HPT_CAPIB
ID HPT_CAPIB Reviewed; 401 AA.
AC B6E141;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 51.
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 Capra ibex (Ibex).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=72542;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rahman M.M.D., Lecchi C., Miranda-Ribera A., Ceciliani F., Sartorelli P.;
RT "The acute phase reaction during alpine Capra ibex mange.";
RL Submitted (SEP-2008) 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, extracellular space {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; FJ194972; ACI31205.1; -; mRNA.
DR AlphaFoldDB; B6E141; -.
DR SMR; B6E141; -.
DR GO; GO:0005615; C:extracellular space; 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; 2.
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; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS50923; SUSHI; 2.
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; Repeat; Secreted;
KW Serine protease homolog; Signal; Sushi.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..401
FT /note="Haptoglobin"
FT /id="PRO_0000367492"
FT CHAIN 19..155
FT /note="Haptoglobin alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000367493"
FT CHAIN 157..401
FT /note="Haptoglobin beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000367494"
FT DOMAIN 28..83
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 85..142
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 157..399
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 313..318
FT /note="Interaction with CD163"
FT /evidence="ECO:0000250"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 49..81
FT /evidence="ECO:0000250"
FT DISULFID 87
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 106..140
FT /evidence="ECO:0000250"
FT DISULFID 144..261
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 304..335
FT /evidence="ECO:0000250"
FT DISULFID 346..376
FT /evidence="ECO:0000250"
SQ SEQUENCE 401 AA; 44641 MW; B94BBC76F18CBD2B CRC64;
MSALQAVVTL LLCGQLLAVE TGSEAAAGSC PKAPEIANGH VEYSVRYQCD KYYKLRAGNG
VYTFNNKQWI NKDIGLQLPE CEEDVSCPEP PKIKNGYVEY SVRYQCKTYY KLRTCGDGVY
TFNSKKQWIN KNVGQQLPEC EAVCGKPKHP VDQTQRIIGG SLDAKGSLPW QAKMVSHHNL
ISGATLINER WLLTTAKNLY LGHTSDKKAK DITPTLRLYV GKNQLVEVEK VVLHPDHSKV
DIGLIKLREK VPVNDKVMPI CLPSKDYVAV DRVGYVSGWG RNENFNFTGH LKYVMLPVAD
QDKCVKHYEG NNAPKNKTAT SPVGVQPILN ENTFCVGLSK YQEDTCYGDA GSAFVVHDQE
DDTWYAAGIL SFDKSCAVAE YGVYVKVTSI LDWVRKTIAN N
