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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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