THAP4_HUMAN
ID THAP4_HUMAN Reviewed; 577 AA.
AC Q8WY91; Q53NU7; Q6GRN0; Q6IPJ3; Q9NW26; Q9Y325;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Peroxynitrite isomerase THAP4 {ECO:0000305|PubMed:30524950};
DE EC=5.99.-.- {ECO:0000269|PubMed:30524950};
DE AltName: Full=Ferric Homo sapiens nitrobindin {ECO:0000303|PubMed:32295384};
DE Short=Hs-Nb(III) {ECO:0000303|PubMed:32295384};
DE AltName: Full=THAP domain-containing protein 4 {ECO:0000312|HGNC:HGNC:23187};
GN Name=THAP4 {ECO:0000312|HGNC:HGNC:23187}; ORFNames=CGI-36, PP238;
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).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-121.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-121.
RC TISSUE=Brain, Eye, Melanoma, and Ovarian carcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-577 (ISOFORM 1).
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DOMAIN.
RX PubMed=30524950; DOI=10.1002/2211-5463.12534;
RA De Simone G., di Masi A., Polticelli F., Ascenzi P.;
RT "Human nitrobindin: the first example of an all-beta-barrel ferric heme-
RT protein that catalyzes peroxynitrite detoxification.";
RL FEBS Open Bio 8:2002-2010(2018).
RN [9]
RP FUNCTION, COFACTOR, AND NO-BINDING.
RX PubMed=32295384; DOI=10.1089/ars.2019.7874;
RA De Simone G., di Masi A., Vita G.M., Polticelli F., Pesce A., Nardini M.,
RA Bolognesi M., Ciaccio C., Coletta M., Turilli E.S., Fasano M.,
RA Tognaccini L., Smulevich G., Abbruzzetti S., Viappiani C., Bruno S.,
RA Ascenzi P.;
RT "Mycobacterial and Human Nitrobindins: Structure and Function.";
RL Antioxid. Redox Signal. 33:229-246(2020).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 415-577 IN COMPLEX WITH HEME,
RP COFACTOR, SUBUNIT, AND DOMAIN.
RX PubMed=21387410; DOI=10.1002/prot.22944;
RA Bianchetti C.M., Bingman C.A., Phillips G.N. Jr.;
RT "Structure of the C-terminal heme-binding domain of THAP domain containing
RT protein 4 from Homo sapiens.";
RL Proteins 79:1337-1341(2011).
CC -!- FUNCTION: Heme-binding protein able to scavenge peroxynitrite and to
CC protect free L-tyrosine against peroxynitrite-mediated nitration, by
CC acting as a peroxynitrite isomerase that converts peroxynitrite to
CC nitrate. Therefore, this protein likely plays a role in peroxynitrite
CC sensing and in the detoxification of reactive nitrogen and oxygen
CC species (RNS and ROS, respectively). Is able to bind nitric oxide (NO)
CC in vitro, but may act as a sensor of peroxynitrite levels in vivo,
CC possibly modulating the transcriptional activity residing in the N-
CC terminal region. {ECO:0000269|PubMed:30524950,
CC ECO:0000269|PubMed:32295384}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peroxynitrite = nitrate; Xref=Rhea:RHEA:63116,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:25941;
CC Evidence={ECO:0000269|PubMed:30524950};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63117;
CC Evidence={ECO:0000305|PubMed:30524950};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:21387410, ECO:0000269|PubMed:32295384};
CC Note=Binds 1 heme b group per subunit, that coordinates a highly
CC solvent-exposed Fe(III) atom. {ECO:0000269|PubMed:32295384};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000305|PubMed:30524950}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:21387410}.
