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Inter-alpha-trypsin inhibitor heavy chain H1 (ITI heavy chain H1) (ITI-HC1) (Inter-alpha-inhibitor heavy chain 1) (Inter-alpha-trypsin inhibitor complex component III) (Serum-derived hyaluronan-associated protein) (SHAP)

 ITIH1_HUMAN             Reviewed;         911 AA.
P19827; A8K9N5; B2RAH9; B7Z558; B7Z8C0; F5H165; F5H7Y8; P78455;
Q01746; Q562G1;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 3.
25-OCT-2017, entry version 174.
RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H1;
Short=ITI heavy chain H1;
Short=ITI-HC1;
Short=Inter-alpha-inhibitor heavy chain 1;
AltName: Full=Inter-alpha-trypsin inhibitor complex component III;
AltName: Full=Serum-derived hyaluronan-associated protein;
Short=SHAP;
Flags: Precursor;
Name=ITIH1; Synonyms=IGHEP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-263; VAL-585
AND ARG-595.
TISSUE=Blood, and Liver;
PubMed=1380832; DOI=10.1016/0167-4781(92)90065-8;
Diarra-Mehrpour M., Bourguignon J., Bost F., Sesboue R., Muschio F.,
Sarafan N., Martin J.-P.;
"Human inter-alpha-trypsin inhibitor: full-length cDNA sequence of the
heavy chain H1.";
Biochim. Biophys. Acta 1132:114-118(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7505744; DOI=10.1111/j.1432-1033.1993.tb18376.x;
Bost F., Bourguignon J., Martin J.-P., Sesboue R., Thiberville L.,
Diarra-Mehrpour M.;
"Isolation and characterization of the human inter-alpha-trypsin
inhibitor heavy-chain H1 gene.";
Eur. J. Biochem. 218:283-291(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANTS VAL-585 AND ARG-595.
TISSUE=Liver, and Thymus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
PROTEIN SEQUENCE OF 30-34; 117-119; 126-137; 318-329; 342-355 AND
478-501.
TISSUE=Plasma;
PubMed=1384548;
Malki N., Balduyck M., Maes P., Capon C., Mizon C., Han K.K.,
Tartar A., Fournet B., Mizon J.;
"The heavy chains of human plasma inter-alpha-trypsin inhibitor: their
isolation, their identification by electrophoresis and partial
sequencing. Differential reactivity with concanavalin A.";
Biol. Chem. Hoppe-Seyler 373:1009-1018(1992).
[8]
PROTEIN SEQUENCE OF 35-54; 110-124; 333-347 AND 399-435.
TISSUE=Plasma;
PubMed=2476436;
Enghild J.J., Thoegersen I.B., Pizzo S.V., Salvesen G.;
"Analysis of inter-alpha-trypsin inhibitor and a novel trypsin
inhibitor, pre-alpha-trypsin inhibitor, from human plasma. Polypeptide
chain stoichiometry and assembly by glycan.";
J. Biol. Chem. 264:15975-15981(1989).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 75-911 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Liver;
PubMed=2471637; DOI=10.1111/j.1432-1033.1989.tb14762.x;
Gebhard W., Schreitmueller T., Hochstrasser K., Wachter E.;
"Two out of the three kinds of subunits of inter-alpha-trypsin
inhibitor are structurally related.";
Eur. J. Biochem. 181:571-576(1989).
[10]
PROTEIN SEQUENCE OF 177-211 AND 387-428, AND HYALURONAN BINDING.
TISSUE=Serum;
PubMed=7504674;
Huang L., Yoneda M., Kimata K.;
"A serum-derived hyaluronan-associated protein (SHAP) is the heavy
chain of the inter alpha-trypsin inhibitor.";
J. Biol. Chem. 268:26725-26730(1993).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 399-723 (ISOFORM 1/2/3).
PubMed=2446322; DOI=10.1073/pnas.84.23.8272;
Salier J.-P., Diarra-Mehrpour M., Sesboue R., Bourguignon J.,
Benarous R., Ohkubo I., Kurachi S., Kurachi K., Martin J.-P.;
"Isolation and characterization of cDNAs encoding the heavy chain of
human inter-alpha-trypsin inhibitor (I alpha TI): unambiguous evidence
for multipolypeptide chain structure of I alpha TI.";
Proc. Natl. Acad. Sci. U.S.A. 84:8272-8276(1987).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 535-685 (ISOFORM 1/2/3).
