ID   HEMO_PIG                Reviewed;         459 AA.
AC   P50828;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Hemopexin;
DE   AltName: Full=Hyaluronidase;
DE            EC=3.2.1.35;
DE   Flags: Precursor;
GN   Name=HPX;
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], AND PROTEIN SEQUENCE OF 29-48 AND 368-388.
RC   TISSUE=Liver;
RX   PubMed=7798203; DOI=10.1016/s0021-9258(18)31605-3;
RA   Zhu L., Hope T.J., Hall J., Davies A., Stern M., Mueller-Eberhard U.,
RA   Stern R., Parslow T.G.;
RT   "Molecular cloning of a mammalian hyaluronidase reveals identity with
RT   hemopexin, a serum heme-binding protein.";
RL   J. Biol. Chem. 269:32092-32097(1994).
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC         glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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}.
CC   -!- CAUTION: Lacks the conserved His heme iron ligand in position 81. There
CC       is a Gln in this position. {ECO:0000305}.
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DR   EMBL; U14751; AAC48457.1; -; mRNA.
DR   PIR; A55486; A55486.
DR   RefSeq; NP_999118.1; NM_213953.2.
DR   AlphaFoldDB; P50828; -.
DR   SMR; P50828; -.
DR   STRING; 9823.ENSSSCP00000015556; -.
DR   GlyCosmos; P50828; 4 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000015556; -.
DR   PeptideAtlas; P50828; -.
DR   GeneID; 396998; -.
DR   KEGG; ssc:396998; -.
DR   CTD; 3263; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   InParanoid; P50828; -.
DR   OrthoDB; 5312290at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; 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:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042168; P:heme metabolic process; IBA:GO_Central.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:InterPro.
DR   CDD; cd00094; HX; 2.
DR   Gene3D; 2.110.10.10; Hemopexin-like domain; 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   PANTHER; PTHR22917:SF9; HEMOPEXIN; 1.
DR   PANTHER; PTHR22917; HEMOPEXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00045; Hemopexin; 4.
DR   PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR   SMART; SM00120; HX; 5.
DR   SUPFAM; SSF50923; Hemopexin-like domain; 2.
DR   PROSITE; PS00024; HEMOPEXIN; 2.
DR   PROSITE; PS51642; HEMOPEXIN_2; 8.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase; Heme;
KW   Hydrolase; Iron; Metal-binding; Reference proteome; Repeat; Secreted;
KW   Signal; Transport.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:7798203"
FT   CHAIN           29..459
FT                   /note="Hemopexin"
FT                   /id="PRO_0000021408"
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..443
FT                   /note="Hemopexin 8"
FT   REGION          31..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
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;  51306 MW;  DB06BB44C29789CF CRC64;
     MARALGTVEA PWLLGLCCSL AIAHPLSLTA GPKHGAEGRN ESKPDPDVTE RCSDGWGFDA
     STLDEHGAML FFKGPSVWAG QNWTRGLISE RWKNAPSSVD AAFRRGHDRV FLIQGDKVWV
     YPPEKEKENP RSLQEEFPGV PSPLDAAVEC HRGECQDEGV LFFQGTHTWF WDSTTKTTKE
     RLWPAVGNCS SAMRWISRYY CFRGNQFLRF DPVTGHVDPK YPRDVRDYFM SCPGRGHAHR
     NATHRGDDRC SPDLVLTALL SDNHGATYAF RGTHYWRLDT SRDGWHSWPI DHQWSHGPSA
     VDAAFSWDDK LYLIQGTQVY IFLTKAGYTL VDNYPKQLEK ELGSPHGISL DAVDATFVCP
     GTSRLHVMAG RKLWWLDLSL GAQGPWTELP WPHEKVDAAL CTEKSLGPNS CSASGLGLYI
     VHGPHVYCYK DVEKLVSAKA LPQPQSVNSL LGCHRSRGS
//