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

 HPT_HUMAN               Reviewed;         406 AA.
P00738; B0AZL5; P00737; Q0VAC4; Q0VAC5; Q2PP15; Q3B7J0; Q6LBY9;
Q9UC67;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 195.
RecName: Full=Haptoglobin;
AltName: Full=Zonulin;
Contains:
RecName: Full=Haptoglobin alpha chain;
Contains:
RecName: Full=Haptoglobin beta chain;
Flags: Precursor;
Name=HP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6688992;
van der Straten A., Herzog A., Jacobs P., Cabezon T., Bollen A.;
"Molecular cloning of human haptoglobin cDNA: evidence for a single
mRNA coding for alpha 2 and beta chains.";
EMBO J. 2:1003-1007(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6310599; DOI=10.1073/pnas.80.19.5875;
Yang F., Brune J.L., Baldwin W.D., Barnett D.R., Bowman B.H.;
"Identification and characterization of human haptoglobin cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:5875-5879(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS 29-ALA--GLU-87 DEL; ASP-129
AND LYS-130.
TISSUE=Liver;
PubMed=6546723; DOI=10.1016/0014-5793(84)80215-X;
van der Straten A., Herzog A., Cabezon T., Bollen A.;
"Characterization of human haptoglobin cDNAs coding for alpha 2FS beta
and alpha 1S beta variants.";
FEBS Lett. 168:103-107(1984).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT 29-ALA--GLU-87 DEL.
PubMed=6330675; DOI=10.1093/nar/12.11.4531;
Brune J.L., Yang F., Barnett D.R., Bowman B.H.;
"Evolution of haptoglobin: comparison of complementary DNA encoding Hp
alpha 1S and Hp alpha 2FS.";
Nucleic Acids Res. 12:4531-4538(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-129.
PubMed=4018023;
Bensi G., Raugei G., Klefenz H., Cortese R.;
"Structure and expression of the human haptoglobin locus.";
EMBO J. 4:119-126(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2987228;
Maeda N.;
"Nucleotide sequence of the haptoglobin and haptoglobin-related gene
pair. The haptoglobin-related gene contains a retrovirus-like
element.";
J. Biol. Chem. 260:6698-6709(1985).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1478675; DOI=10.1016/S0888-7543(05)80116-8;
Erickson L.M., Kim H.S., Maeda N.;
"Junctions between genes in the haptoglobin gene cluster of
primates.";
Genomics 14:948-958(1992).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES HP*1F AND HP*1S).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-19.
PubMed=3519135; DOI=10.1089/dna.1986.5.129;
van der Straten A., Falque J.-C., Loriau R., Bollen A., Cabezon T.;
"Expression of cloned human haptoglobin and alpha 1-antitrypsin
complementary DNAs in Saccharomyces cerevisiae.";
DNA 5:129-136(1986).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-406.
PubMed=6310515; DOI=10.1093/nar/11.17.5811;
Raugei G., Bensi G., Colantuoni V., Romano V., Santoro C.,
Costanzo F., Cortese R.;
"Sequence of human haptoglobin cDNA: evidence that the alpha and beta
subunits are coded by the same mRNA.";
Nucleic Acids Res. 11:5811-5819(1983).
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 3-406.
PubMed=10493829; DOI=10.1006/geno.1999.5927;
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
Harris P.C., Venter J.C., Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from
human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-375.
PubMed=6325933; DOI=10.1038/309131a0;
Maeda N., Yang F., Barnett D.R., Bowman B.H., Smithies O.;
"Duplication within the haptoglobin Hp2 gene.";
Nature 309:131-135(1984).
[16]
PROTEIN SEQUENCE OF 19-28; 88-160 AND 162-406, AND DISULFIDE BONDS.
PubMed=6997877; DOI=10.1073/pnas.77.6.3388;
Kurosky A., Barnett D.R., Lee T.-H., Touchstone B., Hay R.E.,
Arnott M.S., Bowman B.H., Fitch W.M.;
"Covalent structure of human haptoglobin: a serine protease homolog.";
Proc. Natl. Acad. Sci. U.S.A. 77:3388-3392(1980).
