HPT_MESAU
ID HPT_MESAU Reviewed; 346 AA.
AC O35086;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 108.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9629670; DOI=10.1016/s0305-0491(97)00363-5;
RA Yamamoto K., Matsui I., Nakatani T., Matsuura K., Sinohara H.;
RT "Cloning and sequencing of cDNA encoding haptoglobin, an acute phase
RT protein in Syrian hamster, Mesacricetus auratus.";
RL Comp. Biochem. Physiol. 119B:375-379(1998).
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}.
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 EMBL; AB006130; BAA21723.1; -; mRNA.
DR RefSeq; NP_001268308.1; NM_001281379.1.
DR AlphaFoldDB; O35086; -.
DR SMR; O35086; -.
DR STRING; 10036.XP_005073078.1; -.
DR MEROPS; S01.972; -.
DR GeneID; 101841186; -.
DR CTD; 3240; -.
DR eggNOG; KOG3627; Eukaryota.
DR OrthoDB; 798576at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR GO; GO:0030492; F:hemoglobin binding; IEA:UniProtKB-KW.
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 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; 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 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 2: Evidence at transcript 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..346
FT /note="Haptoglobin"
FT /id="PRO_0000028459"
FT CHAIN 19..100
FT /note="Haptoglobin alpha chain"
FT /id="PRO_0000028460"
FT CHAIN 102..346
FT /note="Haptoglobin beta chain"
FT /id="PRO_0000028461"
FT DOMAIN 31..87
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 102..344
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 258..263
FT /note="Interaction with CD163"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 52..85
FT /evidence="ECO:0000250"
FT DISULFID 89..206
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 249..280
FT /evidence="ECO:0000250"
FT DISULFID 291..321
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 38602 MW; C59132AFBCDDC525 CRC64;
MRALGAVVTL LLWGQLFAVD LSNDAMDTAD DSCPKPPEIE NGYVEHLVRY RCQHYRLRTE
GDGVYTLNSE KQWVNTAAGE RLPECEAVCG KPKHPVDQVQ RIIGGSLDAK GSFPWQAKMV
SRHELITGAT LISDQWLLTT AKNLFLNHSE DATSKDIAPT LKLYVGKMQP VEIEKVVIHP
NRSVVDIGVI KLRQKVPVNE RVMPICLPSK DYIAPGRMGY VSGWGRNANF RFTDRLKYVM
LPVADQDSCM LHYEGSTVPE KEGSKSSVGV QPILNEHTFC AGMTKYQEDT CYGDAGSAFA
IHDLEQDTWY AAGILSFDKS CSVAEYGVYV KVNSFLDWIQ ETMAKN
