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Hemopexin

 HEMO_RABIT              Reviewed;         460 AA.
P20058;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
10-MAY-2017, entry version 120.
RecName: Full=Hemopexin;
Flags: Precursor;
Name=HPX;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND HEME-BINDING
SITES.
TISSUE=Liver;
PubMed=7681064;
Morgan W.T., Muster P., Tatum F., Kao S.-M., Alam J., Smith A.;
"Identification of the histidine residues of hemopexin that coordinate
with heme-iron and of a receptor-binding region.";
J. Biol. Chem. 268:6256-6262(1993).
[2]
PROTEIN SEQUENCE OF 26-53.
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).
[3]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 242-460, AND DISULFIDE BONDS.
PubMed=8590016; DOI=10.1016/S0969-2126(01)00189-7;
Faber H.R., Groom C.R., Baker H.M., Morgan W.T., Smith A., Baker E.N.;
"1.8-A crystal structure of the C-terminal domain of rabbit serum
haemopexin.";
Structure 3:551-559(1995).
[4]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HEME, AND
DISULFIDE BONDS.
PubMed=10504726; DOI=10.1038/13294;
Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A.,
Baker E.N.;
"Crystal structure of hemopexin reveals a novel high-affinity heme
site formed between two beta-propeller domains.";
Nat. Struct. Biol. 6:926-931(1999).
-!- 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.
-!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000305}.
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EMBL; X16429; CAA34452.1; -; mRNA.
PIR; A46006; OQRB.
RefSeq; NP_001076229.1; NM_001082760.1.
UniGene; Ocu.3101; -.
PDB; 1HXN; X-ray; 1.80 A; A=242-460.
PDB; 1QHU; X-ray; 2.30 A; A=1-460.
PDB; 1QJS; X-ray; 2.90 A; A/B=1-460.
PDB; 4RT6; X-ray; 2.80 A; B=26-239.
PDBsum; 1HXN; -.
PDBsum; 1QHU; -.
PDBsum; 1QJS; -.
PDBsum; 4RT6; -.
ProteinModelPortal; P20058; -.
SMR; P20058; -.
STRING; 9986.ENSOCUP00000021163; -.
PRIDE; P20058; -.
GeneID; 100009541; -.
KEGG; ocu:100009541; -.
CTD; 3263; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000112887; -.
HOVERGEN; HBG005956; -.
InParanoid; P20058; -.
KO; K18977; -.
EvolutionaryTrace; P20058; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IDA:MGI.
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.
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; 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;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Heme; Iron; Metal-binding;
Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 25 {ECO:0000269|PubMed:3421961}.
CHAIN 26 460 Hemopexin.
/FTId=PRO_0000021409.
REPEAT 55 95 Hemopexin 1.
REPEAT 96 141 Hemopexin 2.
REPEAT 142 186 Hemopexin 3.
REPEAT 187 233 Hemopexin 4.
REPEAT 257 302 Hemopexin 5.
REPEAT 303 350 Hemopexin 6.
REPEAT 355 394 Hemopexin 7.
REPEAT 398 448 Hemopexin 8.
METAL 81 81 Iron (heme 1 axial ligand).
METAL 152 152 Iron (heme 1 axial ligand).
METAL 238 238 Iron (heme 2 axial ligand).
METAL 291 291 Iron (heme 2 axial ligand).
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 233
DISULFID 151 156
DISULFID 190 202
DISULFID 255 458
DISULFID 364 406
DISULFID 416 433
CONFLICT 52 52 C -> W (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 50 52 {ECO:0000244|PDB:1QHU}.
STRAND 59 63 {ECO:0000244|PDB:1QHU}.
STRAND 69 73 {ECO:0000244|PDB:1QHU}.
STRAND 76 79 {ECO:0000244|PDB:1QHU}.
TURN 80 83 {ECO:0000244|PDB:1QHU}.
STRAND 84 87 {ECO:0000244|PDB:1QHU}.
HELIX 88 91 {ECO:0000244|PDB:1QHU}.
STRAND 92 94 {ECO:0000244|PDB:4RT6}.
STRAND 100 105 {ECO:0000244|PDB:1QHU}.
