HPT_MOUSE
ID HPT_MOUSE Reviewed; 347 AA.
AC Q61646;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Haptoglobin;
DE Contains:
DE RecName: Full=Haptoglobin alpha chain;
DE Contains:
DE RecName: Full=Haptoglobin beta chain;
DE Flags: Precursor;
GN Name=Hp;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Ponte P.A., White R.T., Uyeda C.M., Coleman R.T.;
RT "Expression of haptoglobin in mouse adipose tissue.";
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-148; ASN-182 AND ASN-256.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
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: As a result of hemolysis, hemoglobin is found to accumulate
CC in the kidney and is secreted in the urine. Haptoglobin captures, and
CC combines with free plasma hemoglobin to allow hepatic recycling of heme
CC iron and to prevent kidney damage. Haptoglobin also acts as an
CC antioxidant, has antibacterial activity and plays a role in modulating
CC many aspects of the acute phase response. Hemoglobin/haptoglobin
CC complexes are rapidly cleared by the macrophage CD163 scavenger
CC receptor expressed on the surface of liver Kupfer cells through an
CC endocytic lysosomal degradation pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains; disulfide-linked
CC (By similarity). The hemoglobin/haptoglobin complex is composed of a
CC haptoglobin dimer bound to two hemoglobin alpha-beta dimers (By
CC similarity). Interacts with CD163 (By similarity). Interacts with
CC ERGIC3 (By similarity). {ECO:0000250|UniProtKB:P00738,
CC ECO:0000250|UniProtKB:Q8SPS7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- DOMAIN: The beta chain mediates most of the interactions with both
CC subunits of hemoglobin, while the alpha chain forms the homodimeric
CC interface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although homologous to serine proteases, it has lost all
CC essential catalytic residues and has no enzymatic activity.
CC {ECO:0000305}.
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DR EMBL; M96827; AAA37779.1; -; mRNA.
DR CCDS; CCDS40470.1; -.
DR RefSeq; NP_059066.1; NM_017370.2.
DR AlphaFoldDB; Q61646; -.
DR SMR; Q61646; -.
DR BioGRID; 200400; 8.
DR STRING; 10090.ENSMUSP00000074436; -.
DR MEROPS; S01.972; -.
DR CarbonylDB; Q61646; -.
DR GlyConnect; 717; 1 N-Linked glycan (2 sites).
DR GlyGen; Q61646; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q61646; -.
DR PhosphoSitePlus; Q61646; -.
DR SwissPalm; Q61646; -.
DR CPTAC; non-CPTAC-3406; -.
DR CPTAC; non-CPTAC-3407; -.
DR CPTAC; non-CPTAC-5609; -.
DR jPOST; Q61646; -.
DR MaxQB; Q61646; -.
DR PaxDb; Q61646; -.
DR PeptideAtlas; Q61646; -.
DR PRIDE; Q61646; -.
DR ProteomicsDB; 273170; -.
DR DNASU; 15439; -.
DR Ensembl; ENSMUST00000074898; ENSMUSP00000074436; ENSMUSG00000031722.
DR GeneID; 15439; -.
DR KEGG; mmu:15439; -.
DR UCSC; uc009nin.2; mouse.
DR CTD; 3240; -.
DR MGI; MGI:96211; Hp.
DR VEuPathDB; HostDB:ENSMUSG00000031722; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159903; -.
DR HOGENOM; CLU_006842_0_0_1; -.
DR InParanoid; Q61646; -.
DR OMA; EKQWVNK; -.
DR OrthoDB; 798576at2759; -.
DR PhylomeDB; Q61646; -.
DR TreeFam; TF334326; -.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 15439; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Hp; mouse.
DR PRO; PR:Q61646; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61646; protein.
DR Bgee; ENSMUSG00000031722; Expressed in lacrimal gland and 116 other tissues.
DR ExpressionAtlas; Q61646; baseline and differential.
DR Genevisible; Q61646; MM.
DR GO; GO:0072562; C:blood microparticle; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; ISO:MGI.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR GO; GO:0030492; F:hemoglobin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0002526; P:acute inflammatory response; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0001889; P:liver development; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR008292; Haptoglobin.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24255:SF27; PTHR24255:SF27; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001137; Haptoglobin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW Acute phase; Antibiotic; Antimicrobial; Antioxidant; Disulfide bond;
KW Glycoprotein; Hemoglobin-binding; Immunity; Reference proteome; Secreted;
KW Serine protease homolog; Signal; Sushi.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..347
FT /note="Haptoglobin"
FT /id="PRO_0000028462"
FT CHAIN 19..101
FT /note="Haptoglobin alpha chain"
FT /id="PRO_0000028463"
FT CHAIN 103..347
FT /note="Haptoglobin beta chain"
FT /id="PRO_0000028464"
FT DOMAIN 31..88
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 103..345
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 259..264
FT /note="Interaction with CD163"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 52..86
FT /evidence="ECO:0000250"
FT DISULFID 90..207
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 250..281
FT /evidence="ECO:0000250"
FT DISULFID 292..322
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 38752 MW; 63822D121232F130 CRC64;
MRALGAVVTL LLWGQLFAVE LGNDAMDFED DSCPKPPEIA NGYVEHLVRY RCRQFYRLRA
EGDGVYTLND EKQWVNTVAG EKLPECEAVC GKPKHPVDQV QRIIGGSMDA KGSFPWQAKM
ISRHGLTTGA TLISDQWLLT TAKNLFLNHS ETASAKDITP TLTLYVGKNQ LVEIEKVVLH
PNHSVVDIGL IKLKQRVLVT ERVMPICLPS KDYIAPGRVG YVSGWGRNAN FRFTDRLKYV
MLPVADQDKC VVHYENSTVP EKKNLTSPVG VQPILNEHTF CAGLTKYQED TCYGDAGSAF
AIHDMEEDTW YAAGILSFDK SCAVAEYGVY VRATDLKDWV QETMAKN