CC -!- INTERACTION:
CC Q8WY91; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-726691, EBI-11522760;
CC Q8WY91; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-726691, EBI-11957045;
CC Q8WY91; P17707: AMD1; NbExp=3; IntAct=EBI-726691, EBI-6872827;
CC Q8WY91; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-726691, EBI-12109402;
CC Q8WY91; Q8WZ55: BSND; NbExp=3; IntAct=EBI-726691, EBI-7996695;
CC Q8WY91; Q06432: CACNG1; NbExp=3; IntAct=EBI-726691, EBI-9686780;
CC Q8WY91; P60033: CD81; NbExp=3; IntAct=EBI-726691, EBI-712921;
CC Q8WY91; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-726691, EBI-11522780;
CC Q8WY91; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-726691, EBI-2807956;
CC Q8WY91; P29400-2: COL4A5; NbExp=3; IntAct=EBI-726691, EBI-12211159;
CC Q8WY91; Q96FN4: CPNE2; NbExp=5; IntAct=EBI-726691, EBI-7097057;
CC Q8WY91; P78329: CYP4F2; NbExp=3; IntAct=EBI-726691, EBI-1752413;
CC Q8WY91; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-726691, EBI-12831978;
CC Q8WY91; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-726691, EBI-3918971;
CC Q8WY91; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-726691, EBI-11991950;
CC Q8WY91; O60883: GPR37L1; NbExp=3; IntAct=EBI-726691, EBI-2927498;
CC Q8WY91; P24593: IGFBP5; NbExp=3; IntAct=EBI-726691, EBI-720480;
CC Q8WY91; O43561-2: LAT; NbExp=3; IntAct=EBI-726691, EBI-8070286;
CC Q8WY91; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-726691, EBI-12033434;
CC Q8WY91; Q969L2: MAL2; NbExp=5; IntAct=EBI-726691, EBI-944295;
CC Q8WY91; P11836: MS4A1; NbExp=3; IntAct=EBI-726691, EBI-2808234;
CC Q8WY91; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-726691, EBI-11978907;
CC Q8WY91; Q04941: PLP2; NbExp=3; IntAct=EBI-726691, EBI-608347;
CC Q8WY91; Q59EV6: PPGB; NbExp=3; IntAct=EBI-726691, EBI-14210385;
CC Q8WY91; Q96LZ7: RMDN2; NbExp=3; IntAct=EBI-726691, EBI-2806908;
CC Q8WY91; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-726691, EBI-10244780;
CC Q8WY91; O15126: SCAMP1; NbExp=3; IntAct=EBI-726691, EBI-954338;
CC Q8WY91; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-726691, EBI-10262251;
CC Q8WY91; P08247: SYP; NbExp=3; IntAct=EBI-726691, EBI-9071725;
CC Q8WY91; Q8WY91: THAP4; NbExp=3; IntAct=EBI-726691, EBI-726691;
CC Q8WY91; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-726691, EBI-12845616;
CC Q8WY91; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-726691, EBI-2852148;
CC Q8WY91; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-726691, EBI-12015604;
CC Q8WY91; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-726691, EBI-2548832;
CC Q8WY91; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-726691, EBI-1044859;
CC Q8WY91; P55327-2: TPD52; NbExp=3; IntAct=EBI-726691, EBI-12124194;
CC Q8WY91; P49638: TTPA; NbExp=3; IntAct=EBI-726691, EBI-10210710;
CC Q8WY91; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-726691, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes mainly in the
CC cytoplasm and partially in the nucleus. {ECO:0000269|PubMed:32295384}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WY91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WY91-2; Sequence=VSP_020078, VSP_020079;
CC -!- DOMAIN: The C-terminal nitrobindin region coordinates a heme and bears
CC the isomerase activity. The N-terminal zinc finger domain likely binds
CC DNA and may be involved in transcriptional regulation.
CC {ECO:0000269|PubMed:21387410, ECO:0000269|PubMed:30524950}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the nitrobindin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH09439.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91560.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF132970; AAD27745.1; -; mRNA.
DR EMBL; AF258556; AAG23759.1; -; mRNA.
