ID A0A2U4CD99_TURTR Unreviewed; 473 AA.
AC A0A2U4CD99;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Hemopexin {ECO:0000256|ARBA:ARBA00013632};
GN Name=HPX {ECO:0000313|RefSeq:XP_019803408.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019803408.1};
RN [1] {ECO:0000313|RefSeq:XP_019803408.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019803408.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00002031}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the hemopexin family.
CC {ECO:0000256|ARBA:ARBA00011072}.
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DR RefSeq; XP_019803408.1; XM_019947849.2.
DR AlphaFoldDB; A0A2U4CD99; -.
DR GlyCosmos; A0A2U4CD99; 1 site, No reported glycans.
DR GeneID; 101339490; -.
DR InParanoid; A0A2U4CD99; -.
DR OrthoDB; 5312290at2759; -.
DR Proteomes; UP000245320; Chromosome 8.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:intracellular iron ion homeostasis; IEA:InterPro.
DR CDD; cd00094; HX; 2.
DR Gene3D; 2.110.10.10; Hemopexin-like domain; 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 PANTHER; PTHR22917:SF9; HEMOPEXIN; 1.
DR PANTHER; PTHR22917; HEMOPEXIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00045; Hemopexin; 3.
DR PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR SMART; SM00120; HX; 5.
DR SUPFAM; SSF50923; Hemopexin-like domain; 2.
DR PROSITE; PS00024; HEMOPEXIN; 2.
DR PROSITE; PS51642; HEMOPEXIN_2; 7.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002551-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR002551-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR002551-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR002551-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..473
FT /note="Hemopexin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015545900"
FT REPEAT 74..114
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 115..158
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 159..203
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 204..250
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 270..315
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 316..363
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 368..407
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT BINDING 169
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:0000256|PIRSR:PIRSR002551-2"
FT BINDING 255
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:0000256|PIRSR:PIRSR002551-2"
FT BINDING 304
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:0000256|PIRSR:PIRSR002551-2"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-3"
FT DISULFID 71..250
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
FT DISULFID 168..173
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
FT DISULFID 207..219
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
FT DISULFID 377..419
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
SQ SEQUENCE 473 AA; 53526 MW; B10677EEDA6B6D86 CRC64;
MARALGTPVV PWLLGLCWSL ANAHPLSLAN APRHGAEHGN ATKLDPDLCL CAVSSDWPFI
CYRPTSFPER CSDGWGFDAT TLDEHGTMLF FKGEFVWKGQ DWTRELISER WKDVPGPVDA
AFRHGHDRVF LIKGDRVWVY PHDKKEYPKL LQEEFPGIPS PVDAAVECHT EECRNEGVLF
FQGNRTWFWD FTTKTKKERS WQAVGNCSSA MRWLSRYYCF RGNQFLRFNP VTGMVFPKYP
LDVRDYFMPC PGRGHAHGNA TRHGDKRCSP DLVLSALLSD KHGATYAFSG SHYWRLDSSQ
DGWHSWPIEH LWPHGPSTVD TAFSWDDKVY LIQGTQVYIF LTKGGYILVD GYPKRLEKEF
GSPHGINLDT VDAAFTCPGS SRLHIMAGRR LWWLDLKLGA QATWTELPWP HEKVDTALCM
EKSLGPSSCS ANGLGLYLVQ GPNLYCYGDV EKLNVAKALP QPQKVNSLLG CPH
//
