HEMO_MOUSE
ID HEMO_MOUSE Reviewed; 460 AA.
AC Q91X72; P97824; Q3UKP2; Q8WUP0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Hemopexin;
DE Flags: Precursor;
GN Name=Hpx; Synonyms=Hpxn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-460.
RC TISSUE=Liver;
RA Koepsel R.R., Rohrbach D.H., Brekheiser B.B.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-186.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hemopexin family. {ECO:0000305}.
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DR EMBL; AK145928; BAE26759.1; -; mRNA.
DR EMBL; CH466531; EDL16785.1; -; Genomic_DNA.
DR EMBL; BC011246; AAH11246.1; -; mRNA.
DR EMBL; BC019901; AAH19901.1; -; mRNA.
DR EMBL; U89889; AAB49490.1; -; mRNA.
DR CCDS; CCDS21654.1; -.
DR RefSeq; NP_059067.2; NM_017371.2.
DR AlphaFoldDB; Q91X72; -.
DR SMR; Q91X72; -.
DR BioGRID; 200414; 5.
DR IntAct; Q91X72; 1.
DR STRING; 10090.ENSMUSP00000033185; -.
DR CarbonylDB; Q91X72; -.
DR GlyGen; Q91X72; 6 sites.
DR iPTMnet; Q91X72; -.
DR PhosphoSitePlus; Q91X72; -.
DR SwissPalm; Q91X72; -.
DR CPTAC; non-CPTAC-5608; -.
DR EPD; Q91X72; -.
DR jPOST; Q91X72; -.
DR MaxQB; Q91X72; -.
DR PaxDb; Q91X72; -.
DR PeptideAtlas; Q91X72; -.
DR PRIDE; Q91X72; -.
DR ProteomicsDB; 269562; -.
DR Antibodypedia; 23841; 567 antibodies from 38 providers.
DR DNASU; 15458; -.
DR Ensembl; ENSMUST00000033185; ENSMUSP00000033185; ENSMUSG00000030895.
DR GeneID; 15458; -.
DR KEGG; mmu:15458; -.
DR UCSC; uc009iyl.2; mouse.
DR CTD; 3263; -.
DR MGI; MGI:105112; Hpx.
DR VEuPathDB; HostDB:ENSMUSG00000030895; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00390000009178; -.
DR HOGENOM; CLU_061713_0_0_1; -.
DR InParanoid; Q91X72; -.
DR OMA; CSSAMRW; -.
DR OrthoDB; 792317at2759; -.
DR PhylomeDB; Q91X72; -.
DR TreeFam; TF331201; -.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR BioGRID-ORCS; 15458; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Hpx; mouse.
DR PRO; PR:Q91X72; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q91X72; protein.
DR Bgee; ENSMUSG00000030895; Expressed in left lobe of liver and 48 other tissues.
DR ExpressionAtlas; Q91X72; baseline and differential.
DR Genevisible; Q91X72; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO: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 GO; GO:0042168; P:heme metabolic process; IMP:MGI.
DR GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0060332; P:positive regulation of response to interferon-gamma; IMP:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:MGI.
DR GO; GO:0051246; P:regulation of protein metabolic process; IMP:MGI.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IMP:MGI.
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; 6.
DR SUPFAM; SSF50923; SSF50923; 2.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 8.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Heme; Iron; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..460
FT /note="Hemopexin"
FT /id="PRO_0000021407"
FT REPEAT 53..93
FT /note="Hemopexin 1"
FT REPEAT 94..138
FT /note="Hemopexin 2"
FT REPEAT 139..183
FT /note="Hemopexin 3"
FT REPEAT 184..230
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 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 149
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 235
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 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 /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
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 CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..230
FT /evidence="ECO:0000250"
FT DISULFID 148..153
FT /evidence="ECO:0000250"
FT DISULFID 187..199
FT /evidence="ECO:0000250"
FT DISULFID 255..458
FT /evidence="ECO:0000250"
FT DISULFID 364..406
FT /evidence="ECO:0000250"
FT DISULFID 416..433
FT /evidence="ECO:0000250"
FT CONFLICT 30
FT /note="N -> H (in Ref. 3; AAH11246/AAH19901)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="R -> Q (in Ref. 4; AAB49490)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="Missing (in Ref. 4; AAB49490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51318 MW; 5DF86BA50CC23B48 CRC64;
MARTAVALNI LVLLGLCWSL AVASPLPTAN GRVAEVENGT KPDSDVPEHC LDTWSFDAAT
MDHNGTMLFF KGEFVWRGHS GTRELISARW KNPITSVDAA FRGPDSVFLI KEDKVWVYPP
EKKENGYPKL FQEEFPGIPY PPDAAVECHR GECQSEGVLF FQGNRKWFWD FATRTQKERS
WSTVGNCTAA LRWLERYYCF QGNKFLRFNP VTGEVPPRYP LDARDYFVSC PGRGHGRPRN
GTAHGNSTHP MHSRCSPDPG LTALLSDHRG ATYAFTGSHY WRLDSSRDGW HSWPIAHHWP
QGPSTVDAAF SWDDKVYLIQ GTQVYVFLTK GGNNLVSGYP KRLEKELGSP PGISLETIDA
AFSCPGSSRL YVSSGRRLWW LDLKSGAQAT WTEVSWPHEK VDGALCLDKS LGPNTCSSNG
SSLYFIHGPN LYCYSSIDKL NAAKSLPQPQ KVNSILGCSQ