[17]
PROTEIN SEQUENCE OF 162-176.
TISSUE=Eye;
PubMed=7637327;
Kliffen M., de Jong P.T.V.M., Luider T.M.;
"Protein analysis of human maculae in relation to age-related
maculopathy.";
Lab. Invest. 73:267-272(1995).
[18]
DISULFIDE BONDS.
PubMed=4573324;
Malchy B., Dixon G.H.;
"Studies on the interchain disulfides of human haptoglobins.";
Can. J. Biochem. 51:249-264(1973).
[19]
GLYCOSYLATION AT ASN-207 AND ASN-241.
TISSUE=Plasma, and Serum;
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-207; ASN-211 AND
ASN-241.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-207; ASN-211 AND
ASN-241.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-207 AND ASN-211.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-207; ASN-211 AND
ASN-241.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[24]
GLYCOSYLATION AT ASN-184 AND ASN-241.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[25]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241, AND STRUCTURE OF
CARBOHYDRATE.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[26]
IDENTIFICATION AS ZONULIN.
PubMed=19805376; DOI=10.1073/pnas.0906773106;
Tripathi A., Lammers K.M., Goldblum S., Shea-Donohue T.,
Netzel-Arnett S., Buzza M.S., Antalis T.M., Vogel S.N., Zhao A.,
Yang S., Arrietta M.C., Meddings J.B., Fasano A.;
"Identification of human zonulin, a physiological modulator of tight
junctions, as prehaptoglobin-2.";
Proc. Natl. Acad. Sci. U.S.A. 106:16799-16804(2009).
[27]
REVIEW.
PubMed=19659435; DOI=10.1089/ars.2009.2793;
Levy A.P., Asleh R., Blum S., Levy N.S., Miller-Lotan R.,
Kalet-Litman S., Anbinder Y., Lache O., Nakhoul F.M., Asaf R.,
Farbstein D., Pollak M., Soloveichik Y.Z., Strauss M., Alshiek J.,
Livshits A., Schwartz A., Awad H., Jad K., Goldenstein H.;
"Haptoglobin: basic and clinical aspects.";
Antioxid. Redox Signal. 12:293-304(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
FUNCTION OF ZONULIN.
PubMed=21248165; DOI=10.1152/physrev.00003.2008;
Fasano A.;
"Zonulin and its regulation of intestinal barrier function: the
biological door to inflammation, autoimmunity, and cancer.";
Physiol. Rev. 91:151-175(2011).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
VARIANT AHP THR-247, AND CHARACTERIZATION OF VARIANT AHP THR-247.
PubMed=14999562; DOI=10.1007/s00439-004-1098-6;
Teye K., Quaye I.K., Koda Y., Soejima M., Pang H., Tsuneoka M.,
Amoah A.G., Adjei A., Kimura H.;
"A novel I247T missense mutation in the haptoglobin 2 beta-chain
decreases the expression of the protein and is associated with
ahaptoglobinemia.";
Hum. Genet. 114:499-502(2004).
-!- 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 Antimicrobial; 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.
{ECO:0000269|PubMed:21248165}.
-!- 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:0000269|PubMed:21248165}.
-!- 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.
-!- INTERACTION:
P02647:APOA1; NbExp=3; IntAct=EBI-1220767, EBI-701692;
P02649:APOE; NbExp=7; IntAct=EBI-1220767, EBI-1222467;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00738-1; Sequence=Displayed;
Name=2;
IsoId=P00738-2; Sequence=VSP_055024;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- POLYMORPHISM: In the human populations there are two major allelic
forms, alpha-1 (1-1) with 83 residues and alpha-2 (2-2) with 142
residues. These alleles determine 3 possible genotypes, homozygous
(1-1 or 2-2) and heterozygous (2-1), and 3 major phenotypes
HP*1F/HP*1S and HP*2FS. The two main alleles of HP*1 are called
HP*1F (fast) and HP*1S (slow). The alleles exhibit different
oligomerization properties. In healthy males, but not in females,
the Hp 2-2 phenotype is associated with higher serum iron,
decreased Antimicrobial; Antioxidant capability, and less
efficient clearance from the circulation, than Hp 1-1 and 2-1.
