-Smith J., Daly S.B., Williams S.G., Bhaskar S.S., Urquhart J.E.,
RA Anderson B., O'Sullivan J., Boute O., Gundlach J., Czeschik J.C.,
RA van Essen A.J., Hazan F., Park S., Hing A., Kuechler A., Lohmann D.R.,
RA Ludwig K.U., Mangold E., Steenpass L., Zeschnigk M., Lemke J.R.,
RA Lourenco C.M., Hehr U., Prott E.C., Waldenberger M., Bohmer A.C.,
RA Horsthemke B., O'Keefe R.T., Meitinger T., Burn J., Ludecke H.J.,
RA Strom T.M.;
RT "Compound heterozygosity of low-frequency promoter deletions and rare loss-
RT of-function mutations in TXNL4A causes Burn-McKeown syndrome.";
RL Am. J. Hum. Genet. 95:698-707(2014).
RN [13]
RP STRUCTURE BY NMR, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF CYS-38.
RX PubMed=11015569; DOI=10.1152/physiolgenomics.1999.1.3.109;
RA Zhang Y.-Z., Gould K.L., Dunbrack R.L. Jr., Cheng H., Roder H.,
RA Golemis E.A.;
RT "The evolutionarily conserved Dim1 protein defines a novel branch of the
RT thioredoxin fold superfamily.";
RL Physiol. Genomics 1:109-118(1999).
RN [14]
RP STRUCTURE BY NMR OF 1-128, CIRCULAR DICHROISM, DISULFIDE BOND, AND
RP MUTAGENESIS.
RX PubMed=12911302; DOI=10.1021/bi034486i;
RA Zhang Y.Z., Cheng H., Gould K.L., Golemis E.A., Roder H.;
RT "Structure, stability, and function of hDim1 investigated by NMR, circular
RT dichroism, and mutational analysis.";
RL Biochemistry 42:9609-9618(2003).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH CD2BP2, AND
RP INTERACTION WITH CD2BP2.
RX PubMed=17467737; DOI=10.1016/j.jmb.2007.03.077;
RA Nielsen T.K., Liu S., Luhrmann R., Ficner R.;
RT "Structural basis for the bifunctionality of the U5 snRNP 52K protein
RT (CD2BP2).";
RL J. Mol. Biol. 369:902-908(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 4-137 IN COMPLEX WITH PQBP1 AND
RP CD2BP2, AND INTERACTION WITH PQBP1 AND CD2BP2.
RX PubMed=24781215; DOI=10.1038/ncomms4822;
RA Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y., Okazawa H.;
RT "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal
RT protein U5-15 kD.";
RL Nat. Commun. 5:3822-3822(2014).
RN [17] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26912367; DOI=10.1126/science.aad2085;
RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA Luhrmann R., Stark H.;
RT "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL Science 351:1416-1420(2016).
RN [18] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as component of the U5 snRNP
CC and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome
CC assembly, and as component of the precatalytic spliceosome (spliceosome
CC B complex). {ECO:0000269|PubMed:28781166, ECO:0000305|PubMed:10610776,
CC ECO:0000305|PubMed:26912367}.
