ID   HEMO_DANRE              Reviewed;         447 AA.
AC   Q6PHG2; A9JSW7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Hemopexin {ECO:0000250|UniProtKB:P20058};
DE   Flags: Precursor;
GN   Name=hpx {ECO:0000312|EMBL:AAI55108.1,
GN   ECO:0000312|ZFIN:ZDB-GENE-030131-5773};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAH56563.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH56563.2};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2007) 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|UniProtKB:P20058}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P20058}.
CC   -!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000255}.
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DR   EMBL; BC056563; AAH56563.2; -; mRNA.
DR   EMBL; BC155107; AAI55108.1; -; mRNA.
DR   RefSeq; NP_001315463.1; NM_001328534.1.
DR   AlphaFoldDB; Q6PHG2; -.
DR   SMR; Q6PHG2; -.
DR   STRING; 7955.ENSDARP00000111337; -.
DR   PaxDb; Q6PHG2; -.
DR   Ensembl; ENSDART00000121506; ENSDARP00000111337; ENSDARG00000012609.
DR   GeneID; 327588; -.
DR   KEGG; dre:327588; -.
DR   CTD; 327588; -.
DR   ZFIN; ZDB-GENE-030131-5773; hpxa.
DR   eggNOG; KOG1565; Eukaryota.
DR   GeneTree; ENSGT00940000166972; -.
DR   HOGENOM; CLU_061713_0_0_1; -.
DR   InParanoid; Q6PHG2; -.
DR   OMA; GSGNDNH; -.
DR   OrthoDB; 792317at2759; -.
DR   PhylomeDB; Q6PHG2; -.
DR   TreeFam; TF331201; -.
DR   Reactome; R-DRE-2168880; Scavenging of heme from plasma.
DR   PRO; PR:Q6PHG2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 9.
DR   Bgee; ENSDARG00000012609; Expressed in liver and 16 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0071391; P:cellular response to estrogen stimulus; IDA:ZFIN.
DR   GO; GO:0042168; P:heme metabolic process; IBA:GO_Central.
DR   CDD; cd00094; HX; 1.
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   PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR   SMART; SM00120; HX; 5.
DR   SUPFAM; SSF50923; SSF50923; 2.
DR   PROSITE; PS51642; HEMOPEXIN_2; 8.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Metal-binding; Reference proteome; Repeat;
KW   Secreted; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..447
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000382471"
FT   REPEAT          53..93
FT                   /note="Hemopexin 1"
FT   REPEAT          99..151
FT                   /note="Hemopexin 2"
FT   REPEAT          152..197
FT                   /note="Hemopexin 3"
FT   REPEAT          198..243
FT                   /note="Hemopexin 4"
FT   REPEAT          262..304
FT                   /note="Hemopexin 5"
FT   REPEAT          305..351
FT                   /note="Hemopexin 6"
FT   REPEAT          352..395
FT                   /note="Hemopexin 7"
FT   REPEAT          396..441
FT                   /note="Hemopexin 8"
FT   REGION          20..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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|UniProtKB:P20058"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        362
FT                   /note="E -> A (in Ref. 1; AAI55108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="A -> T (in Ref. 1; AAI55108)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  51027 MW;  6681AAF09B0917D2 CRC64;
     MRLIQALSLC LALSLSLAAP PQHKEDHSHK GKPGGEGHKH ELHHGAQLDR CKGIEFDAVA
     VNEEGVPYFF KGDHLFKGFH GKAELSNKTF PELDDHHHLG HVDAAFRMHS EDSPDHHDHQ
     FFFLDNMVFS YFKHKLEKDY PKLISAVFPG IPDHLDAAVE CPKPDCPNDT VIFFKGDEIY
     HFNMHTKKVD EKEFKSMPNC TGAFRYMGHY YCFHGHQFSK FDPMTGEVHG KYPKEARDYF
     MRCPHFGSKT TDDHIEREQC SRVHLDAITS DDAGNIYAFR GHHFLSITGD KFHSDTIESE
     FKELHSEVDS VFSYDGHFYM IKDNDVFVYK VGKPHTHLEG YPKPLKDVLG IEGPVDAAFV
     CEDHHVVHII KGQSIYDVDL KATPRKLVKE GTITQFKRID AAMCGPKGVT VVIGNHFYNY
     DSVQVMLMAK IMPEQQKVSQ QLFGCDH