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Inter-alpha-trypsin inhibitor heavy chain H3 (ITI heavy chain H3) (ITI-HC3) (Inter-alpha-inhibitor heavy chain 3) (Serum-derived hyaluronan-associated protein) (SHAP)

 ITIH3_HUMAN             Reviewed;         890 AA.
Q06033; Q3B7H5; Q53F06; Q6LAM2; Q99085;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
07-NOV-2018, entry version 145.
RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3;
Short=ITI heavy chain H3;
Short=ITI-HC3;
Short=Inter-alpha-inhibitor heavy chain 3;
AltName: Full=Serum-derived hyaluronan-associated protein;
Short=SHAP;
Flags: Precursor;
Name=ITIH3;
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 2), AND VARIANT LYS-315.
TISSUE=Liver;
PubMed=7681778; DOI=10.1111/j.1432-1033.1993.tb17717.x;
Bourguignon J., Diarra-Mehrpour M., Thiberville L., Bost F.,
Sesboue R., Martin J.-P.;
"Human pre-alpha-trypsin inhibitor-precursor heavy chain. cDNA and
deduced amino-acid sequence.";
Eur. J. Biochem. 212:771-776(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=9756925; DOI=10.1074/jbc.273.41.26809;
Diarra-Mehrpour M., Sarafan N., Bourguignon J., Bonnet F., Bost F.,
Martin J.-P.;
"Human inter-alpha-trypsin inhibitor heavy chain H3 gene. Genomic
organization, promoter analysis, and gene linkage.";
J. Biol. Chem. 273:26809-26819(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[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 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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-27 (ISOFORM 2).
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).
[7]
PROTEIN SEQUENCE OF 34-53; 467-481 AND 501-519.
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 345-890 (ISOFORMS 1/2).
TISSUE=Liver;
PubMed=2465147; DOI=10.1111/j.1432-1033.1989.tb14532.x;
Diarra-Mehrpour M., Bourguignon J., Sesboue R., Mattei M.-G.,
Passage E., Salier J.-P., Martin J.-P.;
"Human plasma inter-alpha-trypsin inhibitor is encoded by four genes
on three chromosomes.";
Eur. J. Biochem. 179:147-154(1989).
[9]
PROTEIN SEQUENCE OF 635-651, AND CROSS-LINK SITE TO BIKUNIN.
PubMed=1898736;
Enghild J.J., Salvesen G., Hefta S.A., Thoegersen I.B., Rutherfurd S.,
Pizzo S.V.;
"Chondroitin 4-sulfate covalently cross-links the chains of the human
blood protein pre-alpha-inhibitor.";
J. Biol. Chem. 266:747-751(1991).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91 AND ASN-580.
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).
-!- 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.
-!- 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=2;
Name=1;
IsoId=Q06033-1; Sequence=Displayed;
Name=2;
IsoId=Q06033-2; Sequence=VSP_029842;
-!- PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate
esterified to the alpha-carboxyl of the C-terminal aspartate after
propeptide cleavage.
-!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA32821.1; Type=Frameshift; Positions=732, 736, 739; Evidence={ECO:0000305};
Sequence=CAA47439.1; Type=Frameshift; Positions=21, 732, 736, 739; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X67055; CAA47439.1; ALT_FRAME; mRNA.
EMBL; X99854; CAC79611.1; -; Genomic_DNA.
EMBL; AK222757; BAD96477.1; -; mRNA.
EMBL; AK223483; BAD97203.1; -; mRNA.
EMBL; AC006254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC107604; AAI07605.1; -; mRNA.
EMBL; BC107605; AAI07606.1; -; mRNA.
EMBL; BC107814; AAI07815.1; -; mRNA.
EMBL; X14690; CAA32821.1; ALT_FRAME; mRNA.
CCDS; CCDS46845.1; -. [Q06033-1]
PIR; S30350; S30350.
RefSeq; NP_002208.3; NM_002217.3. [Q06033-1]
UniGene; Hs.76716; -.
ProteinModelPortal; Q06033; -.
SMR; Q06033; -.
BioGrid; 109905; 8.
IntAct; Q06033; 4.
MINT; Q06033; -.
STRING; 9606.ENSP00000415769; -.
CarbonylDB; Q06033; -.
GlyConnect; 1421; -.
iPTMnet; Q06033; -.
PhosphoSitePlus; Q06033; -.
BioMuta; ITIH3; -.
DMDM; 166203665; -.
MaxQB; Q06033; -.
PaxDb; Q06033; -.
PeptideAtlas; Q06033; -.
PRIDE; Q06033; -.
ProteomicsDB; 58409; -.
ProteomicsDB; 58410; -. [Q06033-2]
Ensembl; ENST00000449956; ENSP00000415769; ENSG00000162267. [Q06033-1]
GeneID; 3699; -.
KEGG; hsa:3699; -.
UCSC; uc003dfv.3; human. [Q06033-1]
CTD; 3699; -.
DisGeNET; 3699; -.
EuPathDB; HostDB:ENSG00000162267.12; -.
GeneCards; ITIH3; -.
H-InvDB; HIX0024346; -.
HGNC; HGNC:6168; ITIH3.
HPA; HPA017373; -.
MIM; 146650; gene.
neXtProt; NX_Q06033; -.
OpenTargets; ENSG00000162267; -.
