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Hemopexin

 HEMO_RAT                Reviewed;         460 AA.
P20059; Q5BKB4;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 3.
22-NOV-2017, entry version 136.
RecName: Full=Hemopexin;
Flags: Precursor;
Name=Hpx;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1988069; DOI=10.1021/bi00217a036;
Nikkilae H., Gitlin J.D., Mueller-Eberhard U.;
"Rat hemopexin. Molecular cloning, primary structural
characterization, and analysis of gene expression.";
Biochemistry 30:823-829(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=1599480; DOI=10.1016/S0006-291X(05)81002-2;
Nagae Y., Mueller-Eberhard U.;
"Identification of an interleukin-6 responsive element and
characterization of the proximal promoter region of the rat hemopexin
gene.";
Biochem. Biophys. Res. Commun. 185:420-429(1992).
[4]
PROTEIN SEQUENCE OF 24-53.
PubMed=3421961; DOI=10.1016/S0006-291X(88)80540-0;
Wellner D., Cheng K.C., Mueller-Eberhard U.;
"N-terminal amino acid sequences of the hemopexins from chicken, rat
and rabbit.";
Biochem. Biophys. Res. Commun. 155:622-625(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-43.
PubMed=1587840;
Swerts J.P., Soula C., Sagot Y., Guinaudy M.J., Guillemot J.-C.,
Ferrara P., Duprat A.-M., Cochard P.;
"Hemopexin is synthesized in peripheral nerves but not in central
nervous system and accumulates after axotomy.";
J. Biol. Chem. 267:10596-10600(1992).
[6]
PROTEIN SEQUENCE OF 90-102; 151-165; 208-218; 255-269 AND 270-282, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
-!- FUNCTION: Binds heme and transports it to the liver for breakdown
and iron recovery, after which the free hemopexin returns to the
circulation.
-!- 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}.
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EMBL; M62642; AAA41337.1; -; Genomic_DNA.
EMBL; X60006; CAA42621.1; -; Genomic_DNA.
EMBL; BC091137; AAH91137.1; -; mRNA.
PIR; A43079; OQRT.
RefSeq; NP_445770.1; NM_053318.1.
UniGene; Rn.2380; -.
ProteinModelPortal; P20059; -.
SMR; P20059; -.
STRING; 10116.ENSRNOP00000024710; -.
ChEMBL; CHEMBL2176811; -.
iPTMnet; P20059; -.
PhosphoSitePlus; P20059; -.
PaxDb; P20059; -.
PRIDE; P20059; -.
Ensembl; ENSRNOT00000024710; ENSRNOP00000024710; ENSRNOG00000018257.
GeneID; 58917; -.
KEGG; rno:58917; -.
UCSC; RGD:62040; rat.
CTD; 3263; -.
RGD; 62040; Hpx.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00390000009178; -.
HOGENOM; HOG000112887; -.
HOVERGEN; HBG005956; -.
InParanoid; P20059; -.
KO; K18977; -.
OMA; AVECHRG; -.
OrthoDB; EOG091G052J; -.
PhylomeDB; P20059; -.
TreeFam; TF331201; -.
Reactome; R-RNO-2168880; Scavenging of heme from plasma.
PRO; PR:P20059; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000018257; -.
Genevisible; P20059; RN.
GO; GO:0072562; C:blood microparticle; ISO:RGD.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0015232; F:heme transporter activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
GO; GO:0042168; P:heme metabolic process; ISO:RGD.
GO; GO:0020027; P:hemoglobin metabolic process; ISO:RGD.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; ISO:RGD.
GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:RGD.
GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; ISO:RGD.
GO; GO:0060332; P:positive regulation of response to interferon-gamma; ISO:RGD.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
GO; GO:0051246; P:regulation of protein metabolic process; ISO:RGD.
CDD; cd00094; HX; 2.
Gene3D; 2.110.10.10; -; 2.
InterPro; IPR016358; Hemopexin.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
Pfam; PF00045; Hemopexin; 4.
PIRSF; PIRSF002551; Hemopexin_chordata; 1.
SMART; SM00120; HX; 5.
SUPFAM; SSF50923; SSF50923; 2.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 8.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Heme; Iron; Metal-binding; Reference proteome; Repeat;
Secreted; Signal; Transport.
SIGNAL 1 23 {ECO:0000269|PubMed:3421961}.
CHAIN 24 460 Hemopexin.
/FTId=PRO_0000021410.
REPEAT 53 93 Hemopexin 1.
REPEAT 94 138 Hemopexin 2.
REPEAT 139 183 Hemopexin 3.
REPEAT 184 230 Hemopexin 4.
REPEAT 257 302 Hemopexin 5.
REPEAT 303 350 Hemopexin 6.
REPEAT 355 394 Hemopexin 7.
REPEAT 398 448 Hemopexin 8.
METAL 79 79 Iron (heme 1 axial ligand).
{ECO:0000250}.
METAL 149 149 Iron (heme 1 axial ligand).
{ECO:0000250}.
METAL 235 235 Iron (heme 2 axial ligand).
{ECO:0000250}.
METAL 291 291 Iron (heme 2 axial ligand).
{ECO:0000250}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 230 {ECO:0000250}.
DISULFID 148 153 {ECO:0000250}.
DISULFID 187 199 {ECO:0000250}.
DISULFID 255 458 {ECO:0000250}.
DISULFID 364 406 {ECO:0000250}.
DISULFID 416 433 {ECO:0000250}.
CONFLICT 38 38 N -> C (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 49 50 HC -> KW (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 135 135 F -> S (in Ref. 1; AAA41337).
{ECO:0000305}.
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


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