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ITIH1_MESAU
ID   ITIH1_MESAU             Reviewed;         914 AA.
AC   P97278;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H1;
DE            Short=ITI heavy chain H1;
DE            Short=ITI-HC1;
DE            Short=Inter-alpha-inhibitor heavy chain 1;
DE   Flags: Precursor;
GN   Name=ITIH1;
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 387-401 AND 461-475, 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. Inter-alpha-
CC       inhibitor (I-alpha-I) is composed of ITIH1/HC1, ITIH2/HC2 and bikunin.
CC       Interacts with TNFAIP6 (via Link and CUB domains).
CC       {ECO:0000250|UniProtKB:P19827}.
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   -!- PTM: The S-linked glycan is composed of two 6-carbon sugars, possibly
CC       Glc or Gal. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR   EMBL; D89285; BAA13938.1; -; mRNA.
DR   PIR; JC5574; JC5574.
DR   AlphaFoldDB; P97278; -.
DR   SMR; P97278; -.
DR   PRIDE; P97278; -.
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   Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW   Protease inhibitor; Proteoglycan; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   PROPEP          31..36
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016512"
FT   CHAIN           37..675
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H1"
FT                   /id="PRO_0000016513"
FT   PROPEP          676..914
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016514"
FT   DOMAIN          39..168
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          293..453
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19827"
FT   MOD_RES         405
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P19827"
FT   MOD_RES         410
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P19827"
FT   MOD_RES         675
FT                   /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="S-linked (Hex...) cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        656
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q0VCM5"
SQ   SEQUENCE   914 AA;  101786 MW;  B693FF5656FE89E3 CRC64;
     MDGAAVGLRV LLGLGLVSLL TLEAMPAAWG LATTGRPRAR EKRQAVDTTP DGVLVKSLKV
     NCKVTSRFAH YIITSQVVNR QPNEAREVAF DVEIPKTAFI SDFAITADGN TFIGDIKDKA
     SAWKQYRKAI SGENAGLVRT SGRNMEQFTI HITVGAQSKA TFQLTYEEVL KRRLTQYDIV
     IKVKPKQLVQ HFEIDVDIFE PQGISKLDAQ ASFLSKELAA QTIKESFSGK KGHVLFRPTV
     SQQQQPCPTC STSWLNGDFK VTYDVNRDKL CDLLVANNYF AHFFAPKNLT NMSKNLVFVI
     DISGSMEGQK VKQTKEALLK ILGDVKPGDS FDLVLFGSRV QSWKGSLVPA TQANLQAAQD
     FVRRFSLAGA TNLNGGLLRG IEILNKAQGS HPELSSPASI LIMLTDGEPT EGETDRSQIL
     KNVRNAIRGR FPLYNLGFGH DLDFNFLEVM SMENSGWAQR IYEDHDATQQ LQGFYNQVAN
     PLLTDVELQY PQDSVLSLTQ HRHKQYYDGS EIVVAGRIAD HKLSTFKADV RARGERQEFK
     ATCLVDEEEM KKLLRERGHM LENHVERLWA YLTIQELLAK RMKMEGEERA NLSSQALKMS
     LDYQFVTPLT SMTIRGLTDE DGLEPTIDKT PEDSQPLVKV GPRRTFVLSA TQPSPTARSS
     VVSKLPNQVT GVDTDPHFII YVPQKEDSLC FNINEEPGVI LSLVQDPDTG FSVNGQLIGS
     KPSRPGQHEA TYFGRLGISN PPSDFQLEVT PRNITLNPSS GGPVFSWRDQ ATPQKDGVLV
     TINKKRNLVV SVEDGATFEI VLHRTWKGSA AHQDFLGFYV LDSSRMSART RGLLGQFFCP
     LDFEVSDIRP GSDPMKLDAT MRVKNRQLAV TRGLQRDYSK DPRHGTEVSC WFIHNNGAGL
     IDGVHTDYIV PDIF
 
 
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