ID   ITIH3_PONAB             Reviewed;         876 AA.
AC   Q5RB37;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
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; CR858818; CAH91023.1; -; mRNA.
DR   RefSeq; NP_001125590.1; NM_001132118.1.
DR   AlphaFoldDB; Q5RB37; -.
DR   SMR; Q5RB37; -.
DR   STRING; 9601.ENSPPYP00000015436; -.
DR   GeneID; 100172506; -.
DR   KEGG; pon:100172506; -.
DR   CTD; 3699; -.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   InParanoid; Q5RB37; -.
DR   Proteomes; UP000001595; 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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..31
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000312439"
FT   CHAIN           32..637
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT                   /id="PRO_0000312440"
FT   PROPEP          638..876
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000312441"
FT   DOMAIN          26..155
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          281..464
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   MOD_RES         637
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   876 AA;  98410 MW;  9DADE7C3F8E24EBA CRC64;
     MVALSHLGSA LQLGSLWGFP RSPFRLLGKR SLPEGVANGI EVYSTKINSK VTSRFAHNVV
     TTRVVNHADT AKEVSFDVEL PKTAFITNFT LTIDGVIYPG NVKEKEVAKK QYEKAVSQGK
     TAGLVKASGR KLEKFTVSVN VAAGSKVTFE LTYEELLKRH KGKYEMYLKV QPKQLVKHFE
     IEVDIFEPQG ISMLDAEASF ITNDLLGSAL TKSFSGKKGH VSFKPSLDQQ RPCPTCTDSL
     LNGDFTITYD VNRESPGNVQ IVNGYFVHFF APQGLPVVPK NVAFVIDISG SMAGRKLEQT
     KEALLRILED MKKEDYLNFI LFSGDVSTWK EHLVQATPEN LQEARTFVKS MEDKGMTNIN
     DGLLRGISML NKAREEHRVP ERSTSIVIML TDGDANVGES RPEKIQENVR NAIGGKFPLY
     NLGFGNNLNY NFLENMALEN HGFARRIYED SDADLQLQGF YEEVANPLLT GVEVEYPENA
     ILDLTQNTYQ HFYDGSEIVV AGRLVDEDMN SFKADVKGHG ATNDLTFTEE VDMKEMEKAL
     QERDYIFGNY IERLWAYLTI EQLLEKRKNA HGEEKENLTA RALDLSLKYH FVTPLTSMVV
     TKPEDNEDER AIADKPGEDA EASYQPPQNP YYYVDGDPHF IIQVPEKDDA LCFNIDEAPG
     TVLRLIQDPV TGLTVNGQII GDKRGSPDSK TKKTYFGKLG IANAQMDFQV EVTTEKVTLW
     NRAVQSTFSW LDTVTVMQDG LSMMINRKNM VVSFGDGVTF VVVLHQVWKK HPVHRDFLGF
     YVVDSHRMSA QTHGLLGQFF QPFDFKVSDI RPGSDPTKPD ATLLVKNHQL IVTRGSQKDY
     RKDASIGTKV VRWFVYNNGE GLIDGVHTDY IVPNLF