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Haptoglobin (Zonulin) [Cleaved into: Haptoglobin alpha chain; Haptoglobin beta chain]

 HPT_PONAB               Reviewed;         347 AA.
Q5R5F6; Q5NVR4;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
10-MAY-2017, entry version 67.
RecName: Full=Haptoglobin;
AltName: Full=Zonulin;
Contains:
RecName: Full=Haptoglobin alpha chain;
Contains:
RecName: Full=Haptoglobin beta chain;
Flags: Precursor;
Name=HP;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: As a result of hemolysis, hemoglobin is found to
accumulate in the kidney and is secreted in the urine. Haptoglobin
captures, and combines with free plasma hemoglobin to allow
hepatic recycling of heme iron and to prevent kidney damage.
Haptoglobin also acts as an antioxidant, has antibacterial
activity and plays a role in modulating many aspects of the acute
phase response. Hemoglobin/haptoglobin complexes are rapidely
cleared by the macrophage CD163 scavenger receptor expressed on
the surface of liver Kupfer cells through an endocytic lysosomal
degradation pathway (By similarity). {ECO:0000250}.
-!- FUNCTION: Uncleaved haptoglogin, also known as zonulin, plays a
role in intestinal permeability, allowing intercellular tight
junction disassembly, and controlling the equilibrium between
tolerance and immunity to non-self antigens. {ECO:0000250}.
-!- SUBUNIT: Tetramer of two alpha and two beta chains; disufide-
linked. The Hemoglobin/haptoglobin complex is composed of a
haptoglobin dimer bound to two hemoglobin alpha-beta dimers.
Interacts with CD163 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- DOMAIN: The beta chain mediates most of the interactions with both
subunits of hemoglobin, while the alpha chain forms the
homodimeric interface. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: Although homologous to serine proteases, it has lost all
essential catalytic residues and has no enzymatic activity.
{ECO:0000305}.
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EMBL; CR860905; CAH93010.1; -; mRNA.
EMBL; CR925941; CAI29599.1; -; mRNA.
RefSeq; NP_001126778.1; NM_001133306.1.
ProteinModelPortal; Q5R5F6; -.
SMR; Q5R5F6; -.
STRING; 9601.ENSPPYP00000008491; -.
MEROPS; S01.972; -.
PRIDE; Q5R5F6; -.
GeneID; 100173782; -.
KEGG; pon:100173782; -.
CTD; 3240; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
HOVERGEN; HBG005989; -.
InParanoid; Q5R5F6; -.
KO; K16142; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
GO; GO:0030492; F:hemoglobin binding; IEA:UniProtKB-KW.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
CDD; cd00033; CCP; 1.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR008292; Haptoglobin.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
PANTHER; PTHR24256:SF389; PTHR24256:SF389; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001137; Haptoglobin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS50923; SUSHI; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
2: Evidence at transcript level;
Acute phase; Antibiotic; Antimicrobial; Antioxidant;
Complete proteome; Disulfide bond; Glycoprotein; Hemoglobin-binding;
Immunity; Reference proteome; Secreted; Serine protease homolog;
Signal; Sushi.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 347 Haptoglobin.
/FTId=PRO_0000028477.
CHAIN 19 101 Haptoglobin alpha chain.
/FTId=PRO_0000028478.
CHAIN 103 347 Haptoglobin beta chain.
/FTId=PRO_0000028479.
DOMAIN 31 88 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 103 347 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 259 264 Interaction with CD163. {ECO:0000250}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 33 33 Interchain. {ECO:0000250}.
DISULFID 52 86 {ECO:0000250}.
DISULFID 90 207 Interchain (between alpha and beta
chains). {ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00302}.
DISULFID 250 281 {ECO:0000250}.
DISULFID 292 322 {ECO:0000250}.
CONFLICT 26 26 M -> T (in Ref. 1; CAI29599).
{ECO:0000305}.
CONFLICT 235 235 E -> D (in Ref. 1; CAI29599).
{ECO:0000305}.
SEQUENCE 347 AA; 38496 MW; 29D9494FBDADAFC9 CRC64;
MSALGAVIAL LLWGQLFAVD SGNDVMDISD DGCPKPPQIA HGYVEHSVRY QCKNYYRLRT
EGDGVYTLNS EKQWINKAVG DKLPECEAVC GKPKNPANPV QRILGGHLDA KGSFPWQAKM
VSRHNLTTGA TLINEQWLLT TAKNLFLNHS ENATAKDIAP TLTLYVGKKQ LVEIEKVVLH
PNYSQVDIGL IKLKQKVPVN ERVMPICLPS KDYAEVGRVG YVSGWGRNAN FKFTEHLKYV
MLPVADQDQC VRHYEGSTVP EKKTPKSPVG VQPILNEHTF CAGMSKYQED TCYGDAGSAF
AVHDLEEDTW YAAGILSFDK SCAVAEYGVY VKVTSIQDWV QKTIAKN


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