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Hemopexin (Hyaluronidase) (EC 3.2.1.35)

 HEMO_PIG                Reviewed;         459 AA.
P50828;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-MAY-2017, entry version 104.
RecName: Full=Hemopexin;
AltName: Full=Hyaluronidase;
EC=3.2.1.35;
Flags: Precursor;
Name=HPX;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-48 AND 368-388.
TISSUE=Liver;
PubMed=7798203;
Zhu L., Hope T.J., Hall J., Davies A., Stern M., Mueller-Eberhard U.,
Stern R., Parslow T.G.;
"Molecular cloning of a mammalian hyaluronidase reveals identity with
hemopexin, a serum heme-binding protein.";
J. Biol. Chem. 269:32092-32097(1994).
-!- FUNCTION: Binds heme and transports it to the liver for breakdown
and iron recovery, after which the free hemopexin returns to the
circulation.
-!- CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-linkages between
N-acetyl-beta-D-glucosamine and D-glucuronate residues in
hyaluronate.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- MISCELLANEOUS: The isolated N-terminal domain binds one heme. The
full-length protein also binds one heme, but at a different site.
The physiological significance of this is not clear (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000305}.
-!- CAUTION: Lacks the conserved His heme iron ligand in position 81.
There is a Gln in this position. {ECO:0000305}.
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EMBL; U14751; AAC48457.1; -; mRNA.
PIR; A55486; A55486.
RefSeq; NP_999118.1; NM_213953.2.
UniGene; Ssc.4250; -.
ProteinModelPortal; P50828; -.
SMR; P50828; -.
STRING; 9823.ENSSSCP00000015556; -.
PaxDb; P50828; -.
PeptideAtlas; P50828; -.
PRIDE; P50828; -.
GeneID; 396998; -.
KEGG; ssc:396998; -.
CTD; 3263; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000112887; -.
HOVERGEN; HBG005956; -.
InParanoid; P50828; -.
KO; K18977; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0015232; F:heme transporter activity; IEA:InterPro.
GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
CDD; cd00094; HX; 2.
Gene3D; 2.110.10.10; -; 2.
InterPro; IPR016358; Hemopexin.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
Pfam; PF00045; Hemopexin; 3.
PIRSF; PIRSF002551; Hemopexin_chordata; 1.
SMART; SM00120; HX; 5.
SUPFAM; SSF50923; SSF50923; 2.
PROSITE; PS00024; HEMOPEXIN; 2.
PROSITE; PS51642; HEMOPEXIN_2; 8.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Glycosidase; Heme; Hydrolase; Iron; Metal-binding;
Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 28 {ECO:0000269|PubMed:7798203}.
CHAIN 29 459 Hemopexin.
/FTId=PRO_0000021408.
REPEAT 55 95 Hemopexin 1.
REPEAT 96 140 Hemopexin 2.
REPEAT 141 185 Hemopexin 3.
REPEAT 186 232 Hemopexin 4.
REPEAT 252 297 Hemopexin 5.
REPEAT 298 345 Hemopexin 6.
REPEAT 350 389 Hemopexin 7.
REPEAT 393 443 Hemopexin 8.
METAL 151 151 Iron (heme 1 axial ligand).
{ECO:0000250}.
METAL 237 237 Iron (heme 2 axial ligand).
{ECO:0000250}.
METAL 286 286 Iron (heme 2 axial ligand).
{ECO:0000250}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 232 {ECO:0000250}.
DISULFID 150 155 {ECO:0000250}.
DISULFID 189 201 {ECO:0000250}.
DISULFID 250 453 {ECO:0000250}.
DISULFID 359 401 {ECO:0000250}.
DISULFID 411 428 {ECO:0000250}.
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


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