ID   ITIH3_MESAU             Reviewed;         886 AA.
AC   P97280;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3;
DE            Short=ITI heavy chain H3;
DE            Short=ITI-HC3;
DE            Short=Inter-alpha-inhibitor heavy chain 3;
DE   Flags: Precursor;
GN   Name=ITIH3;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9276673; DOI=10.1093/oxfordjournals.jbchem.a021742;
RA   Nakatani T., Suzuki Y., Yamamoto T., Sinohara H.;
RT   "Molecular cloning and sequencing of cDNAs encoding three heavy-chain
RT   precursors of the inter-alpha-trypsin inhibitor in Syrian hamster:
RT   implications for the evolution of the inter-alpha-trypsin inhibitor heavy
RT   chain family.";
RL   J. Biochem. 122:71-82(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 31-50; 446-472 AND 504-523, AND SUBUNIT.
RC   TISSUE=Plasma;
RX   PubMed=8864857; DOI=10.1093/oxfordjournals.jbchem.a021377;
RA   Yamamoto T., Yamamoto K., Sinohara H.;
RT   "Inter-alpha-trypsin inhibitor and its related proteins in Syrian hamster
RT   urine and plasma.";
RL   J. Biochem. 120:145-152(1996).
CC   -!- FUNCTION: May act as a carrier of hyaluronan in serum or as a binding
CC       protein between hyaluronan and other matrix protein, including those on
CC       cell surfaces in tissues to regulate the localization, synthesis and
CC       degradation of hyaluronan which are essential to cells undergoing
CC       biological processes. {ECO:0000250}.
CC   -!- SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or
CC       two heavy chains (HC) and one light chain, bikunin. Pre-alpha-inhibitor
CC       (P-alpha-I) is composed of ITIH3/HC3 and bikunin.
CC       {ECO:0000250|UniProtKB:Q06033}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Heavy chains are linked to bikunin via chondroitin 4-sulfate
CC       esterified to the alpha-carboxyl of the C-terminal aspartate after
CC       propeptide cleavage. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR   EMBL; D89287; BAA13940.1; -; mRNA.
DR   RefSeq; NP_001268279.1; NM_001281350.1.
DR   AlphaFoldDB; P97280; -.
DR   SMR; P97280; -.
DR   GeneID; 101826575; -.
DR   CTD; 3699; -.
DR   OrthoDB; 955432at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR010600; ITI_HC_C.
DR   InterPro; IPR013694; VIT.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF06668; ITI_HC_C; 1.
DR   Pfam; PF08487; VIT; 1.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00609; VIT; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS51468; VIT; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Glycoprotein; Protease inhibitor; Proteoglycan; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..30
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016532"
FT   CHAIN           31..646
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /id="PRO_0000016533"
FT   PROPEP          647..886
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016534"
FT   DOMAIN          26..155
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          279..439
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   MOD_RES         646
FT                   /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        577
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   886 AA;  99018 MW;  AC0594C6852576B8 CRC64;
     MWWPYLVLAL LSGLEASGFP RSPLRLLGKR SLPEGVVDGV EVYSTKISCK VTSRFAHNVV
     TTRAVNRADQ AKEVSFDVEL PKTAFITNFT LTIDGVTYPG NIKEKEVAQK QYDKAVSQGK
     TAGLVKASGR KLEKFTVSVN VAAGSKVTFE LTYEELLKRH KGKYEMYLKV QPKQLVRHFE
     IDAHIFEPQG ISMLDAEASF ITNDLLGSAL TKSFSGKKGH VSFKPSLDQQ RSCPTCTDSL
     LNGDFTIVYD VNRESPGNVQ VVNGYFVHFF APQGLPVVPK NIVFVIDISG SMAGRKIQQT
     RVALLKILDD MKQDDYLNFI LFSTGVTTWK DSLVQATPAN LEEARTFVRS ISDQGMTNIN
     DGLLRGIRML TDAREQHTVP ERSTSIIIML TDGDANTGES RPEKIQENVR KAIEGRFPLY
     NLGFGNNLNY NFLETMALEN HGVARRIYED SDANLQLQGF YEEVANPLLT NVEVEYPENA
     ILDLTKNSYP HFYDGSETAV AGRLADSDMN NFKADVKGHG ALNDLTFTEE VDMKEMDAAL
     KEQGYIFGNY IERLWAYLTI EQLLEKRKNA HGEEKENLTA QALELSLKYH FVTPLTPMVV
     TKPEDNEDQT SIADKPGEDA PYAATSTAYL TSHQSPPTPY YYVDGDPHFI IQVPGKNDTI
     CFNIDEKPGT VLRLIQDPVT GITVTGQIIG DKGSSPYSRT GKTYFGKLGI THAWMDFRIE
     VTTEKIILGT EDELSTFSWL DTVTITQTGL FVAINRKKNM VVSFGDGVNF VIVLHQVWKK
     HPLHQDFLGF YVVDSHRMSA RTHGLLGQFF RPFDFEVSDV RPGSDPAKPD ATMVVKNHQL
     TVTRGSQRDY RKDASVGTKV TCWFVHNNGE GLIDGVHTDY IVPSLF