ID   ITIH3_RAT               Reviewed;         887 AA.
AC   Q63416;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 118.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   Blom A., Fries E.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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.
CC   -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR   EMBL; X83231; CAA58233.1; -; mRNA.
DR   RefSeq; NP_059047.1; NM_017351.1.
DR   AlphaFoldDB; Q63416; -.
DR   SMR; Q63416; -.
DR   BioGRID; 248430; 1.
DR   IntAct; Q63416; 1.
DR   MINT; Q63416; -.
DR   STRING; 10116.ENSRNOP00000023984; -.
DR   GlyGen; Q63416; 2 sites.
DR   jPOST; Q63416; -.
DR   PaxDb; Q63416; -.
DR   PRIDE; Q63416; -.
DR   Ensembl; ENSRNOT00000023984; ENSRNOP00000023984; ENSRNOG00000017689.
DR   GeneID; 50693; -.
DR   KEGG; rno:50693; -.
DR   UCSC; RGD:620633; rat.
DR   CTD; 3699; -.
DR   RGD; 620633; Itih3.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   GeneTree; ENSGT00940000154554; -.
DR   HOGENOM; CLU_008101_0_0_1; -.
DR   InParanoid; Q63416; -.
DR   OrthoDB; 955432at2759; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   PRO; PR:Q63416; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000017689; Expressed in liver and 19 other tissues.
DR   ExpressionAtlas; Q63416; baseline and differential.
DR   Genevisible; Q63416; RN.
DR   GO; GO:0005576; C:extracellular region; TAS:RGD.
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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Glycoprotein; Protease inhibitor;
KW   Proteoglycan; Reference proteome; Secreted; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..33
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016538"
FT   CHAIN           34..647
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /id="PRO_0000016539"
FT   PROPEP          648..887
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016540"
FT   DOMAIN          29..158
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          282..442
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   MOD_RES         647
FT                   /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   887 AA;  99098 MW;  3B9F0FF96D514096 CRC64;
     MVTLWWPCLV LALLSGLETS GFPRSPLRLL GKRSLPEGVV DGIEIYSTKI SCKVTSRFAH
     NVVTTRAVNR ADKAKEVSFD VELPKTAFIT NFTLTIDGVT YPGSVKEKEV AQKQYEKAVS
     QGKTAGLVKA SGRKLEKFTV SVNVAAGSKV IFELTYEELL KRNKGKYEMY LKVQPKQLVR
     HFEIDAHIFE PQGISMLDAD ASFITNDLLG SALTKSFSGK KGHVSFKPSL DQQRSCPTCT
     DSLLNGDFTI VYDVNRESPG NVQIVNGYFV HFFAPQGLPV VPKNIAFVID VSGSMSGRKI
     QQTREALLKI LDDMKEEDYL NFILFSTGVT TWKDHLVKAT PANLEEARAF VKNIRDRSMT
     NINDGLLRGI EMLNKAREDH LVPERSTSIL VMLTDGDANT GESRPEKIQE NVRNAIRGKF
     PLYNLGFGNN LNYNFLESLA LENHGFARRI YEDSDASLQL QGFYEEVANP LLTNVELEYP
     ENAILDLTRN SYPHFYDGSE IVVAGRLVDR NVDNFKADVK GHGALNDLTF TEEVDMKEMD
     AALKEQGYIF GDYIERLWAY LTIEQLLEKR KNARGDEKEN ITAEALELSL KYHFVTPLTS
     MVVTKPEDNE DQTAIADKPG EEAISASTAY LTSQQSSHSP YYYVDGDPHF IIQVPGKNDT
     ICFNIDEKPG TVLSLIQDPV TGIAVTGQII GEKGNNASSR TGKTYFGKLG IANAWMDFRI
     EVTTEKIILG NGDALSTFSW LDTVTVTQTG LSVTINRKKN MVVSFEDGIS FVIVLHQVWK
     KHPVHQDFLG FYVVDSHRMS AQTHGLLGQF FQPFDFKVFD VRPGSDPMKP DATMVVKSHR
     LTVTRGSQKD YRKDASVGTK VVCWFVHNNG EGFIDGVHTD YIVPSLF