PubMed=3663330;
Schreitmueller T., Hochstrasser K., Resinger P.W.M., Wachter E.,
Gebhard W.;
"cDNA cloning of human inter-alpha-trypsin inhibitor discloses three
different proteins.";
Biol. Chem. Hoppe-Seyler 368:963-970(1987).
[13]
PROTEIN SEQUENCE OF 669-672, AND COVALENT LINKAGE WITH CHONDROITIN
SULFATE.
TISSUE=Plasma;
PubMed=7513643; DOI=10.1111/j.1432-1033.1994.tb18803.x;
Morelle W., Capon C., Balduyck M., Sautiere P., Kouach M.,
Michalski C., Fournet B., Mizon J.;
"Chondroitin sulphate covalently cross-links the three polypeptide
chains of inter-alpha-trypsin inhibitor.";
Eur. J. Biochem. 221:881-888(1994).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 870-911.
PubMed=7522574; DOI=10.1016/0167-4781(94)90087-6;
Diarra-Mehrpour M., Bourguignon J., Sarafan N., Bost F., Sesbouee R.,
Muschio-Bonnet F., Martin J.-P.;
"Tandem orientation of the inter-alpha-trypsin inhibitor heavy chain
H1 and H3 genes.";
Biochim. Biophys. Acta 1219:551-554(1994).
[15]
GLYCOSYLATION AT ASN-285 AND ASN-588, AND MASS SPECTROMETRY.
PubMed=9677337; DOI=10.1042/bj3330749;
Flahaut C., Capon C., Balduyck M., Ricart G., Sautiere P., Mizon J.;
"Glycosylation pattern of human inter-alpha-inhibitor heavy chains.";
Biochem. J. 333:749-756(1998).
[16]
GLYCOSYLATION AT CYS-60; ASN-285; ASN-588 AND THR-653, DISULFIDE
BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=9425062; DOI=10.1021/bi971137d;
Olsen E.H.N., Rahbek-Nielsen H., Thoegersen I.B., Roepstorff P.,
Enghild J.J.;
"Posttranslational modifications of human inter-alpha-inhibitor:
identification of glycans and disulfide bridges in heavy chains 1 and
2.";
Biochemistry 37:408-416(1998).
[17]
GLYCOSYLATION AT ASN-285.
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).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-588.
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-402 AND THR-407, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-750.
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).
[21]
GLYCOSYLATION AT ASN-285.
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND 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).
[23]
VARIANTS VAL-585 AND ARG-595.
PubMed=7535743; DOI=10.1007/BF00208970;
Ding M., Umetsu K., Yuasa I., Sato M., Harada A., Suzuki T.;
"Molecular basis of inter-alpha-trypsin inhibitor heavy chain H1
(ITIH1) polymorphism.";
Hum. Genet. 95:435-436(1995).
-!- FUNCTION: May act as a carrier of hyaluronan in serum or as a
binding protein between hyaluronan and other matrix protein,
including those on cell surfaces in tissues to regulate the
localization, synthesis and degradation of hyaluronan which are
essential to cells undergoing biological processes.
-!- FUNCTION: Contains a potential peptide which could stimulate a
broad spectrum of phagocytotic cells.
-!- SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from
one or two heavy chains (H1, H2 or H3) and one light chain,
bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2
and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and
bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P19827-1; Sequence=Displayed;
Name=2;
IsoId=P19827-2; Sequence=VSP_045420;
Note=No experimental confirmation available.;
Name=3;
IsoId=P19827-3; Sequence=VSP_045419;
Note=No experimental confirmation available.;
-!- PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate
esterified to the alpha-carboxyl of the C-terminal aspartate after
propeptide cleavage.
-!- PTM: The S-linked glycan is composed of two 6-carbon sugars,
possibly Glc or Gal. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9425062,
ECO:0000269|PubMed:9677337}.
-!- MASS SPECTROMETRY: Mass=76258; Method=MALDI; Range=28-672;
Evidence={ECO:0000269|PubMed:9677337};
-!- POLYMORPHISM: There are 3 common alleles; ITIH1*1 with Glu-
585/Gln-595, ITIH1*2 with Val-585/Arg-595 and ITIH1*3 with Glu-
585/Arg-595.
-!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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EMBL; X63652; CAA45188.1; -; mRNA.
