THAP4_MOUSE
ID THAP4_MOUSE Reviewed; 569 AA.
AC Q6P3Z3; Q3US28; Q6NZN6; Q6PEN6; Q91WR2; Q9CVE5; Q9CVG3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Peroxynitrite isomerase THAP4 {ECO:0000305};
DE EC=5.99.-.- {ECO:0000250|UniProtKB:Q8WY91};
DE AltName: Full=Ferric nitrobindin {ECO:0000305};
DE Short=Nb(III) {ECO:0000305};
DE AltName: Full=THAP domain-containing protein 4 {ECO:0000312|MGI:MGI:1914276};
GN Name=Thap4 {ECO:0000312|MGI:MGI:1914276};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, Head, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Embryo, Kidney, and Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q8WY91}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peroxynitrite = nitrate; Xref=Rhea:RHEA:63116,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:25941;
CC Evidence={ECO:0000250|UniProtKB:Q8WY91};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63117;
CC Evidence={ECO:0000250|UniProtKB:Q8WY91};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q8WY91};
CC Note=Binds 1 heme b group per subunit, that coordinates a highly
CC solvent-exposed Fe(III) atom. {ECO:0000250|UniProtKB:Q8WY91};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000250|UniProtKB:Q8WY91}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8WY91}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WY91}. Nucleus
CC {ECO:0000250|UniProtKB:Q8WY91}. Note=Localizes mainly in the cytoplasm
CC and partially in the nucleus. {ECO:0000250|UniProtKB:Q8WY91}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P3Z3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P3Z3-2; Sequence=VSP_020080, VSP_020081;
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:0000250|UniProtKB:Q8WY91}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the nitrobindin
CC family. {ECO:0000305}.
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DR EMBL; AK008304; BAB25589.1; -; mRNA.
DR EMBL; AK008587; BAB25763.1; -; mRNA.
DR EMBL; AK140888; BAE24509.1; -; mRNA.
DR EMBL; AK167814; BAE39840.1; -; mRNA.
DR EMBL; BC013538; AAH13538.2; -; mRNA.
DR EMBL; BC057963; AAH57963.2; -; mRNA.
DR EMBL; BC063758; AAH63758.1; -; mRNA.
DR EMBL; BC066042; AAH66042.1; -; mRNA.
DR CCDS; CCDS15194.1; -. [Q6P3Z3-1]
DR RefSeq; NP_001297690.1; NM_001310761.1.
DR RefSeq; NP_080196.3; NM_025920.3. [Q6P3Z3-1]
DR AlphaFoldDB; Q6P3Z3; -.
DR SMR; Q6P3Z3; -.
DR STRING; 10090.ENSMUSP00000140761; -.
DR iPTMnet; Q6P3Z3; -.
DR PhosphoSitePlus; Q6P3Z3; -.
DR EPD; Q6P3Z3; -.
DR MaxQB; Q6P3Z3; -.
DR PaxDb; Q6P3Z3; -.
DR PeptideAtlas; Q6P3Z3; -.
DR PRIDE; Q6P3Z3; -.
DR ProteomicsDB; 262768; -. [Q6P3Z3-1]
DR ProteomicsDB; 262769; -. [Q6P3Z3-2]
DR Antibodypedia; 34568; 77 antibodies from 23 providers.
DR DNASU; 67026; -.
DR Ensembl; ENSMUST00000112905; ENSMUSP00000108526; ENSMUSG00000026279. [Q6P3Z3-2]
DR Ensembl; ENSMUST00000190116; ENSMUSP00000140761; ENSMUSG00000026279. [Q6P3Z3-1]
DR GeneID; 67026; -.
DR KEGG; mmu:67026; -.
DR UCSC; uc007cef.1; mouse. [Q6P3Z3-1]
DR CTD; 51078; -.
DR MGI; MGI:1914276; Thap4.
DR VEuPathDB; HostDB:ENSMUSG00000026279; -.
DR eggNOG; KOG3371; Eukaryota.
DR GeneTree; ENSGT00940000158447; -.
DR HOGENOM; CLU_037087_0_0_1; -.
DR InParanoid; Q6P3Z3; -.
DR OrthoDB; 1382095at2759; -.
DR PhylomeDB; Q6P3Z3; -.
DR TreeFam; TF315956; -.
DR BioGRID-ORCS; 67026; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Thap4; mouse.
DR PRO; PR:Q6P3Z3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6P3Z3; protein.
DR Bgee; ENSMUSG00000026279; Expressed in seminiferous tubule of testis and 260 other tissues.
DR ExpressionAtlas; Q6P3Z3; baseline and differential.
DR Genevisible; Q6P3Z3; MM.
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; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070026; F:nitric oxide binding; ISS:UniProtKB.
DR GO; GO:0062213; F:peroxynitrite isomerase activity; ISS:UniProtKB.
DR GO; GO:0042126; P:nitrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006570; P:tyrosine metabolic process; ISS: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 Alternative splicing; Cytoplasm; DNA-binding; Heme; Iron; Isomerase;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..569
FT /note="Peroxynitrite isomerase THAP4"
FT /id="PRO_0000247858"
FT ZN_FING 1..85
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 88..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..569
FT /note="Nitrobindin"
FT /evidence="ECO:0000250|UniProtKB:Q8WY91"
FT MOTIF 230..233
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250|UniProtKB:Q8WTV1"
FT COMPBIAS 116..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 436
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q8WY91"
FT BINDING 559
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:0000250|UniProtKB:Q8WY91"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WY91"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WY91"
FT VAR_SEQ 376..379
FT /note="VRKL -> SLPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020080"
FT VAR_SEQ 380..569
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020081"
FT CONFLICT 145
FT /note="P -> L (in Ref. 2; AAH57963)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="T -> S (in Ref. 1; BAE24509)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="T -> N (in Ref. 1; BAB25589/BAB25763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 62571 MW; 902FCB807A17DD5A CRC64;
MVICCAAVNC SNRQGKGEKR AVSFHRFPLK DSKRLIQWLK AVQRDNWTPT KYSFLCSEHF
TKDSFSKRLE DQHRLLKPTA VPSIFHLSEK KRGAGGHGHA RRKTTAAMRG HTSAETGKGT
IGSSLSSSDN LMAKPESRKL KRASPQDDAA PKVTPGAVSQ EQGQSLEKTP GDDPAAPLAR
GQEEAQASAT EADHQKASSS TDAEGADKSG ISMDDFTPPG SGACKFIGSL HSYSFSSKHT
RERPSVPREP MDRKRLKREM EPRCSGNSVA QSPPSSSLTA TPQKASQSPS APPTDVTPKP
AAEAVQSEHS DASPMSINEV ILSASGACKL IDSLHSYCFS ARQNKSQVCC LREQVEKKNG
ELKSLRQKVS RSDSQVRKLR EKLDELRRAS LPYLPYLSGL LPPSHEPPKL NPVVEPLSWM
LGTWLSDPPG VGTFPTLQPF QYLEEVHISH VGQPMLNFSF NSFHPETHKP MHRECGFIRL
KPDTNKVAFV SAQNTGIVEV EEGEVNGQEL CVSSHSVSRI SFAKEPHVEQ ITRKFRLNSE
GKLEQTVSMA TTTQPMTQHL HITYKKVTP
