HPT_CANLF
ID HPT_CANLF Reviewed; 329 AA.
AC P19006; Q9TRH6; Q9TRH7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Haptoglobin;
DE Contains:
DE RecName: Full=Haptoglobin alpha chain;
DE Contains:
DE RecName: Full=Haptoglobin beta chain;
GN Name=HP;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-9; ASN-107 AND ASN-214.
RX PubMed=1429498; DOI=10.1093/oxfordjournals.jbchem.a123847;
RA Kumazaki T., Urushibara N., Ishii S.;
RT "Amino acid sequence and disulfide-bridge location of canine haptoglobin.";
RL J. Biochem. 112:11-19(1992).
RN [2]
RP PROTEIN SEQUENCE OF 85-124.
RX PubMed=975782; DOI=10.1016/0305-0491(76)90320-5;
RA Kurosky A., Kim H.H., Touchstone B.;
RT "Comparative sequence analysis of the N-terminal region of rat, rabbit, and
RT dog haptoglobin beta-chains.";
RL Comp. Biochem. Physiol. 55B:453-459(1976).
RN [3]
RP PROTEIN SEQUENCE OF 1-20 AND 85-104.
RX PubMed=8461423; DOI=10.1292/jvms.55.27;
RA Tosa N., Morimatsu M., Nakagawa M., Miyoshi F., Uchida E., Niiyama M.,
RA Syuto B., Saito M.;
RT "Purification and identification of a serum protein increased by
RT anthelmintic drugs for Dirofilaria immitis in dogs.";
RL J. Vet. Med. Sci. 55:27-31(1993).
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.
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 PIR; JX0223; HPDG.
DR AlphaFoldDB; P19006; -.
DR SMR; P19006; -.
DR STRING; 9612.ENSCAFP00000029992; -.
DR MEROPS; S01.972; -.
DR iPTMnet; P19006; -.
DR UCD-2DPAGE; P19006; -.
DR PaxDb; P19006; -.
DR PRIDE; P19006; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P19006; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR GO; GO:0030492; F:hemoglobin binding; IEA:UniProtKB-KW.
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:0010942; P:positive regulation of cell death; IBA:GO_Central.
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;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemoglobin-binding; Immunity; Reference proteome; Secreted;
KW Serine protease homolog; Sushi.
FT CHAIN 1..329
FT /note="Haptoglobin"
FT /id="PRO_0000028452"
FT CHAIN 1..83
FT /note="Haptoglobin alpha chain"
FT /id="PRO_0000028453"
FT PROPEP 84
FT /evidence="ECO:0000269|PubMed:8461423,
FT ECO:0000269|PubMed:975782"
FT /id="PRO_0000028454"
FT CHAIN 85..329
FT /note="Haptoglobin beta chain"
FT /id="PRO_0000028455"
FT DOMAIN 13..70
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 85..327
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 241..246
FT /note="Interaction with CD163"
FT /evidence="ECO:0000250"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1429498"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1429498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1429498"
FT DISULFID 34..68
FT /evidence="ECO:0000269|PubMed:1429498"
FT DISULFID 72..189
FT /note="Interchain (between alpha and beta chains)"
FT DISULFID 232..263
FT /evidence="ECO:0000269|PubMed:1429498"
FT DISULFID 274..304
FT /evidence="ECO:0000269|PubMed:1429498"
SQ SEQUENCE 329 AA; 36457 MW; 86E32CA3E9CC2C48 CRC64;
EDTGSEATNN TEVSLPKPPV IENGYVEHMI RYQCKPFYKL HTEGDGVYTL NSEKHWTNKA
VGEKLPECEA VCGKPKNPVD QVQRIMGGSV DAKGSFPWQA KMVSHHNLTS GATLINEQWL
LTTAKNLFLG HKDDAKANDI APTLKLYVGK NQLVEVEKVV LHPDYSKVDI GLIKLKQKVP
IDERVMPICL PSKDYAEVGR IGYVSGWGRN SNFNFTELLK YVMLPVADQD KCVQHYEGST
VPEKKSPKSP VGVQPILNEH TFCAGMSKFQ EDTCYGDAGS AFAVHDQDED TWYAAGILSF
DKSCTVAEYG VYVKVPSVLA WVQETIAGN
