HEMO_RABIT
ID HEMO_RABIT Reviewed; 460 AA.
AC P20058;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Hemopexin;
DE Flags: Precursor;
GN Name=HPX;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND HEME-BINDING
RP SITES.
RC TISSUE=Liver;
RX PubMed=7681064; DOI=10.1016/s0021-9258(18)53247-6;
RA Morgan W.T., Muster P., Tatum F., Kao S.-M., Alam J., Smith A.;
RT "Identification of the histidine residues of hemopexin that coordinate with
RT heme-iron and of a receptor-binding region.";
RL J. Biol. Chem. 268:6256-6262(1993).
RN [2]
RP PROTEIN SEQUENCE OF 26-53.
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 242-460, AND DISULFIDE BONDS.
RX PubMed=8590016; DOI=10.1016/s0969-2126(01)00189-7;
RA Faber H.R., Groom C.R., Baker H.M., Morgan W.T., Smith A., Baker E.N.;
RT "1.8-A crystal structure of the C-terminal domain of rabbit serum
RT haemopexin.";
RL Structure 3:551-559(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HEME, AND DISULFIDE
RP BONDS.
RX PubMed=10504726; DOI=10.1038/13294;
RA Paoli M., Anderson B.F., Baker H.M., Morgan W.T., Smith A., Baker E.N.;
RT "Crystal structure of hemopexin reveals a novel high-affinity heme site
RT formed between two beta-propeller domains.";
RL Nat. Struct. Biol. 6:926-931(1999).
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.
CC -!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000305}.
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DR EMBL; X16429; CAA34452.1; -; mRNA.
DR PIR; A46006; OQRB.
DR RefSeq; NP_001076229.1; NM_001082760.1.
DR PDB; 1HXN; X-ray; 1.80 A; A=242-460.
DR PDB; 1QHU; X-ray; 2.30 A; A=1-460.
DR PDB; 1QJS; X-ray; 2.90 A; A/B=1-460.
DR PDB; 4RT6; X-ray; 2.80 A; B=26-239.
DR PDBsum; 1HXN; -.
DR PDBsum; 1QHU; -.
DR PDBsum; 1QJS; -.
DR PDBsum; 4RT6; -.
DR AlphaFoldDB; P20058; -.
DR SMR; P20058; -.
DR STRING; 9986.ENSOCUP00000021163; -.
DR PRIDE; P20058; -.
DR GeneID; 100009541; -.
DR KEGG; ocu:100009541; -.
DR CTD; 3263; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; P20058; -.
DR OrthoDB; 792317at2759; -.
DR EvolutionaryTrace; P20058; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:MGI.
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 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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Heme; Iron; Metal-binding; Reference proteome; Repeat; Secreted; Signal;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:3421961"
FT CHAIN 26..460
FT /note="Hemopexin"
FT /id="PRO_0000021409"
FT REPEAT 55..95
FT /note="Hemopexin 1"
FT REPEAT 96..141
FT /note="Hemopexin 2"
FT REPEAT 142..186
FT /note="Hemopexin 3"
FT REPEAT 187..233
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 81
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 BINDING 152
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 BINDING 238
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 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 CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..233
FT DISULFID 151..156
FT DISULFID 190..202
FT DISULFID 255..458
FT DISULFID 364..406
FT DISULFID 416..433
FT CONFLICT 52
FT /note="C -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1QHU"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1QHU"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4RT6"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1QHU"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1QHU"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1QHU"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1QJS"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1QHU"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1QHU"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1QHU"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1QHU"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1QJS"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1QJS"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:1HXN"
FT HELIX 383..388
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:1HXN"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:1HXN"
FT HELIX 437..442
FT /evidence="ECO:0007829|PDB:1HXN"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:1HXN"
SQ 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