DR EMBL; AC133528; AAY14918.1; -; Genomic_DNA.
DR EMBL; BC000247; AAH00247.1; ALT_INIT; mRNA.
DR EMBL; BC009439; AAH09439.1; ALT_INIT; mRNA.
DR EMBL; BC069235; AAH69235.1; -; mRNA.
DR EMBL; BC071896; AAH71896.1; -; mRNA.
DR EMBL; BC094822; AAH94822.1; -; mRNA.
DR EMBL; AK001216; BAA91560.1; ALT_INIT; mRNA.
DR CCDS; CCDS2551.1; -. [Q8WY91-1]
DR CCDS; CCDS54440.1; -. [Q8WY91-2]
DR RefSeq; NP_001157828.1; NM_001164356.1. [Q8WY91-2]
DR RefSeq; NP_057047.4; NM_015963.5. [Q8WY91-1]
DR PDB; 3IA8; X-ray; 1.79 A; A/B=415-577.
DR PDBsum; 3IA8; -.
DR AlphaFoldDB; Q8WY91; -.
DR SMR; Q8WY91; -.
DR BioGRID; 119269; 73.
DR IntAct; Q8WY91; 56.
DR MINT; Q8WY91; -.
DR STRING; 9606.ENSP00000385006; -.
DR iPTMnet; Q8WY91; -.
DR PhosphoSitePlus; Q8WY91; -.
DR BioMuta; THAP4; -.
DR DMDM; 29839589; -.
DR EPD; Q8WY91; -.
DR jPOST; Q8WY91; -.
DR MassIVE; Q8WY91; -.
DR MaxQB; Q8WY91; -.
DR PaxDb; Q8WY91; -.
DR PeptideAtlas; Q8WY91; -.
DR PRIDE; Q8WY91; -.
DR ProteomicsDB; 75134; -. [Q8WY91-1]
DR ProteomicsDB; 75135; -. [Q8WY91-2]
DR Antibodypedia; 34568; 77 antibodies from 23 providers.
DR DNASU; 51078; -.
DR Ensembl; ENST00000402136.5; ENSP00000385931.1; ENSG00000176946.13. [Q8WY91-2]
DR Ensembl; ENST00000407315.6; ENSP00000385006.1; ENSG00000176946.13. [Q8WY91-1]
DR GeneID; 51078; -.
DR KEGG; hsa:51078; -.
DR MANE-Select; ENST00000407315.6; ENSP00000385006.1; NM_015963.6; NP_057047.4.
DR UCSC; uc002wbs.3; human. [Q8WY91-1]
DR CTD; 51078; -.
DR GeneCards; THAP4; -.
DR HGNC; HGNC:23187; THAP4.
DR HPA; ENSG00000176946; Low tissue specificity.
DR MIM; 612533; gene.
DR neXtProt; NX_Q8WY91; -.
DR OpenTargets; ENSG00000176946; -.
DR PharmGKB; PA134864723; -.
DR VEuPathDB; HostDB:ENSG00000176946; -.
DR eggNOG; KOG3371; Eukaryota.
DR GeneTree; ENSGT00940000158447; -.
DR HOGENOM; CLU_085483_1_1_1; -.
DR InParanoid; Q8WY91; -.
DR OrthoDB; 1382095at2759; -.
DR PhylomeDB; Q8WY91; -.
DR TreeFam; TF315956; -.
DR PathwayCommons; Q8WY91; -.
DR SignaLink; Q8WY91; -.
DR BioGRID-ORCS; 51078; 23 hits in 1098 CRISPR screens.
DR ChiTaRS; THAP4; human.
DR EvolutionaryTrace; Q8WY91; -.
DR GeneWiki; THAP4; -.
DR GenomeRNAi; 51078; -.
DR Pharos; Q8WY91; Tbio.
DR PRO; PR:Q8WY91; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WY91; protein.
DR Bgee; ENSG00000176946; Expressed in apex of heart and 201 other tissues.