{ECO:0000269|PubMed:4018023, ECO:0000269|PubMed:6330675,
ECO:0000269|PubMed:6546723}.
-!- DISEASE: Anhaptoglobinemia (AHP) [MIM:614081]: A condition
characterized by the absence of the serum glycoprotein
haptoglobin. Serum levels of haptoglobin vary among normal
persons: levels are low in the neonatal period and in the elderly,
differ by population, and can be influenced by environmental
factors, such as infection. Secondary hypohaptoglobinemia can
occur as a consequence of hemolysis, during which haptoglobin
binds to free hemoglobin. Congenital haptoglobin deficiency is a
risk factor for anaphylactic non-hemolytic transfusion reactions.
{ECO:0000269|PubMed:14999562}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HP";
-!- WEB RESOURCE: Name=Wikipedia; Note=Haptoglobin entry;
URL="https://en.wikipedia.org/wiki/Haptoglobin";
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EMBL; K00422; AAA52687.1; -; mRNA.
EMBL; K01763; AAA52684.1; -; mRNA.
EMBL; L29394; AAA52685.1; -; mRNA.
EMBL; X00637; CAA25267.1; -; mRNA.
EMBL; X01793; CAA25926.1; -; Genomic_DNA.
EMBL; X01786; CAA25926.1; JOINED; Genomic_DNA.
EMBL; X02206; CAA25926.1; JOINED; Genomic_DNA.
EMBL; X01789; CAA25926.1; JOINED; Genomic_DNA.
EMBL; X01791; CAA25926.1; JOINED; Genomic_DNA.
EMBL; M10935; AAA88080.1; -; Genomic_DNA.
EMBL; M69197; AAA88078.1; -; Genomic_DNA.
EMBL; AK314700; BAF98793.1; -; mRNA.
EMBL; DQ314870; ABC40729.1; -; Genomic_DNA.
EMBL; AC004682; AAC27432.1; -; Genomic_DNA.
EMBL; AC009087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC107587; AAI07588.1; -; mRNA.
EMBL; BC121124; AAI21125.1; -; mRNA.
EMBL; BC121125; AAI21126.1; -; mRNA.
EMBL; M13192; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X00606; CAA25248.1; -; Genomic_DNA.
CCDS; CCDS45524.1; -. [P00738-1]
CCDS; CCDS45525.1; -. [P00738-2]
PIR; A92532; HPHU2.
PIR; A93521; HPHU1.
RefSeq; NP_001119574.1; NM_001126102.2. [P00738-2]
RefSeq; NP_001305067.1; NM_001318138.1.
RefSeq; NP_005134.1; NM_005143.4. [P00738-1]
UniGene; Hs.513711; -.
UniGene; Hs.702099; -.
PDB; 4WJG; X-ray; 3.10 A; 2/C/H/M/R/W=92-406.
PDB; 4X0L; X-ray; 2.05 A; C=148-406.
PDB; 5HU6; X-ray; 2.90 A; C=148-406.
PDBsum; 4WJG; -.
PDBsum; 4X0L; -.
PDBsum; 5HU6; -.
ProteinModelPortal; P00738; -.
SMR; P00738; -.
BioGrid; 109480; 27.
IntAct; P00738; 18.
STRING; 9606.ENSP00000348170; -.
MEROPS; S01.972; -.
iPTMnet; P00738; -.
PhosphoSitePlus; P00738; -.
SwissPalm; P00738; -.
UniCarbKB; P00738; -.
BioMuta; HP; -.
DMDM; 123508; -.
DOSAC-COBS-2DPAGE; P00738; -.
