ID   HEBP1_PIG               Reviewed;         189 AA.
AC   Q5ISC6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Heme-binding protein 1;
GN   Name=HEBP1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15623572; DOI=10.1084/jem.20041277;
RA   Migeotte I., Riboldi E., Franssen J.-D., Gregoire F., Loison C.,
RA   Wittamer V., Detheux M., Robberecht P., Costagliola S., Vassart G.,
RA   Sozzani S., Parmentier M., Communi D.;
RT   "Identification and characterization of an endogenous chemotactic ligand
RT   specific for FPRL2.";
RL   J. Exp. Med. 201:83-93(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HEBP family. {ECO:0000305}.
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DR   EMBL; AY662687; AAU10512.1; -; mRNA.
DR   RefSeq; NP_001011509.1; NM_001011509.1.
DR   AlphaFoldDB; Q5ISC6; -.
DR   SMR; Q5ISC6; -.
DR   STRING; 9823.ENSSSCP00000000651; -.
DR   PaxDb; Q5ISC6; -.
DR   PeptideAtlas; Q5ISC6; -.
DR   PRIDE; Q5ISC6; -.
DR   Ensembl; ENSSSCT00005028750; ENSSSCP00005017559; ENSSSCG00005018195.
DR   Ensembl; ENSSSCT00035067455; ENSSSCP00035027338; ENSSSCG00035050626.
DR   Ensembl; ENSSSCT00040035245; ENSSSCP00040014611; ENSSSCG00040026265.
DR   Ensembl; ENSSSCT00045008296; ENSSSCP00045005642; ENSSSCG00045004985.
DR   Ensembl; ENSSSCT00050054615; ENSSSCP00050023060; ENSSSCG00050040387.
DR   Ensembl; ENSSSCT00055015865; ENSSSCP00055012476; ENSSSCG00055008075.
DR   Ensembl; ENSSSCT00060077498; ENSSSCP00060033492; ENSSSCG00060056871.
DR   GeneID; 494567; -.
DR   KEGG; ssc:494567; -.
DR   CTD; 50865; -.
DR   eggNOG; ENOG502RYZW; Eukaryota.
DR   HOGENOM; CLU_068699_3_1_1; -.
DR   InParanoid; Q5ISC6; -.
DR   OrthoDB; 1611913at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..189
FT                   /note="Heme-binding protein 1"
FT                   /id="PRO_0000116899"
SQ   SEQUENCE   189 AA;  21070 MW;  BE9B446729D7465F CRC64;
     MLGMIKNSLF GSVETWPWQV LSKGDKQDIS YEERACEGGK FATVEMTDKP VDEALREAMP
     KVMKYVGGSN DKGIGMGMTV PISFAVFPSD GGSLQKKLKV WFRIPNEFQS NPPVPSDDSI
     KIEERESITV YSLQFGGYAK EADYVARAAQ LRTALEGIAT CRSDVYFCTG YDPPMKPYGR
     RNEVWLVKA