CC -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC complex) (PubMed:28781166). Component of the U5 snRNP complex
CC (PubMed:10610776). Component of the U4/U6-U5 tri-snRNP complex
CC (PubMed:26912367). The U4/U6-U5 tri-snRNP complex is a building block
CC of the precatalytic spliceosome (spliceosome B complex)
CC (PubMed:26912367, PubMed:28781166). The U4/U6-U5 tri-snRNP complex is
CC composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6,
CC PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1
CC and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8
CC (PubMed:16723661, PubMed:26912367, PubMed:28781166). Directly interacts
CC with CD2BP2 (PubMed:17467737, PubMed:24781215). Interacts with HNRPF,
CC HNRPH2, NEDD9 and PQBP1 (PubMed:11054566). Interacts with ERBB4
CC (PubMed:20858735). {ECO:0000269|PubMed:10610776,
CC ECO:0000269|PubMed:11054566, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:17467737, ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:24781215, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC P83876; O95400: CD2BP2; NbExp=3; IntAct=EBI-746539, EBI-768015;
CC P83876; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-746539, EBI-742054;
CC P83876; O00471: EXOC5; NbExp=3; IntAct=EBI-746539, EBI-949824;
CC P83876; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-746539, EBI-741037;
CC P83876; O94906: PRPF6; NbExp=4; IntAct=EBI-746539, EBI-536755;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10610776,
CC ECO:0000269|PubMed:11054566, ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
CC -!- PTM: The disulfide bond seen in structures determined by X-ray
CC crystallography (PubMed:10610776) and NMR (PubMed:12911302) is not
CC essential for protein folding and function (PubMed:12911302 and
CC PubMed:17467737). {ECO:0000269|PubMed:10610776,
CC ECO:0000269|PubMed:12911302}.
CC -!- DISEASE: Burn-McKeown syndrome (BMKS) [MIM:608572]: A disease
CC characterized by choanal atresia, sensorineural deafness, cardiac
CC defects, and typical craniofacial dysmorphism consisting of narrow
CC palpebral fissures, coloboma of the lower eyelids, prominent nose with
CC high nasal bridge, short philtrum, cleft lip and/or palate, and large
CC and protruding ears. Intellectual development is normal.
CC {ECO:0000269|PubMed:25434003}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DIM1 family. {ECO:0000305}.
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DR EMBL; AF023611; AAB81950.1; -; mRNA.
DR EMBL; AF146373; AAF17332.1; -; mRNA.
DR EMBL; AK314901; BAG37415.1; -; mRNA.
DR EMBL; CH471117; EAW66640.1; -; Genomic_DNA.
DR EMBL; BC001046; AAH01046.1; -; mRNA.
DR EMBL; BC019272; AAH19272.1; -; mRNA.
DR CCDS; CCDS32852.1; -.
DR RefSeq; NP_001290400.1; NM_001303471.2.
DR RefSeq; NP_001292486.1; NM_001305557.1.
DR RefSeq; NP_001292492.1; NM_001305563.1.
DR RefSeq; NP_001292493.1; NM_001305564.1.
DR RefSeq; NP_006692.1; NM_006701.4.
DR PDB; 1PQN; NMR; -; A=2-128.
DR PDB; 1QGV; X-ray; 1.40 A; A=1-142.
DR PDB; 1SYX; X-ray; 2.35 A; A/C/E=1-142.
DR PDB; 3JCR; EM; 7.00 A; E=1-142.
DR PDB; 4BWQ; X-ray; 2.10 A; A/C/E/G=4-137.
DR PDB; 4BWS; X-ray; 2.50 A; A/D=4-137.
DR PDB; 4CDO; X-ray; 2.50 A; A/C=4-137.
DR PDB; 5O9Z; EM; 4.50 A; J=1-142.
DR PDB; 6AH0; EM; 5.70 A; O=1-142.
DR PDB; 6AHD; EM; 3.80 A; O=1-142.
DR PDB; 6QW6; EM; 2.92 A; 5D=1-142.
DR PDB; 6QX9; EM; 3.28 A; 5D=1-142.
DR PDBsum; 1PQN; -.
DR PDBsum; 1QGV; -.
DR PDBsum; 1SYX; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 4BWQ; -.
DR PDBsum; 4BWS; -.
DR PDBsum; 4CDO; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; P83876; -.
DR SMR; P83876; -.
DR BioGRID; 116113; 77.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; P83876; -.
DR IntAct; P83876; 31.
DR MINT; P83876; -.
DR STRING; 9606.ENSP00000269601; -.
DR GlyGen; P83876; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P83876; -.
DR PhosphoSitePlus; P83876; -.
DR BioMuta; TXNL4A; -.
DR DMDM; 46577662; -.
DR EPD; P83876; -.
DR jPOST; P83876; -.
