ID   HPTR_PANTR              Reviewed;         346 AA.
AC   Q28801; Q28804;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Haptoglobin-related protein;
DE   Flags: Fragment;
GN   Name=HPR;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1478675; DOI=10.1016/s0888-7543(05)80116-8;
RA   Erickson L.M., Kim H.S., Maeda N.;
RT   "Junctions between genes in the haptoglobin gene cluster of primates.";
RL   Genomics 14:948-958(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-346.
RX   PubMed=3170608; DOI=10.1016/s0021-9258(19)37650-1;
RA   McEvoy S.M., Maeda N.;
RT   "Complex events in the evolution of the haptoglobin gene cluster in
RT   primates.";
RL   J. Biol. Chem. 263:15740-15747(1988).
CC   -!- FUNCTION: Primate-specific plasma protein associated with
CC       apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL).
CC       Binds hemoglobin with high affinity and may contribute to the clearance
CC       of cell-free hemoglobin to allow hepatic recycling of heme iron.
CC       {ECO:0000250|UniProtKB:P00739}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00739}.
CC       Note=Secreted into blood plasma and associated with subtypes of high
CC       density lipoproteins (HDL). {ECO:0000250|UniProtKB:P00739}.
CC   -!- DOMAIN: The uncleaved signal sequence interacts with HDL fluid lipids
CC       and mediates incorporation into the HDL particle.
CC       {ECO:0000250|UniProtKB:P00739}.
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; M84463; AAA70197.1; -; Genomic_DNA.
DR   EMBL; M20761; AAA35413.1; -; Genomic_DNA.
DR   PIR; I36942; I36942.
DR   AlphaFoldDB; Q28801; -.
DR   SMR; Q28801; -.
DR   MEROPS; S01.972; -.
DR   PaxDb; Q28801; -.
DR   PRIDE; Q28801; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; Q28801; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0010942; P:positive regulation of cell death; IBA:GO_Central.
DR   GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
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; 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   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hemoglobin-binding; Reference proteome; Secreted;
KW   Serine protease homolog; Signal; Sushi.
FT   CHAIN           <1..346
FT                   /note="Haptoglobin-related protein"
FT                   /id="PRO_0000028487"
FT   SIGNAL          <1..16
FT                   /note="Not cleaved"
FT                   /evidence="ECO:0000250|UniProtKB:P00739"
FT   DOMAIN          32..85
FT                   /note="Sushi"
FT   DOMAIN          102..344
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        249..280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        291..321
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        122
FT                   /note="R -> H (in Ref. 2; AAA35413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147
FT                   /note="S -> N (in Ref. 2; AAA35413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="S -> I (in Ref. 2; AAA35413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="R -> P (in Ref. 2; AAA35413)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   346 AA;  38867 MW;  F7E54E93E53E34FB CRC64;
     DLGAVIYLLL WGRQLFALYS SNDVTDISDD RFPKPPEIAN GYVEHLFRYQ RKNYYRLRTE
     GDGVYTLNDK KQWINKAVGD KLPECEAVCG KPKNPANPVQ RILGGHLDAK GSFPWQAKMV
     SRHNLTTGAT LINEQWLLTT AKNLFLSHSE NATAKDSAPT LTLYVGKKQL VEIEKVVLHP
     NYHQVDIGLI KLKQKVLVNE RVMPICLPSK NYAEVGRVGY VSGWGQSNNF KLTDHLKYVM
     LPVADQDQCI RHYEGSTVPE KKTPKSPVGV QPILNEHTFC AGMSKYQEDT CYGDAGSAFA
     VHDLEEDTWY AAGILSFDKS CAVAEYGVYV KVTSIHVWVQ KTIAEN