THAP4_RAT
ID THAP4_RAT Reviewed; 569 AA.
AC Q642B6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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|RGD:1359473};
GN Name=Thap4 {ECO:0000312|RGD:1359473};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
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 -!- 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; BC081882; AAH81882.1; -; mRNA.
DR RefSeq; NP_001005564.1; NM_001005564.1.
DR AlphaFoldDB; Q642B6; -.
DR SMR; Q642B6; -.
DR STRING; 10116.ENSRNOP00000024794; -.
DR iPTMnet; Q642B6; -.
DR PhosphoSitePlus; Q642B6; -.
DR PaxDb; Q642B6; -.
DR Ensembl; ENSRNOT00000024794; ENSRNOP00000024794; ENSRNOG00000018351.
DR GeneID; 363291; -.
DR KEGG; rno:363291; -.
DR UCSC; RGD:1359473; rat.
DR CTD; 51078; -.
DR RGD; 1359473; Thap4.
DR eggNOG; KOG3371; Eukaryota.
DR GeneTree; ENSGT00940000158447; -.
DR HOGENOM; CLU_037087_0_0_1; -.
DR InParanoid; Q642B6; -.
DR OMA; QRENWTP; -.
DR OrthoDB; 1382095at2759; -.
DR PhylomeDB; Q642B6; -.
DR TreeFam; TF315956; -.
DR PRO; PR:Q642B6; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000018351; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q642B6; RN.
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:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Heme; Iron; Isomerase; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..569
FT /note="Peroxynitrite isomerase THAP4"
FT /id="PRO_0000247859"
FT ZN_FING 1..85
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 83..219
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"
SQ SEQUENCE 569 AA; 62407 MW; 2DDDC2E59CAE8441 CRC64;
MVICCAAVNC SNRQGKGEKR AVSFHRFPLK DSKRLIQWLK AVQRDNWTPT KYSFLCSEHF
TKDSFSKRLE DQHRLLKPTA VPSIFHLSEK KRGAGGHGPA RRKTTGAMRG HTSAATGKGT
IGSSLSSSDN LMAKPESRKL KRASPQDDTA PKATPGAVSQ EPGQSLERTP GDQAAPLARG
QEEAQVSATE ADHQKASSSA ADAGGADKSG ISMDDFTPPG SGACKFIGSL HSYSFSSKHT
RERPSVPREP MDRKRLKRDI EPRCSGNSVA QSPPSSSLTA TPQKASQSPS APPTDVTPKP
AAEAVQSEHS DANPMSINEV ILSASGACKL IDSLHSYCFS ARQNKSQVCC LREQVEKKNG
ELKSLRQRVS RSDSQVRKLR EKLDELRRAS LPYLPYLSGL LPPSHEPPKL NPVVEPLSWM
LGTWLSEPPG VGTFPTLQPF QYLEEVHISH VGQPMLNFSF NSFHPETHKP MHRECGFIRL
KPDTNKVAFV SAQNTGVVEV EEGEVNGQEL CVSSHSISRI SFAKEPHVQQ ITRKFRLNSE
GKLEQTVSMA TTTQPMTQHL HITYKKVTP
