HEMO_PIG
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 03-AUG-2022, entry version 118.
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 PaxDb; P50828; -.
DR PeptideAtlas; P50828; -.
DR PRIDE; P50828; -.
DR GeneID; 396998; -.
DR KEGG; ssc:396998; -.
DR CTD; 3263; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; P50828; -.
DR OrthoDB; 792317at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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; 5.
DR SUPFAM; SSF50923; SSF50923; 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