DR MassIVE; P83876; -.
DR MaxQB; P83876; -.
DR PaxDb; P83876; -.
DR PeptideAtlas; P83876; -.
DR PRIDE; P83876; -.
DR ProteomicsDB; 57740; -.
DR TopDownProteomics; P83876; -.
DR Antibodypedia; 23516; 78 antibodies from 20 providers.
DR DNASU; 10907; -.
DR Ensembl; ENST00000269601.10; ENSP00000269601.4; ENSG00000141759.15.
DR GeneID; 10907; -.
DR KEGG; hsa:10907; -.
DR MANE-Select; ENST00000269601.10; ENSP00000269601.4; NM_006701.5; NP_006692.1.
DR UCSC; uc002lnp.4; human.
DR CTD; 10907; -.
DR DisGeNET; 10907; -.
DR GeneCards; TXNL4A; -.
DR GeneReviews; TXNL4A; -.
DR HGNC; HGNC:30551; TXNL4A.
DR HPA; ENSG00000141759; Low tissue specificity.
DR MalaCards; TXNL4A; -.
DR MIM; 608572; phenotype.
DR MIM; 611595; gene.
DR neXtProt; NX_P83876; -.
DR OpenTargets; ENSG00000141759; -.
DR Orphanet; 1200; Burn-McKeown syndrome.
DR PharmGKB; PA134937290; -.
DR VEuPathDB; HostDB:ENSG00000141759; -.
DR eggNOG; KOG3414; Eukaryota.
DR GeneTree; ENSGT00390000010779; -.
DR HOGENOM; CLU_117348_0_0_1; -.
DR InParanoid; P83876; -.
DR OMA; DFNEMYE; -.
DR OrthoDB; 1320693at2759; -.
DR PhylomeDB; P83876; -.
DR TreeFam; TF313562; -.
DR PathwayCommons; P83876; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; P83876; -.
DR BioGRID-ORCS; 10907; 813 hits in 994 CRISPR screens.
DR ChiTaRS; TXNL4A; human.
DR EvolutionaryTrace; P83876; -.
DR GeneWiki; TXNL4A; -.
DR GenomeRNAi; 10907; -.
DR Pharos; P83876; Tbio.
DR PRO; PR:P83876; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P83876; protein.
DR Bgee; ENSG00000141759; Expressed in parotid gland and 201 other tissues.
DR ExpressionAtlas; P83876; baseline and differential.
DR Genevisible; P83876; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; TAS:UniProtKB.
DR CDD; cd02954; DIM1; 1.
DR IDEAL; IID00559; -.
DR InterPro; IPR004123; Dim1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12052; PTHR12052; 1.
DR Pfam; PF02966; DIM1; 1.
DR PIRSF; PIRSF017199; mRNA_splic_U5; 1.
DR SMART; SM01410; DIM1; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Deafness;
KW Direct protein sequencing; Disulfide bond; Mitosis; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..142
FT /note="Thioredoxin-like protein 4A"
FT /id="PRO_0000218287"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT DISULFID 38..79
FT /evidence="ECO:0000269|PubMed:10610776,
FT ECO:0000269|PubMed:12911302"
FT MUTAGEN 38
FT /note="C->A: Viable when expressed in S.pombe."
FT /evidence="ECO:0000269|PubMed:11015569"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:1QGV"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:1QGV"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:1QGV"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1QGV"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1QGV"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1QGV"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1QGV"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1QGV"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1QGV"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4BWQ"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1PQN"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:1QGV"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1QGV"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1QGV"
SQ SEQUENCE 142 AA; 16786 MW; EDDDAD7ADAEE87F3 CRC64;
MSYMLPHLHN GWQVDQAILS EEDRVVVIRF GHDWDPTCMK MDEVLYSIAE KVKNFAVIYL
VDITEVPDFN KMYELYDPCT VMFFFRNKHI MIDLGTGNNN KINWAMEDKQ EMVDIIETVY
RGARKGRGLV VSPKDYSTKY RY
