ID HPT_CEREL Reviewed; 400 AA. AC B6D985; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 02-DEC-2020, entry version 44. 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 Cervus elaphus (Red deer). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae; OC Cervinae; Cervus. OX NCBI_TaxID=9860; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Rahman M.M.D., Lecchi C., Miranda-Ribera A., Ceciliani F., Sartorelli P.; RT "The acute phase proteins in Cervus elaphus."; RL Submitted (JUL-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 The hemoglobin/haptoglobin complex is composed of a haptoglobin dimer CC bound to two hemoglobin alpha-beta dimers. Interacts with CD163 (By CC similarity). {ECO:0000250}. 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}. 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; EU884574; ACH73014.1; -; mRNA. DR SMR; B6D985; -. 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; 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; 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..400 FT /note="Haptoglobin" FT /id="PRO_0000367495" FT CHAIN 19..154 FT /note="Haptoglobin alpha chain" FT /evidence="ECO:0000250" FT /id="PRO_0000367496" FT CHAIN 156..400 FT /note="Haptoglobin beta chain" FT /evidence="ECO:0000250" FT /id="PRO_0000367497" FT DOMAIN 28..83 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 84..141 FT /note="Sushi 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 156..398 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 312..317 FT /note="Interaction with CD163" FT /evidence="ECO:0000250" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 309 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 315 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 86 FT /note="Interchain" FT /evidence="ECO:0000250" FT DISULFID 105..139 FT /evidence="ECO:0000250" FT DISULFID 143..260 FT /note="Interchain (between alpha and beta chains)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274, FT ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 303..334 FT /evidence="ECO:0000250" FT DISULFID 345..375 FT /evidence="ECO:0000250" SQ SEQUENCE 400 AA; 44690 MW; 6E8281618AB2E448 CRC64; MSALPVVVTL LLCGQLLAVE ISSEATADSC PKAPEIANSH VEYSVRYQCD KYYKLRAGDG VYTFNNKQWI NKDIGQQLPE CEDASCPEPP KIENGYVEHS IRFQCKTYYK LRSAGDGVYT FNSKKQWINK NVGQQLPECE AVCGKPKHPV DQVQRIIGGS LDAKGSFPWQ AKMVSHHNLI SGATLINERW LLTTAKNLYL GHTSDKKAKD IAPTLRLYVG KNQPVEVEKV VLHPDRSKVD IGLIKLRQKV PVNEKVMPIC LPSKDYVAVG RVGYVSGWGR NANFNFTEHL KYIMLPVADQ DKCVEHYENS TVPENKTDKS PVGVQPILNK NTFCVGLSKY QEDTCYGDAG SAFVVHDQED DTWYAAGILS FDKSCAVAEY GVYVKVTSIL DWVRKTIADN //