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 16-JUN-2009, entry version 5. 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; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Cervidae; Cervinae; Cervus. OX NCBI_TaxID=9860; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Rahman M.M.D., Lecchi C., Miranda-Ribera A., Ceciliani F., RA Sartorelli P.; RT "The acute phase proteins in Cervus elaphus."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Haptoglobin combines with free plasma hemoglobin, CC preventing loss of iron through the kidneys and protecting the CC kidneys from damage by hemoglobin, while making the hemoglobin CC accessible to degradative enzymes (By similarity). CC -!- SUBUNIT: Tetramer of two alpha and two beta chains (By CC similarity). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space (By CC similarity). CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- MISCELLANEOUS: The hemoglobin binding site is located in the beta CC chain. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC -!- SIMILARITY: Contains 1 Sushi (CCP/SCR) domain. CC -!- CAUTION: Although homologous to serine proteases, it has lost all CC essential catalytic residues and has no enzymatic activity. 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 GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0030492; F:hemoglobin binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR008292; Haptoglobin. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR000436; Sushi_SCR_CCP. DR PANTHER; PTHR19355:SF42; HaptoGlobin; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PROSITE; PS50923; SUSHI; 2. DR PROSITE; PS50240; TRYPSIN_DOM; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Hemoglobin-binding; Repeat; Secreted; KW Serine protease homolog; Signal; Sushi. FT SIGNAL 1 18 By similarity. FT CHAIN 19 400 Haptoglobin. FT /FTId=PRO_0000367495. FT CHAIN 19 154 Haptoglobin alpha chain (By similarity). FT /FTId=PRO_0000367496. FT CHAIN 156 400 Haptoglobin beta chain (By similarity). FT /FTId=PRO_0000367497. FT DOMAIN 28 83 Sushi 1. FT DOMAIN 84 141 Sushi 2. FT DOMAIN 156 398 Peptidase S1. FT CARBOHYD 285 285 N-linked (GlcNAc...) (Potential). FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential). FT CARBOHYD 315 315 N-linked (GlcNAc...) (Potential). FT DISULFID 30 30 Interchain (By similarity). FT DISULFID 49 81 By similarity. FT DISULFID 86 86 Interchain (By similarity). FT DISULFID 105 139 By similarity. FT DISULFID 143 260 Interchain (between alpha and beta FT chains) (By similarity). FT DISULFID 303 334 By similarity. FT DISULFID 345 375 By similarity. 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 //