ID   HEMO_BOVIN              Reviewed;         459 AA.
AC   Q3SZV7;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Hemopexin;
DE   Flags: Precursor;
GN   Name=HPX;
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=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds heme and transports it to the liver for breakdown and
CC       iron recovery, after which the free hemopexin returns to the
CC       circulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- MISCELLANEOUS: The isolated N-terminal domain binds one heme. The full-
CC       length protein also binds one heme, but at a different site. The
CC       physiological significance of this is not clear (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000305}.
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DR   EMBL; BC102687; AAI02688.1; -; mRNA.
DR   RefSeq; NP_001029784.1; NM_001034612.2.
DR   AlphaFoldDB; Q3SZV7; -.
DR   SMR; Q3SZV7; -.
DR   STRING; 9913.ENSBTAP00000004635; -.
DR   PaxDb; Q3SZV7; -.
DR   PeptideAtlas; Q3SZV7; -.
DR   PRIDE; Q3SZV7; -.
DR   GeneID; 534509; -.
DR   KEGG; bta:534509; -.
DR   CTD; 3263; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   HOGENOM; CLU_061713_0_0_1; -.
DR   InParanoid; Q3SZV7; -.
DR   OrthoDB; 792317at2759; -.
DR   TreeFam; TF331201; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0015232; F:heme transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0042168; P:heme metabolic process; IBA:GO_Central.
DR   CDD; cd00094; HX; 2.
DR   Gene3D; 2.110.10.10; -; 2.
DR   InterPro; IPR016358; Hemopexin.
DR   InterPro; IPR000585; Hemopexin-like_dom.
DR   InterPro; IPR036375; Hemopexin-like_dom_sf.
DR   InterPro; IPR018487; Hemopexin-like_repeat.
DR   InterPro; IPR018486; Hemopexin_CS.
DR   Pfam; PF00045; Hemopexin; 3.
DR   PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR   SMART; SM00120; HX; 6.
DR   SUPFAM; SSF50923; SSF50923; 2.
DR   PROSITE; PS00024; HEMOPEXIN; 2.
DR   PROSITE; PS51642; HEMOPEXIN_2; 8.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Heme; Iron; Metal-binding;
KW   Reference proteome; Repeat; Secreted; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..459
FT                   /note="Hemopexin"
FT                   /id="PRO_0000353184"
FT   REPEAT          55..95
FT                   /note="Hemopexin 1"
FT   REPEAT          96..140
FT                   /note="Hemopexin 2"
FT   REPEAT          141..185
FT                   /note="Hemopexin 3"
FT   REPEAT          186..232
FT                   /note="Hemopexin 4"
FT   REPEAT          252..297
FT                   /note="Hemopexin 5"
FT   REPEAT          298..345
FT                   /note="Hemopexin 6"
FT   REPEAT          350..389
FT                   /note="Hemopexin 7"
FT   REPEAT          393..444
FT                   /note="Hemopexin 8"
FT   BINDING         81
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..232
FT                   /evidence="ECO:0000250"
FT   DISULFID        150..155
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..201
FT                   /evidence="ECO:0000250"
FT   DISULFID        250..453
FT                   /evidence="ECO:0000250"
FT   DISULFID        359..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        411..428
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  52209 MW;  7E09A31CA926CBFF CRC64;
     MARALRVPVA LWLLGLCWSL AKAHPLARAP ELGHGVEGGN VAKPDPEVTE RCSDGWGFDA
     TTLDEHGNML FLKGEFVWKG HAWARQLISE RWKDAPSPVD AAFRYDRNSV LLIKGDKFWV
     YPPEKGEEYP KLLQEKFPGI PFPLDAAVEC HRGECSHEGV FFFQGNHTWF WDFSTKTIKK
     RSWPAVGNCS SAIRWLNRYY CFRGNKFLRF DPVTGEVNST YPRDVRDYFM SCPNRGHAHR
     NATQHMDKRC SPHLVLSALL SDNHSATYAF SENHYWRLDS SRDGWHSWRI EHLWPQGPST
     VDAAFLWDKK LYLIQGTQVY IFLTRAGYTL VKDYPKQLEK EFGSPDGVCL HSVDAAFTCP
     GSSQLYIMAG QKLWRLDLNL GAQATWTELP WLHTKVDGAL CTEKSLGPHS CSANGLGLYL
     VQGPNLYCYK DVEELSKTKD LPQAQRMNSL LGCAPHQHS