ID G1MD79_AILME Unreviewed; 464 AA.
AC G1MD79;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Hemopexin {ECO:0000256|ARBA:ARBA00013632};
GN Name=HPX {ECO:0000313|Ensembl:ENSAMEP00000017307.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000017307.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000017307.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000017307.2}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_019661247.1; XM_019805688.1.
DR AlphaFoldDB; G1MD79; -.
DR STRING; 9646.ENSAMEP00000017307; -.
DR Ensembl; ENSAMET00000018016.2; ENSAMEP00000017307.2; ENSAMEG00000016372.2.
DR GeneID; 100474911; -.
DR KEGG; aml:100474911; -.
DR CTD; 3263; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00390000009178; -.
DR HOGENOM; CLU_061713_0_0_1; -.
DR InParanoid; G1MD79; -.
DR TreeFam; TF331201; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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:0042168; P:heme metabolic process; IEA:Ensembl.
DR GO; GO:0020027; P:hemoglobin metabolic process; IEA:Ensembl.
DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:InterPro.
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 type II interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; IEA:Ensembl.
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; 4.
DR PIRSF; PIRSF002551; Hemopexin_chordata; 1.
DR SMART; SM00120; HX; 5.
DR SUPFAM; SSF50923; Hemopexin-like domain; 2.
DR PROSITE; PS00024; HEMOPEXIN; 1.
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:UP000008912};
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..464
FT /note="Hemopexin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030171530"
FT REPEAT 55..95
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 96..141
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 142..186
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 187..233
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 261..306
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 307..354
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 359..398
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
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 /evidence="ECO:0000256|PIRSR:PIRSR002551-2"
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 /evidence="ECO:0000256|PIRSR:PIRSR002551-2"
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 /evidence="ECO:0000256|PIRSR:PIRSR002551-2"
FT BINDING 295
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 DISULFID 52..233
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
FT DISULFID 151..156
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
FT DISULFID 190..202
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
FT DISULFID 368..410
FT /evidence="ECO:0000256|PIRSR:PIRSR002551-1"
SQ SEQUENCE 464 AA; 51868 MW; 3461780676FB8408 CRC64;
MARTLGTPIA LGLLGLCWSL AIAHPLPPDG TPGKETEGGS GTRVNPDVTE LCLDGWSFDA
TTLDEHGAML FFKGEFVWKS HRWVQELISE RWKNFTSSVD AAFRRGHNSV FLIKGDKVWV
YPPEKKEKGY PKLLQEEFPG IPSPVDAAVE CHRGECQDEG VLFFKGNQTW FWDLATGTKK
ERSWPAVGEC SSAMRWLSRY YCFRGNQFLR FHPVTGDVLP KYPLDVRDYF IPCPGRGHGH
RNGTGHGNGT HHGHGDMRCS PYLVLSALLT DNHGATYAFS GSHYWRLDTS RDGWHSWPIV
HQWPQGPSTV DAAFSWDNKV YLIQGTQVYI FLTKGGYTLV DGYPKRLEKE FGSPHGINLD
AVDAAFTCPG TSRLHIMAGR KLWWLDLKLG AQATWTELPW PHEKVDGALC MEKSLGPTSC
SANGPGLYLI HGSDLYCYSD VEKLSTAKTL PQPQRVESLL GCNH
//