DR ExpressionAtlas; Q8WY91; baseline and differential.
DR Genevisible; Q8WY91; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070026; F:nitric oxide binding; IDA:UniProtKB.
DR GO; GO:0062213; F:peroxynitrite isomerase activity; IDA:UniProtKB.
DR GO; GO:0042126; P:nitrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006570; P:tyrosine metabolic process; IDA:UniProtKB.
DR CDD; cd07828; lipocalin_heme-bd-THAP4-like; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR Gene3D; 6.20.210.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR045165; Nitrobindin.
DR InterPro; IPR014878; THAP4-like_heme-bd.
DR InterPro; IPR006612; THAP_Znf.
DR InterPro; IPR038441; THAP_Znf_sf.
DR PANTHER; PTHR15854; PTHR15854; 1.
DR Pfam; PF05485; THAP; 1.
DR Pfam; PF08768; THAP4_heme-bd; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00980; THAP; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Heme; Iron;
KW Isomerase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..577
FT /note="Peroxynitrite isomerase THAP4"
FT /id="PRO_0000068646"
FT ZN_FING 1..85
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 84..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..577
FT /note="Nitrobindin"
FT /evidence="ECO:0000269|PubMed:21387410,
FT ECO:0000269|PubMed:30524950"
FT MOTIF 235..238
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250|UniProtKB:Q8WTV1"
FT COMPBIAS 90..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 444
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:21387410,
FT ECO:0007744|PDB:3IA8"
FT BINDING 567
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:21387410,
FT ECO:0007744|PDB:3IA8"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..412
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_020078"
FT VAR_SEQ 413
FT /note="R -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10810093"
FT /id="VSP_020079"
FT VARIANT 121
FT /note="S -> G (in dbSNP:rs7424328)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15498874"
FT /id="VAR_027161"
FT CONFLICT 261
FT /note="L -> P (in Ref. 5; BAA91560)"
FT /evidence="ECO:0000305"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 445..457
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 459..471
FT /evidence="ECO:0007829|PDB:3IA8"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 478..488
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 494..501
FT /evidence="ECO:0007829|PDB:3IA8"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 505..514
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 517..527
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 536..545
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 551..559
FT /evidence="ECO:0007829|PDB:3IA8"
FT STRAND 562..576
FT /evidence="ECO:0007829|PDB:3IA8"
SQ SEQUENCE 577 AA; 62890 MW; 40660A5ACDD0A7C3 CRC64;
MVICCAAVNC SNRQGKGEKR AVSFHRFPLK DSKRLIQWLK AVQRDNWTPT KYSFLCSEHF
TKDSFSKRLE DQHRLLKPTA VPSIFHLTEK KRGAGGHGRT RRKDASKATG GVRGHSSAAT
SRGAAGWSPS SSGNPMAKPE SRRLKQAALQ GEATPRAAQE AASQEQAQQA LERTPGDGLA
TMVAGSQGKA EASATDAGDE SATSSIEGGV TDKSGISMDD FTPPGSGACK FIGSLHSYSF
SSKHTRERPS VPREPIDRKR LKKDVEPSCS GSSLGPDKGL AQSPPSSSLT ATPQKPSQSP
SAPPADVTPK PATEAVQSEH SDASPMSINE VILSASGACK LIDSLHSYCF SSRQNKSQVC
CLREQVEKKN GELKSLRQRV SRSDSQVRKL QEKLDELRRV SVPYPSSLLS PSREPPKMNP
VVEPLSWMLG TWLSDPPGAG TYPTLQPFQY LEEVHISHVG QPMLNFSFNS FHPDTRKPMH
RECGFIRLKP DTNKVAFVSA QNTGVVEVEE GEVNGQELCI ASHSIARISF AKEPHVEQIT
RKFRLNSEGK LEQTVSMATT TQPMTQHLHV TYKKVTP