PharmGKB; PA29966; -.
eggNOG; ENOG410IEJB; Eukaryota.
eggNOG; COG2304; LUCA.
GeneTree; ENSGT00550000074468; -.
HOGENOM; HOG000000680; -.
HOVERGEN; HBG057734; -.
InParanoid; Q06033; -.
OMA; KVACWFV; -.
OrthoDB; EOG091G01HF; -.
PhylomeDB; Q06033; -.
TreeFam; TF328982; -.
Reactome; R-HSA-114608; Platelet degranulation.
ChiTaRS; ITIH3; human.
GeneWiki; ITIH3; -.
GenomeRNAi; 3699; -.
PRO; PR:Q06033; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000162267; Expressed in 111 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_ITIH3; -.
ExpressionAtlas; Q06033; baseline and differential.
Genevisible; Q06033; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
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;
Glycoprotein; Polymorphism; Protease inhibitor; Proteoglycan;
Reference proteome; Secreted; Serine protease inhibitor; Signal.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 34
/FTId=PRO_0000016529.
CHAIN 35 651 Inter-alpha-trypsin inhibitor heavy chain
H3.
/FTId=PRO_0000016530.
PROPEP 652 890
/FTId=PRO_0000016531.
DOMAIN 29 158 VIT. {ECO:0000255|PROSITE-
ProRule:PRU00801}.
DOMAIN 284 467 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
MOD_RES 651 651 Aspartate 1-(chondroitin 4-sulfate)-
ester.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
VAR_SEQ 1 21 MAFAWWPCLILALLSSLAASG -> MVALSHLGSALQLGSL
C (in isoform 2).
{ECO:0000303|PubMed:7522574,
ECO:0000303|PubMed:7681778}.
/FTId=VSP_029842.
VARIANT 315 315 Q -> K (in dbSNP:rs3617).
{ECO:0000269|PubMed:7681778}.
/FTId=VAR_049647.
VARIANT 340 340 T -> M (in dbSNP:rs35271262).
/FTId=VAR_049648.
VARIANT 640 640 P -> L (in dbSNP:rs60805548).
/FTId=VAR_061275.
VARIANT 751 751 T -> A (in dbSNP:rs9883888).
/FTId=VAR_049649.
VARIANT 825 825 R -> Q (in dbSNP:rs2710330).
/FTId=VAR_049650.
VARIANT 858 858 A -> V (in dbSNP:rs2710329).
/FTId=VAR_049651.
CONFLICT 113 113 K -> N (in Ref. 3; BAD97203/BAD96477).
{ECO:0000305}.
CONFLICT 348 348 R -> K (in Ref. 8; CAA32821).
{ECO:0000305}.
CONFLICT 361 361 N -> G (in Ref. 8; CAA32821).
{ECO:0000305}.
CONFLICT 515 515 F -> L (in Ref. 2; CAC79611).
{ECO:0000305}.
CONFLICT 667 667 F -> L (in Ref. 3; BAD97203/BAD96477).
{ECO:0000305}.
CONFLICT 716 716 A -> R (in Ref. 1; CAA47439 and 8;
CAA32821). {ECO:0000305}.
CONFLICT 851 851 Q -> H (in Ref. 8; CAA32821).
{ECO:0000305}.
SEQUENCE 890 AA; 99849 MW; 03B2B768784CB440 CRC64;
MAFAWWPCLI LALLSSLAAS GFPRSPFRLL GKRSLPEGVA NGIEVYSTKI NSKVTSRFAH
NVVTMRAVNR ADTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGNVKEKEV AKKQYEKAVS
QGKTAGLVKA SGRKLEKFTV SVNVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLVK
HFEIEVDIFE PQGISMLDAE ASFITNDLLG SALTKSFSGK KGHVSFKPSL DQQRSCPTCT
DSLLNGDFTI TYDVNRESPG NVQIVNGYFV HFFAPQGLPV VPKNVAFVID ISGSMAGRKL
EQTKEALLRI LEDMQEEDYL NFILFSGDVS TWKEHLVQAT PENLQEARTF VKSMEDKGMT
NINDGLLRGI SMLNKAREEH RIPERSTSIV IMLTDGDANV GESRPEKIQE NVRNAIGGKF
PLYNLGFGNN LNYNFLENMA LENHGFARRI YEDSDADLQL QGFYEEVANP LLTGVEMEYP
ENAILDLTQN TYQHFYDGSE IVVAGRLVDE DMNSFKADVK GHGATNDLTF TEEVDMKEME
KALQERDYIF GNYIERLWAY LTIEQLLEKR KNAHGEEKEN LTARALDLSL KYHFVTPLTS
MVVTKPEDNE DERAIADKPG EDAEATPVSP AMSYLTSYQP PQNPYYYVDG DPHFIIQIPE
KDDALCFNID EAPGTVLRLI QDAVTGLTVN GQITGDKRGS PDSKTRKTYF GKLGIANAQM
DFQVEVTTEK ITLWNRAVPS TFSWLDTVTV TQDGLSMMIN RKNMVVSFGD GVTFVVVLHQ
VWKKHPVHRD FLGFYVVDSH RMSAQTHGLL GQFFQPFDFK VSDIRPGSDP TKPDATLVVK
NHQLIVTRGS QKDYRKDASI GTKVVCWFVH NNGEGLIDGV HTDYIVPNLF


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