THAP4_BOVIN
ID THAP4_BOVIN Reviewed; 584 AA.
AC Q2TBI2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 70.
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:0000250|UniProtKB:Q8WY91};
GN Name=THAP4 {ECO:0000250|UniProtKB:Q8WY91};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10169.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC110168; AAI10169.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001033758.1; NM_001038669.1.
DR AlphaFoldDB; Q2TBI2; -.
DR SMR; Q2TBI2; -.
DR STRING; 9913.ENSBTAP00000017628; -.
DR PaxDb; Q2TBI2; -.
DR GeneID; 507503; -.
DR KEGG; bta:507503; -.
DR CTD; 51078; -.
DR eggNOG; KOG3371; Eukaryota.
DR InParanoid; Q2TBI2; -.
DR OrthoDB; 1382095at2759; -.
DR Proteomes; UP000009136; Unplaced.
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: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..584
FT /note="Peroxynitrite isomerase THAP4"
FT /id="PRO_0000247857"
FT ZN_FING 1..85
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 84..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..584
FT /note="Nitrobindin"
FT /evidence="ECO:0000250|UniProtKB:Q8WY91"
FT MOTIF 236..239
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250|UniProtKB:Q8WTV1"
FT COMPBIAS 160..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 451
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:Q8WY91"
FT BINDING 574
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 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WY91"
SQ SEQUENCE 584 AA; 63450 MW; 0F3452F76AE850D9 CRC64;
MVICCAAANC SNRQGKGEKR AVSFHRFPLK DSKRLMQWLK AVQRDNWTPT KYSFLCSEHF
TKDSFSKRLE DQHRLLKPTA VPSIFHLAEK KRRAGGHGRP RRRDTGKASA GLRAQASDPV
DGKAAAGSPS SSSASPMAKP EPRKLKRATP QGRTAARAAR ETAGQERGRQ PLEGRAEDGP
ASAATSCSQG EAGTGAEDAG EEGATPADRG LVDRSGVSAD DFTPPGSGAC KFIGSLHSYS
FSSKHARERP AVPREPVERK RLRRDAEPGC SGSSPGPEKG PAQSPPRACP SASSSLTATP
QKPAQGASAP PTDVTPKPAA EAVQSEHSDA SPMSINEVIL SASGACKLID SLHSYCFSSR
QSKSQVCCLR EQVEKKNGEL RTLRQRVSRS DSQVRELRQK LDQLRRLSLP HLSSLLPPGR
EPPKMSPVVE PLSWMLGTWL SEPPGAGTFP TLQPFRYLEE AHISHVGQPM LNFSFNAFHP
DTHKPMHREC GFIRLEPDTN KVAFVSAQNT GIVEVEEGEV NGQELCIASH SIARISFAKE
PHVEQITRKF RLNSEGNLEQ TVSMATTTQP LTQHLHVTYK KVTP
