HEMO_PONAB
ID HEMO_PONAB Reviewed; 462 AA.
AC Q5R543; Q5NVR6;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Hemopexin;
DE Flags: Precursor;
GN Name=HPX;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; CR861031; CAH93123.1; -; mRNA.
DR EMBL; CR925939; CAI29597.1; -; mRNA.
DR RefSeq; NP_001127067.1; NM_001133595.1.
DR AlphaFoldDB; Q5R543; -.
DR SMR; Q5R543; -.
DR STRING; 9601.ENSPPYP00000004063; -.
DR PRIDE; Q5R543; -.
DR Ensembl; ENSPPYT00000004222; ENSPPYP00000004063; ENSPPYG00000003544.
DR GeneID; 100174097; -.
DR KEGG; pon:100174097; -.
DR CTD; 3263; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00390000009178; -.
DR HOGENOM; CLU_061713_0_0_1; -.
DR InParanoid; Q5R543; -.
DR OMA; CSSAMRW; -.
DR OrthoDB; 792317at2759; -.
DR TreeFam; TF331201; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
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; 5.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Heme; Iron; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..462
FT /note="Hemopexin"
FT /id="PRO_0000353185"
FT REPEAT 53..93
FT /note="Hemopexin 1"
FT REPEAT 94..139
FT /note="Hemopexin 2"
FT REPEAT 140..184
FT /note="Hemopexin 3"
FT REPEAT 185..231
FT /note="Hemopexin 4"
FT REPEAT 259..304
FT /note="Hemopexin 5"
FT REPEAT 305..352
FT /note="Hemopexin 6"
FT REPEAT 357..396
FT /note="Hemopexin 7"
FT REPEAT 400..450
FT /note="Hemopexin 8"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 150
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 236
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 293
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 64
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..231
FT /evidence="ECO:0000250"
FT DISULFID 149..154
FT /evidence="ECO:0000250"
FT DISULFID 188..200
FT /evidence="ECO:0000250"
FT DISULFID 257..460
FT /evidence="ECO:0000250"
FT DISULFID 366..408
FT /evidence="ECO:0000250"
FT DISULFID 418..435
FT /evidence="ECO:0000250"
FT CONFLICT 390
FT /note="Q -> K (in Ref. 1; CAI29597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51614 MW; E7EDB4CC1668AC4D CRC64;
MARALGAPIA LGLWSLCWSL AIATPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT
LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP
PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER
SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN
GTGHGNGTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ
WPQGPSTVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKQLEKEVG TPHGIILDSV
DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ALWTELPWPH EKVDGALCVE KSLGPNSCSA
NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC TH