TURN 106 108 {ECO:0000244|PDB:1QHU}.
STRAND 109 114 {ECO:0000244|PDB:1QHU}.
STRAND 117 121 {ECO:0000244|PDB:1QHU}.
HELIX 134 137 {ECO:0000244|PDB:1QHU}.
STRAND 147 151 {ECO:0000244|PDB:1QHU}.
STRAND 156 165 {ECO:0000244|PDB:1QHU}.
STRAND 168 173 {ECO:0000244|PDB:1QHU}.
TURN 174 177 {ECO:0000244|PDB:1QHU}.
STRAND 178 182 {ECO:0000244|PDB:1QHU}.
STRAND 185 187 {ECO:0000244|PDB:1QJS}.
STRAND 191 196 {ECO:0000244|PDB:1QHU}.
STRAND 199 204 {ECO:0000244|PDB:1QHU}.
STRAND 207 211 {ECO:0000244|PDB:1QHU}.
TURN 213 215 {ECO:0000244|PDB:1QHU}.
HELIX 226 229 {ECO:0000244|PDB:1QHU}.
HELIX 253 255 {ECO:0000244|PDB:1HXN}.
STRAND 263 266 {ECO:0000244|PDB:1HXN}.
STRAND 272 276 {ECO:0000244|PDB:1HXN}.
STRAND 279 287 {ECO:0000244|PDB:1HXN}.
STRAND 292 294 {ECO:0000244|PDB:1QJS}.
HELIX 295 297 {ECO:0000244|PDB:1HXN}.
STRAND 307 312 {ECO:0000244|PDB:1HXN}.
STRAND 315 320 {ECO:0000244|PDB:1HXN}.
STRAND 323 328 {ECO:0000244|PDB:1HXN}.
STRAND 330 332 {ECO:0000244|PDB:1HXN}.
STRAND 340 342 {ECO:0000244|PDB:1QJS}.
HELIX 343 347 {ECO:0000244|PDB:1HXN}.
STRAND 360 362 {ECO:0000244|PDB:1HXN}.
STRAND 369 374 {ECO:0000244|PDB:1HXN}.
STRAND 377 382 {ECO:0000244|PDB:1HXN}.
HELIX 383 388 {ECO:0000244|PDB:1HXN}.
STRAND 392 394 {ECO:0000244|PDB:1HXN}.
STRAND 402 409 {ECO:0000244|PDB:1HXN}.
STRAND 411 413 {ECO:0000244|PDB:1HXN}.
STRAND 418 420 {ECO:0000244|PDB:1HXN}.
STRAND 422 427 {ECO:0000244|PDB:1HXN}.
STRAND 430 436 {ECO:0000244|PDB:1HXN}.
HELIX 437 442 {ECO:0000244|PDB:1HXN}.
HELIX 452 455 {ECO:0000244|PDB:1HXN}.
SEQUENCE 460 AA; 51767 MW; 193B59856DEF64EE CRC64;
MVKASGIPIA LGVWGLCWSL ATVNSVPLTS AHGNVTEGES GTKPEADVIE QCSDGWSFDA
TTLDDNGTML FFKDEFVWKS HRGIRELISE RWKNFIGPVD AAFRHGHTSV YLIKGDKVWV
YTSEKNEKVY PKSLQDEFPG IPFPLDAAVE CHRGECQDEG ILFFQGNRKW FWDLTTGTKK
ERSWPAVGNC TSALRWLGRY YCFQGNQFLR FNPVSGEVPP GYPLDVRDYF LSCPGRGHRS
SHRNSTQHGH ESTRCDPDLV LSAMVSDNHG ATYVFSGSHY WRLDTNRDGW HSWPIAHQWP
QGPSTVDAAF SWEDKLYLIQ DTKVYVFLTK GGYTLVNGYP KRLEKELGSP PVISLEAVDA
AFVCPGSSRL HIMAGRRLWW LDLKSGAQAT WTELPWPHEK VDGALCMEKP LGPNSCSTSG
PNLYLIHGPN LYCYRHVDKL NAAKNLPQPQ RVSRLLGCTH


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