HEMO_RAT
ID HEMO_RAT Reviewed; 460 AA.
AC P20059; Q5BKB4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Hemopexin;
DE Flags: Precursor;
GN Name=Hpx;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1988069; DOI=10.1021/bi00217a036;
RA Nikkilae H., Gitlin J.D., Mueller-Eberhard U.;
RT "Rat hemopexin. Molecular cloning, primary structural characterization, and
RT analysis of gene expression.";
RL Biochemistry 30:823-829(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1599480; DOI=10.1016/s0006-291x(05)81002-2;
RA Nagae Y., Mueller-Eberhard U.;
RT "Identification of an interleukin-6 responsive element and characterization
RT of the proximal promoter region of the rat hemopexin gene.";
RL Biochem. Biophys. Res. Commun. 185:420-429(1992).
RN [4]
RP PROTEIN SEQUENCE OF 24-53.
RX PubMed=3421961; DOI=10.1016/s0006-291x(88)80540-0;
RA Wellner D., Cheng K.C., Mueller-Eberhard U.;
RT "N-terminal amino acid sequences of the hemopexins from chicken, rat and
RT rabbit.";
RL Biochem. Biophys. Res. Commun. 155:622-625(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-43.
RX PubMed=1587840; DOI=10.1016/s0021-9258(19)50058-8;
RA Swerts J.P., Soula C., Sagot Y., Guinaudy M.J., Guillemot J.-C.,
RA Ferrara P., Duprat A.-M., Cochard P.;
RT "Hemopexin is synthesized in peripheral nerves but not in central nervous
RT system and accumulates after axotomy.";
RL J. Biol. Chem. 267:10596-10600(1992).
RN [6]
RP PROTEIN SEQUENCE OF 90-102; 151-165; 208-218; 255-269 AND 270-282, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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 -!- 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}.
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DR EMBL; M62642; AAA41337.1; -; Genomic_DNA.
DR EMBL; X60006; CAA42621.1; -; Genomic_DNA.
DR EMBL; BC091137; AAH91137.1; -; mRNA.
DR PIR; A43079; OQRT.
DR RefSeq; NP_445770.1; NM_053318.1.
DR AlphaFoldDB; P20059; -.
DR SMR; P20059; -.
DR IntAct; P20059; 1.
DR STRING; 10116.ENSRNOP00000024710; -.
DR ChEMBL; CHEMBL2176811; -.
DR GlyGen; P20059; 5 sites.
DR iPTMnet; P20059; -.
DR PhosphoSitePlus; P20059; -.
DR SwissPalm; P20059; -.
DR jPOST; P20059; -.
DR PaxDb; P20059; -.
DR PRIDE; P20059; -.
DR Ensembl; ENSRNOT00000024710; ENSRNOP00000024710; ENSRNOG00000018257.
DR GeneID; 58917; -.
DR KEGG; rno:58917; -.
DR UCSC; RGD:62040; rat.
DR CTD; 3263; -.
DR RGD; 62040; Hpx.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00390000009178; -.
DR HOGENOM; CLU_061713_0_0_1; -.
DR InParanoid; P20059; -.
DR OMA; CSSAMRW; -.
DR OrthoDB; 792317at2759; -.
DR PhylomeDB; P20059; -.
DR TreeFam; TF331201; -.
DR Reactome; R-RNO-2168880; Scavenging of heme from plasma.
DR PRO; PR:P20059; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018257; Expressed in liver and 19 other tissues.
DR Genevisible; P20059; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0020027; P:hemoglobin metabolic process; ISO:RGD.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; ISO:RGD.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; ISO:RGD.
DR GO; GO:0060332; P:positive regulation of response to interferon-gamma; ISO:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:0051246; P:regulation of protein metabolic process; ISO:RGD.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IEA:Ensembl.
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; 4.
DR PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR SMART; SM00120; HX; 5.
DR SUPFAM; SSF50923; SSF50923; 2.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 8.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heme; Iron;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3421961"
FT CHAIN 24..460
FT /note="Hemopexin"
FT /id="PRO_0000021410"
FT REPEAT 53..93
FT /note="Hemopexin 1"
FT REPEAT 94..138
FT /note="Hemopexin 2"
FT REPEAT 139..183
FT /note="Hemopexin 3"
FT REPEAT 184..230
FT /note="Hemopexin 4"
FT REPEAT 257..302
FT /note="Hemopexin 5"
FT REPEAT 303..350
FT /note="Hemopexin 6"
FT REPEAT 355..394
FT /note="Hemopexin 7"
FT REPEAT 398..448
FT /note="Hemopexin 8"
FT BINDING 79
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 149
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 235
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 291
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 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..230
FT /evidence="ECO:0000250"
FT DISULFID 148..153
FT /evidence="ECO:0000250"
FT DISULFID 187..199
FT /evidence="ECO:0000250"
FT DISULFID 255..458
FT /evidence="ECO:0000250"
FT DISULFID 364..406
FT /evidence="ECO:0000250"
FT DISULFID 416..433
FT /evidence="ECO:0000250"
FT CONFLICT 38
FT /note="N -> C (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..50
FT /note="HC -> KW (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="F -> S (in Ref. 1; AAA41337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51351 MW; 508963FEE0E31D92 CRC64;
MARTVVALNI LVLLGLCWSL AVANPLPAAH ETVAKGENGT KPDSDVIEHC SDAWSFDATT
MDHNGTMLFF KGEFVWRGHS GIRELISERW KNPVTSVDAA FRGPDSVFLI KEDKVWVYPP
EKKENGYPKL FQEEFPGIPY PPDAAVECHR GECQSEGVLF FQGNRKWFWD FATRTQKERS
WPAVGNCTAA LRWLERYYCF QGNKFLRFNP VTGEVPPRYP LDARDYFISC PGRGHGKLRN
GTAHGNSTHP MHSRCNADPG LSALLSDHRG ATYAFSGSHY WRLDSSRDGW HSWPIAHHWP
QGPSAVDAAF SWDEKVYLIQ GTQVYVFLTK GGNNLVSGYP KRLEKELGSP PGISLDTIDA
AFSCPGSSKL YVTSGRRLWW LDLKSGAQAT WAELSWPHEK VDGALCLEKS LGPYSCSSNG
PNLFFIHGPN LYCYSSIDKL NAAKSLPQPQ KVNSILGCSQ