EMBL; X69532; CAA49279.1; -; Genomic_DNA.
EMBL; X69533; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69534; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69535; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69536; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69537; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69538; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69539; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69540; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69541; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69542; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69543; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69544; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69545; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69546; CAA49279.1; JOINED; Genomic_DNA.
EMBL; X69547; CAA49279.1; JOINED; Genomic_DNA.
EMBL; AK292750; BAF85439.1; -; mRNA.
EMBL; AK298455; BAH12794.1; -; mRNA.
EMBL; AK303156; BAH13906.1; -; mRNA.
EMBL; AK314198; BAG36876.1; -; mRNA.
EMBL; AC006254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW65259.1; -; Genomic_DNA.
EMBL; BC069464; AAH69464.1; -; mRNA.
EMBL; X16260; CAA34346.1; -; mRNA.
EMBL; M18192; AAA60557.1; -; mRNA.
EMBL; X75318; CAA53067.1; -; Genomic_DNA.
CCDS; CCDS2864.1; -. [P19827-1]
CCDS; CCDS54595.1; -. [P19827-3]
PIR; S39527; A39967.
RefSeq; NP_001159906.1; NM_001166434.2. [P19827-2]
RefSeq; NP_001159907.1; NM_001166435.2. [P19827-3]
RefSeq; NP_002206.2; NM_002215.3. [P19827-1]
UniGene; Hs.420257; -.
UniGene; Hs.76716; -.
ProteinModelPortal; P19827; -.
BioGrid; 109903; 5.
IntAct; P19827; 4.
STRING; 9606.ENSP00000273283; -.
iPTMnet; P19827; -.
PhosphoSitePlus; P19827; -.
UniCarbKB; P19827; -.
BioMuta; ITIH1; -.
PaxDb; P19827; -.
PeptideAtlas; P19827; -.
PRIDE; P19827; -.
Ensembl; ENST00000273283; ENSP00000273283; ENSG00000055957. [P19827-1]
Ensembl; ENST00000537050; ENSP00000443847; ENSG00000055957. [P19827-3]
GeneID; 3697; -.
KEGG; hsa:3697; -.
UCSC; uc003dfs.4; human. [P19827-1]
CTD; 3697; -.
DisGeNET; 3697; -.
EuPathDB; HostDB:ENSG00000055957.10; -.
GeneCards; ITIH1; -.
HGNC; HGNC:6166; ITIH1.
HPA; HPA041639; -.
HPA; HPA042049; -.
MIM; 147270; gene.
neXtProt; NX_P19827; -.
OpenTargets; ENSG00000055957; -.
PharmGKB; PA29964; -.
eggNOG; ENOG410IEJB; Eukaryota.
eggNOG; COG2304; LUCA.
GeneTree; ENSGT00550000074468; -.
HOGENOM; HOG000000680; -.
HOVERGEN; HBG057734; -.
InParanoid; P19827; -.
KO; K19014; -.
OMA; MSMENNG; -.
OrthoDB; EOG091G01HF; -.
PhylomeDB; P19827; -.
TreeFam; TF328982; -.
GeneWiki; ITIH1; -.
GenomeRNAi; 3697; -.
PRO; PR:P19827; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000055957; -.
CleanEx; HS_ITIH1; -.
ExpressionAtlas; P19827; baseline and differential.
Genevisible; P19827; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR010600; ITI_HC_C.
InterPro; IPR013694; VIT.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF06668; ITI_HC_C; 1.
Pfam; PF08487; VIT; 1.
Pfam; PF00092; VWA; 1.
SMART; SM00609; VIT; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS51468; VIT; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Phosphoprotein; Polymorphism;
Protease inhibitor; Proteoglycan; Reference proteome; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 27 {ECO:0000255}.
PROPEP 28 34 {ECO:0000269|PubMed:2476436}.
/FTId=PRO_0000016506.
CHAIN 35 672 Inter-alpha-trypsin inhibitor heavy chain
H1.
/FTId=PRO_0000016507.
PROPEP 673 911
/FTId=PRO_0000016508.
DOMAIN 37 166 VIT. {ECO:0000255|PROSITE-
ProRule:PRU00801}.
DOMAIN 290 450 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REGION 387 911 Hyaluronan-binding.
MOTIF 181 184 Phagocytosis uptake signal.