SWISS-2DPAGE; P00738; -.
EPD; P00738; -.
MaxQB; P00738; -.
PaxDb; P00738; -.
PeptideAtlas; P00738; -.
PRIDE; P00738; -.
DNASU; 3240; -.
Ensembl; ENST00000355906; ENSP00000348170; ENSG00000257017. [P00738-1]
Ensembl; ENST00000398131; ENSP00000381199; ENSG00000257017. [P00738-2]
Ensembl; ENST00000570083; ENSP00000457629; ENSG00000257017. [P00738-2]
GeneID; 3240; -.
KEGG; hsa:3240; -.
UCSC; uc002fbr.5; human. [P00738-1]
CTD; 3240; -.
DisGeNET; 3240; -.
EuPathDB; HostDB:ENSG00000257017.8; -.
GeneCards; HP; -.
HGNC; HGNC:5141; HP.
HPA; CAB003787; -.
HPA; HPA047750; -.
MalaCards; HP; -.
MIM; 140100; gene.
MIM; 614081; phenotype.
neXtProt; NX_P00738; -.
OpenTargets; ENSG00000257017; -.
PharmGKB; PA29415; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118890; -.
HOGENOM; HOG000112945; -.
HOVERGEN; HBG005989; -.
InParanoid; P00738; -.
KO; K16142; -.
PhylomeDB; P00738; -.
TreeFam; TF334326; -.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P00738; -.
GeneWiki; Haptoglobin; -.
GenomeRNAi; 3240; -.
PRO; PR:P00738; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000257017; -.
CleanEx; HS_HP; -.
ExpressionAtlas; P00738; baseline and differential.
Genevisible; P00738; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
GO; GO:0030492; F:hemoglobin binding; IDA:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; TAS:ProtInc.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:2000296; P:negative regulation of hydrogen peroxide catabolic process; IDA:BHF-UCL.
GO; GO:0051354; P:negative regulation of oxidoreductase activity; IDA:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:BHF-UCL.
CDD; cd00033; CCP; 2.
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.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Alternative splicing; Antibiotic;
Antimicrobial; Antioxidant; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hemoglobin-binding; Immunity; Polymorphism;
Reference proteome; Repeat; Secreted; Serine protease homolog; Signal;
Sushi.
SIGNAL 1 18 {ECO:0000269|PubMed:6997877}.
CHAIN 19 406 Haptoglobin.
/FTId=PRO_0000028456.
CHAIN 19 160 Haptoglobin alpha chain.
/FTId=PRO_0000028457.
CHAIN 162 406 Haptoglobin beta chain.
/FTId=PRO_0000028458.
DOMAIN 31 88 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 90 147 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 162 404 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 318 323 Interaction with CD163. {ECO:0000250}.
CARBOHYD 184 184 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19159218}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19159218}.
CARBOHYD 241 241 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
DISULFID 33 33 Interchain.
DISULFID 52 86
DISULFID 92 92 Interchain.
DISULFID 111 145
DISULFID 149 266 Interchain (between alpha and beta
chains).
DISULFID 309 340
DISULFID 351 381
VAR_SEQ 38 96 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_055024.
VARIANT 29 87 Missing (in allele HP*1F and allele
HP*1S). {ECO:0000269|PubMed:6330675,
ECO:0000269|PubMed:6546723}.
/FTId=VAR_017112.
VARIANT 129 129 N -> D (in allele HP*1F;
dbSNP:rs199926732).
{ECO:0000269|PubMed:4018023,
ECO:0000269|PubMed:6546723}.
/FTId=VAR_005294.
VARIANT 130 130 E -> K (in allele HP*1F;
dbSNP:rs200877317).
{ECO:0000269|PubMed:6546723}.
/FTId=VAR_017113.
VARIANT 247 247 I -> T (in AHP; causes reduced expression
of the protein; dbSNP:rs104894517).
{ECO:0000269|PubMed:14999562}.
/FTId=VAR_066214.
