ID   ITIH3_RABIT             Reviewed;         903 AA.
AC   Q9GLY5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 70.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Suzuki A.;
RT   "Rabbit inter-alpha-trypsin inhibitor heavy chain.";
RL   Submitted (OCT-2000) 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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR   EMBL; AB050593; BAB17302.1; -; mRNA.
DR   RefSeq; NP_001075477.1; NM_001082008.1.
DR   AlphaFoldDB; Q9GLY5; -.
DR   SMR; Q9GLY5; -.
DR   STRING; 9986.ENSOCUP00000018231; -.
DR   PRIDE; Q9GLY5; -.
DR   GeneID; 100008624; -.
DR   KEGG; ocu:100008624; -.
DR   CTD; 3699; -.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   InParanoid; Q9GLY5; -.
DR   OrthoDB; 955432at2759; -.
DR   Proteomes; UP000001811; 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   2: Evidence at transcript level;
KW   Glycoprotein; Protease inhibitor; Proteoglycan; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..34
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000312434"
FT   CHAIN           35..663
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /id="PRO_0000312435"
FT   PROPEP          664..903
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000312436"
FT   DOMAIN          29..158
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          284..467
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   MOD_RES         663
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   903 AA;  100754 MW;  12D0B1518DF9C933 CRC64;
     MASAQWLGLV LALLSSLAAS GFPGSPFRLL GKRSLPEGAV NGIEIYSTKI NCKVTSRFAH
     NVVTTRAVNR ADTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGHVKEKEV AKKQYEKAVS
     QGKTAGLVKA SGRKLEKFTV SVNVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLVK
     HFEIDAHIFE PQGISMLDAE ASFITNDLLG SALTKSFSGK KGHVSFKPSL DQQRSCPTCT
     DSLLNGDFTI TYDVNRESPA NIQIVNGYFV HFFAPQGLPV VPKNVVFVID VSGSMYGRKL
     EQTKDALLKI LEDMREEDHL NFILFSSDVT TWKEHLVQAT PENLQEARAF VKSIQDQGST
     NLNDGLLRGI SMLNTAREEH RVPERSTSIV IMLTDGDANS GESRPEKIQE NVRNAIGGKF
     PLYNLGFGNN LNYNFLESLA LENDGFARRI YEDSDANLQL HGFYEEVANP LLTSVEMEYP
     KNAILDLTQN SYQHFYDGSE IVVAGRLADE DMNSFKADVK GHGALNDLTF TEEVDLKETE
     AALKEREYIF GNYIERLWAY LTIEQLLEKR KNARGEEKEN LTAQALDLSL KYHFVTPLTS
     MVVTKPEDNE DQTAIADKPG EEQAQAASQT SFSAYRTSYQ PPLGSAASYQ PPLGTPYYYV
     DGDPHFIIQV PEQDNAICFN IDEEPGTVLR LIQDPATGLT VNGQIIGDKK SSPDSATRKT
     YFGKLGIASA HMDLRIEVTT EKISLWNEVG RSTFSWLDTV TVTQDGLSMT INRKKNMVVS
     FGEGVTFVVI LHQVWKNHPI HQDFLGFYVV DSHRMSAWTH GLLGQFFHPF DFKVSDVHPG
     SEPTKPDATM VVKNRQLTVT RGSQRDYRMD ARAGTKVACW FVHNNGEGLI DGVHTDYIVP
     NLF