{ECO:0000255}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 402 402 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 407 407 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 672 672 Aspartate 1-(chondroitin 4-sulfate)-
ester.
CARBOHYD 60 60 S-linked (Hex...) cysteine.
{ECO:0000269|PubMed:9425062}.
CARBOHYD 285 285 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:9425062,
ECO:0000269|PubMed:9677337}.
/FTId=CAR_000138.
CARBOHYD 588 588 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:9425062,
ECO:0000269|PubMed:9677337}.
/FTId=CAR_000139.
CARBOHYD 653 653 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:9425062}.
/FTId=CAR_000213.
CARBOHYD 750 750 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 244 247 {ECO:0000269|PubMed:9425062}.
DISULFID 268 540 {ECO:0000269|PubMed:9425062}.
VAR_SEQ 1 288 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045419.
VAR_SEQ 1 142 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045420.
VARIANT 263 263 S -> T (in dbSNP:rs1042777).
{ECO:0000269|PubMed:1380832}.
/FTId=VAR_011873.
VARIANT 585 585 E -> V (in allele ITIH1*2; dbSNP:rs678).
{ECO:0000269|PubMed:1380832,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:7535743}.
/FTId=VAR_004019.
VARIANT 595 595 Q -> R (in allele ITIH1*2 and allele
ITIH1*3; dbSNP:rs1042779).
{ECO:0000269|PubMed:1380832,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:7535743}.
/FTId=VAR_004020.
VARIANT 695 695 G -> C (in dbSNP:rs1042904).
/FTId=VAR_011874.
VARIANT 844 844 D -> E (in dbSNP:rs1042849).
/FTId=VAR_011875.
CONFLICT 51 51 V -> T (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 54 54 R -> A (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 266 266 K -> E (in Ref. 1; CAA45188).
{ECO:0000305}.
CONFLICT 539 539 T -> A (in Ref. 3; BAH12794).
{ECO:0000305}.
CONFLICT 798 798 V -> A (in Ref. 3; BAH12794).
{ECO:0000305}.
SEQUENCE 911 AA; 101389 MW; 8FE715FF223FC917 CRC64;
MDGAMGPRGL LLCMYLVSLL ILQAMPALGS ATGRSKSSEK RQAVDTAVDG VFIRSLKVNC
KVTSRFAHYV VTSQVVNTAN EAREVAFDLE IPKTAFISDF AVTADGNAFI GDIKDKVTAW
KQYRKAAISG ENAGLVRASG RTMEQFTIHL TVNPQSKVTF QLTYEEVLKR NHMQYEIVIK
VKPKQLVHHF EIDVDIFEPQ GISKLDAQAS FLPKELAAQT IKKSFSGKKG HVLFRPTVSQ
QQSCPTCSTS LLNGHFKVTY DVSRDKICDL LVANNHFAHF FAPQNLTNMN KNVVFVIDIS
GSMRGQKVKQ TKEALLKILG DMQPGDYFDL VLFGTRVQSW KGSLVQASEA NLQAAQDFVR
GFSLDEATNL NGGLLRGIEI LNQVQESLPE LSNHASILIM LTDGDPTEGV TDRSQILKNV
RNAIRGRFPL YNLGFGHNVD FNFLEVMSME NNGRAQRIYE DHDATQQLQG FYSQVAKPLL
VDVDLQYPQD AVLALTQNHH KQYYEGSEIV VAGRIADNKQ SSFKADVQAH GEGQEFSITC
LVDEEEMKKL LRERGHMLEN HVERLWAYLT IQELLAKRMK VDREERANLS SQALQMSLDY
GFVTPLTSMS IRGMADQDGL KPTIDKPSED SPPLEMLGPR RTFVLSALQP SPTHSSSNTQ
RLPDRVTGVD TDPHFIIHVP QKEDTLCFNI NEEPGVILSL VQDPNTGFSV NGQLIGNKAR
SPGQHDGTYF GRLGIANPAT DFQLEVTPQN ITLNPGFGGP VFSWRDQAVL RQDGVVVTIN
KKRNLVVSVD DGGTFEVVLH RVWKGSSVHQ DFLGFYVLDS HRMSARTHGL LGQFFHPIGF
EVSDIHPGSD PTKPDATMVV RNRRLTVTRG LQKDYSKDPW HGAEVSCWFI HNNGAGLIDG
AYTDYIVPDI F


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