VARIANT 397 397 D -> H (in dbSNP:rs12646).
/FTId=VAR_017114.
CONFLICT 70 70 D -> N (in Ref. 2; AAA52687).
{ECO:0000305}.
CONFLICT 130 130 E -> G (in Ref. 11; AAI07588).
{ECO:0000305}.
STRAND 101 111 {ECO:0000244|PDB:4WJG}.
STRAND 115 121 {ECO:0000244|PDB:4WJG}.
STRAND 123 127 {ECO:0000244|PDB:4WJG}.
STRAND 133 135 {ECO:0000244|PDB:4WJG}.
TURN 136 138 {ECO:0000244|PDB:4WJG}.
STRAND 144 147 {ECO:0000244|PDB:4WJG}.
STRAND 163 167 {ECO:0000244|PDB:4X0L}.
STRAND 176 180 {ECO:0000244|PDB:4X0L}.
STRAND 186 193 {ECO:0000244|PDB:4X0L}.
STRAND 196 199 {ECO:0000244|PDB:4X0L}.
HELIX 201 204 {ECO:0000244|PDB:4X0L}.
TURN 205 207 {ECO:0000244|PDB:4X0L}.
HELIX 214 217 {ECO:0000244|PDB:4X0L}.
HELIX 218 220 {ECO:0000244|PDB:4X0L}.
STRAND 222 225 {ECO:0000244|PDB:4X0L}.
TURN 226 228 {ECO:0000244|PDB:4X0L}.
STRAND 229 231 {ECO:0000244|PDB:4X0L}.
STRAND 233 238 {ECO:0000244|PDB:4X0L}.
TURN 240 244 {ECO:0000244|PDB:4X0L}.
STRAND 248 254 {ECO:0000244|PDB:4X0L}.
STRAND 259 261 {ECO:0000244|PDB:5HU6}.
STRAND 278 283 {ECO:0000244|PDB:4X0L}.
STRAND 290 292 {ECO:0000244|PDB:4X0L}.
STRAND 297 303 {ECO:0000244|PDB:4X0L}.
HELIX 306 314 {ECO:0000244|PDB:4X0L}.
HELIX 319 321 {ECO:0000244|PDB:4X0L}.
STRAND 327 330 {ECO:0000244|PDB:4WJG}.
STRAND 338 341 {ECO:0000244|PDB:4X0L}.
STRAND 358 363 {ECO:0000244|PDB:4X0L}.
TURN 364 367 {ECO:0000244|PDB:4X0L}.
STRAND 368 377 {ECO:0000244|PDB:4X0L}.
TURN 381 383 {ECO:0000244|PDB:4X0L}.
STRAND 387 391 {ECO:0000244|PDB:4X0L}.
HELIX 392 394 {ECO:0000244|PDB:4X0L}.
HELIX 396 405 {ECO:0000244|PDB:4X0L}.
SEQUENCE 406 AA; 45205 MW; A98B56B2B1BE891E CRC64;
MSALGAVIAL LLWGQLFAVD SGNDVTDIAD DGCPKPPEIA HGYVEHSVRY QCKNYYKLRT
EGDGVYTLND KKQWINKAVG DKLPECEADD GCPKPPEIAH GYVEHSVRYQ CKNYYKLRTE
GDGVYTLNNE KQWINKAVGD KLPECEAVCG KPKNPANPVQ RILGGHLDAK GSFPWQAKMV
SHHNLTTGAT LINEQWLLTT AKNLFLNHSE NATAKDIAPT LTLYVGKKQL VEIEKVVLHP
NYSQVDIGLI KLKQKVSVNE RVMPICLPSK DYAEVGRVGY VSGWGRNANF KFTDHLKYVM
LPVADQDQCI RHYEGSTVPE KKTPKSPVGV QPILNEHTFC AGMSKYQEDT CYGDAGSAFA
VHDLEEDTWY ATGILSFDKS CAVAEYGVYV KVTSIQDWVQ KTIAEN


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