HPT_MUSSA
ID HPT_MUSSA Reviewed; 347 AA.
AC Q62558;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 23-FEB-2022, entry version 99.
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 saxicola (Brown spiny mouse) (Rock-loving mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Pyromys.
OX NCBI_TaxID=10094;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Pajovic S., Jones V.E., Prowse K.R., Berger F.G., Baumann H.;
RT "Evolution of mouse haptoglobin genes.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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; L10353; AAB65440.1; -; mRNA.
DR MEROPS; S01.972; -.
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; 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 2: Evidence at transcript level;
KW Acute phase; Antibiotic; Antimicrobial; Antioxidant; Disulfide bond;
KW Glycoprotein; Hemoglobin-binding; Immunity; 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_0000028468"
FT CHAIN 19..101
FT /note="Haptoglobin alpha chain"
FT /id="PRO_0000028469"
FT CHAIN 103..347
FT /note="Haptoglobin beta chain"
FT /id="PRO_0000028470"
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:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 38795 MW; BC61D78B634A7ECE CRC64;
MRALGAVVTL LLWGQLFAAE LGNDAMDFED DSCPKPPEIA NGYVEHLVRY RCRQFYRLRT
EGDGVYTLND EKQWVNTAAG EKLPECEAVC GKPKHPVVQV QRIIGGSMDA KGSFPWQAKM
ISRHGLTTGA TLISDQWLLT TAKNLFLNHS ETASAKDIAP TLTLYVGKNQ LVEIEKVVLH
PNHSVVDIGL IKLKQRVLVT ERVMPICLPS KDYVAPGRVG YLSGWGRNVN FRFTERFKYV
MLPVADQDKC VVHYENSTVP EKKNFTSPVG VQPILNEHTF CVGLSRYQED TCYGDAGSAF
AIHDMEEDTW XAAGILSFDK SCAVAEYGVY VRATDLKDWV QETMAKK
