ID   ITIH2_PIG               Reviewed;         935 AA.
AC   O02668;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H2;
DE            Short=ITI heavy chain H2;
DE            Short=ITI-HC2;
DE            Short=Inter-alpha-inhibitor heavy chain 2;
DE   Flags: Precursor;
GN   Name=ITIH2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Gebhard W.;
RL   Submitted (MAR-1997) 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. Inter-alpha-
CC       inhibitor (I-alpha-I) is composed of ITIH1/HC1, ITIH2/HC2 and bikunin.
CC       {ECO:0000250|UniProtKB:P19823}.
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   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P19823}.
CC   -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR   EMBL; Y11545; CAA72308.1; -; mRNA.
DR   RefSeq; NP_999068.1; NM_213903.1.
DR   AlphaFoldDB; O02668; -.
DR   SMR; O02668; -.
DR   STRING; 9823.ENSSSCP00000011867; -.
DR   PaxDb; O02668; -.
DR   PeptideAtlas; O02668; -.
DR   PRIDE; O02668; -.
DR   Ensembl; ENSSSCT00045037844; ENSSSCP00045026301; ENSSSCG00045021935.
DR   GeneID; 396937; -.
DR   KEGG; ssc:396937; -.
DR   CTD; 3698; -.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   HOGENOM; CLU_046425_0_0_1; -.
DR   InParanoid; O02668; -.
DR   OrthoDB; 955432at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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   Gamma-carboxyglutamic acid; Glycoprotein; Phosphoprotein;
KW   Protease inhibitor; Proteoglycan; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..53
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016526"
FT   CHAIN           54..691
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H2"
FT                   /id="PRO_0000016527"
FT   PROPEP          692..935
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016528"
FT   DOMAIN          45..174
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          297..457
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   MOD_RES         271
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P19823"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19823"
FT   MOD_RES         691
FT                   /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         875
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19823"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   935 AA;  104622 MW;  88D4AC1BEED367CC CRC64;
     MKGLTCFLLC FLLSEAQGFE IPTNGLSEFA EYGDLAELAL GKFHVVPGNR RSQEGVDQVT
     LYSYKVQSTI TSRMANTVIQ TKVVNHSPEP QDVVFDIQIP KGAFISNFSM TVDGTKFTSS
     IKEKTVGRAL YWQARAKGKT AGLVRSRALD MENFKTEVNI APGAKVQFEL HYQEVKWRNL
     GSYEHRIHLQ PGRLAKHLEV DVQIIEPQGL RFLHVLDTFD GHFDGVPVVV KGQQKAHVAF
     KPTVAQQRKC PSCSETAVDG ELVVMYDVNR EQKAGELQLF NGYFVHFFAP ESMDPIPKNI
     LFVIDVSGSM WGIKMKQTVE AMKTILDDLR AEDQFSLVDF NHNIRTWRND LVSATKTQVA
     DAKTYIEKIQ PSGGTNINEA LLRAIFILNE ANNLGLLDPN SVSLIILVSD GDPTVGELQL
     SKIQKNVKQN IQDNVSLFSL GIGFDVDYDF LKRLSNDNRG MAQRIYGNQD TASQLKKFYN
     QVSTPLLRNV QFNYPQASVT DVTQNSFPNY FGGSEIVVAG KFNPEKLEQL QGIITATSAN
     VELVLETLAE MDGLEAFLAK DRHADPDFTK KLWAYLTINQ LLDERSRAPS AAVKKKITKS
     ILQMSLDHHI VTPLTAMVVE NEAGDERMLA DAPPQDQSCC SGTLNYGRKV TPNSLPSWVN
     PLPTPRVPLP AVGPSVIEAT PPPHVMRVEN DPHFIIYLPR SQQNICFNID SEPGKILNLV
     SDPESGIVIN GQLISAKKLK DGKLSTYFGK IGFYFQHEDV KVEISTETIS LSRGSRVSVL
     SWSDSALVLN QRVHISVKKE KTVTVTLDQE VSFSVLLHRV WKKHPINVDF LGIYIPPTTK
     FSPKAHGLIG QFMHEPEIRI FNERPGKDPE KPEASMEVKG QTLVVTRGLQ KDYRTDRVFG
     TDVPCWFVHN SGKGFIDGHY KDYLVPLLYS FLKRP