HEBP1_MOUSE
ID HEBP1_MOUSE Reviewed; 190 AA.
AC Q9R257; O88814;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Heme-binding protein 1;
DE AltName: Full=p22HBP;
GN Name=Hebp1; Synonyms=Hbp;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9813049; DOI=10.1074/jbc.273.47.31388;
RA Taketani S., Adachi Y., Kohno H., Ikehara S., Tokunaga R., Ishii T.;
RT "Molecular characterization of a newly identified heme-binding protein
RT induced during differentiation of Murine erythroleukemia cells.";
RL J. Biol. Chem. 273:31388-31394(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10640688; DOI=10.1016/s0169-328x(99)00277-6;
RA Zylka M.J., Reppert S.M.;
RT "Discovery of a putative heme-binding protein family (SOUL/HBP) by two-
RT tissue suppression subtractive hybridization and database searches.";
RL Brain Res. Mol. Brain Res. 74:175-181(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=12413491; DOI=10.1016/s0003-9861(02)00471-x;
RA Jacob Blackmon B., Dailey T.A., Lianchun X., Dailey H.A.;
RT "Characterization of a human and mouse tetrapyrrole-binding protein.";
RL Arch. Biochem. Biophys. 407:196-201(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [8]
RP STRUCTURE BY NMR OF 7-190, FUNCTION AS HEME-BINDING PROTEIN, SUBUNIT, AND
RP DOMAIN.
RX PubMed=16905545; DOI=10.1074/jbc.m605988200;
RA Dias J.S., Macedo A.L., Ferreira G.C., Peterson F.C., Volkman B.F.,
RA Goodfellow B.J.;
RT "The first structure from the SOUL/HBP family of heme-binding proteins,
RT murine P22HBP.";
RL J. Biol. Chem. 281:31553-31561(2006).
RN [9]
RP STRUCTURE BY NMR, SUBUNIT, AND DOMAIN.
RX PubMed=16905148; DOI=10.1016/j.jmb.2006.07.010;
RA Gell D.A., Westman B.J., Gorman D., Liew C., Welch J.J., Weiss M.J.,
RA Mackay J.P.;
RT "A novel haem-binding interface in the 22 kDa haem-binding protein
RT p22HBP.";
RL J. Mol. Biol. 362:287-297(2006).
CC -!- FUNCTION: May bind free porphyrinogens that may be present in the cell
CC and thus facilitate removal of these potentially toxic compound. Binds
CC with a high affinity to one molecule of heme or porphyrins. It binds
CC metalloporphyrins, free porphyrins and N-methylprotoporphyrin with
CC similar affinities. {ECO:0000269|PubMed:12413491,
CC ECO:0000269|PubMed:16905545}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12413491,
CC ECO:0000269|PubMed:16905148, ECO:0000269|PubMed:16905545}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12413491,
CC ECO:0000269|PubMed:9813049}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Extremely abundant in
CC liver. {ECO:0000269|PubMed:9813049}.
CC -!- DOMAIN: Forms a distorted beta-barrel structure, with two helices that
CC are packed against the outer surface of the barrel. Porphyrins are
CC expected to bind to a hydrophobic patch on the outer surface of the
CC beta-barrel structure. {ECO:0000269|PubMed:16905148,
CC ECO:0000269|PubMed:16905545}.
CC -!- SIMILARITY: Belongs to the HEBP family. {ECO:0000305}.
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DR EMBL; AB013095; BAA33770.1; -; mRNA.
DR EMBL; AF117613; AAD32096.1; -; mRNA.
DR EMBL; CT010262; CAJ18470.1; -; mRNA.
DR EMBL; AC131718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012654; AAH12654.1; -; mRNA.
DR CCDS; CCDS20645.1; -.
DR RefSeq; NP_038574.3; NM_013546.3.
DR PDB; 2GOV; NMR; -; A=7-190.
DR PDB; 2HVA; NMR; -; A=1-190.
DR PDB; 4A1M; NMR; -; A=7-190.
DR PDB; 7OON; X-ray; 2.80 A; A/B=7-190.
DR PDBsum; 2GOV; -.
DR PDBsum; 2HVA; -.
DR PDBsum; 4A1M; -.
DR PDBsum; 7OON; -.
DR AlphaFoldDB; Q9R257; -.
DR BMRB; Q9R257; -.
DR SMR; Q9R257; -.
DR BioGRID; 200269; 3.
DR IntAct; Q9R257; 2.
DR STRING; 10090.ENSMUSP00000042232; -.
DR iPTMnet; Q9R257; -.
DR PhosphoSitePlus; Q9R257; -.
DR SwissPalm; Q9R257; -.
DR CPTAC; non-CPTAC-3818; -.
DR jPOST; Q9R257; -.
DR MaxQB; Q9R257; -.
DR PaxDb; Q9R257; -.
DR PeptideAtlas; Q9R257; -.
DR PRIDE; Q9R257; -.
DR ProteomicsDB; 269554; -.
DR DNASU; 15199; -.
DR GeneID; 15199; -.
DR KEGG; mmu:15199; -.
DR UCSC; uc009elh.1; mouse.
DR CTD; 50865; -.
DR MGI; MGI:1333880; Hebp1.
DR eggNOG; ENOG502RYZW; Eukaryota.
DR InParanoid; Q9R257; -.
DR OrthoDB; 1611913at2759; -.
DR TreeFam; TF328887; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
DR BioGRID-ORCS; 15199; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Hebp1; mouse.
DR EvolutionaryTrace; Q9R257; -.
DR PRO; PR:Q9R257; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R257; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0042168; P:heme metabolic process; IC:MGI.
DR Gene3D; 3.20.80.10; -; 1.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR InterPro; IPR006917; SOUL_haem-bd.
DR PANTHER; PTHR11220; PTHR11220; 1.
DR Pfam; PF04832; SOUL; 1.
DR SUPFAM; SSF55136; SSF55136; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..190
FT /note="Heme-binding protein 1"
FT /id="PRO_0000116898"
FT CONFLICT 86
FT /note="L -> V (in Ref. 1; BAA33770, 2; AAD32096, 4;
FT CAJ18470 and 6; AAH12654)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2HVA"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 39..49
FT /evidence="ECO:0007829|PDB:7OON"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2HVA"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:7OON"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:7OON"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:7OON"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:2GOV"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:7OON"
SQ SEQUENCE 190 AA; 21067 MW; C1EA42E1798931DB CRC64;
MLGMIRNSLF GSVETWPWQV LSTGGKEDVS YEERACEGGK FATVEVTDKP VDEALREAMP
KIMKYVGGTN DKGVGMGMTV PVSFALFPNE DGSLQKKLKV WFRIPNQFQG SPPAPSDESV
KIEEREGITV YSTQFGGYAK EADYVAHATQ LRTTLEGTPA TYQGDVYYCA GYDPPMKPYG
RRNEVWLVKA
