ITIH1_PIG
ID ITIH1_PIG Reviewed; 902 AA.
AC Q29052; O02669;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 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 Suzuki H., Hamasima N., Kimura M., Ozawa A., Yasue H.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-902.
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 Interacts with TNFAIP6 (via Link and CUB domains).
CC {ECO:0000250|UniProtKB:P19827}.
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: 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}.
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DR EMBL; D38754; BAA07632.1; -; mRNA.
DR EMBL; Y11546; CAA72309.1; -; mRNA.
DR RefSeq; NP_999089.1; NM_213924.1.
DR AlphaFoldDB; Q29052; -.
DR SMR; Q29052; -.
DR STRING; 9823.ENSSSCP00000012202; -.
DR PeptideAtlas; Q29052; -.
DR PRIDE; Q29052; -.
DR GeneID; 396963; -.
DR KEGG; ssc:396963; -.
DR CTD; 3697; -.
DR eggNOG; ENOG502RXR2; Eukaryota.
DR InParanoid; Q29052; -.
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 Glycoprotein; Phosphoprotein; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..663
FT /note="Inter-alpha-trypsin inhibitor heavy chain H1"
FT /id="PRO_0000016515"
FT PROPEP 664..902
FT /evidence="ECO:0000250"
FT /id="PRO_0000016516"
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 REGION 637..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19827"
FT MOD_RES 663
FT /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="S-linked (Hex...) cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q0VCM5"
FT CARBOHYD 644
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q0VCM5"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 432
FT /note="E -> D (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="R -> M (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="S -> A (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="W -> G (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="C -> S (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="G -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 779..780
FT /note="VR -> SV (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="L -> V (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 823
FT /note="A -> G (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="I -> L (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="H -> Y (in Ref. 2; CAA72309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 902 AA; 100395 MW; BD950C230FF14185 CRC64;
MDGTMGLQGL LCLCLASHLA LQAMPTQGSP TDSTKGNKAV NGVVIRSLKV NCKVTSRFAH
YVVTSQVVNN TNKPKEVAFD VEIPKTAFIS DFAITADENT FVGDIKDKVT AWKQYRKAAI
SGENSGLVRA SGRTMEQFTI HVTIGPRSKA TFQLTYEEVL RRKLTQYDIV IKVKPKQLVQ
HFEIDVDIFE PQGISKLDAQ ASFLSKEAAA QLIKKSFSGK KGHVLFRPTV GQQQSCSTCS
TTLLNGDFKV TYDVNREKLC DLLVANNYFA HFFAPQNLTK LNKNVVFVID ISSSMEGQKV
KQTKEALLKI LSDLKPGDYF DLVLFGSAVQ SWRGSLVQAS TANLDAARSY VRQFSLAGST
NLNGGLLRGI EILNKAQGSL PEFSNRASIL IMLTDGEPTE GVTDRSQILK NVRDAIRGRF
PLYNLGFGHD VEWNFLEVRA LENNGRAQRI YEDHDSAQQL QGFYDQVANP LLKDVELQYP
ADAVLALTQH RHKQYYEGSE ITVAGRIADN KLSSFKADVQ ASGDQGFKTT CLVDEEEMKK
LLQERGHMLE NYVERLWAYL TIQELLAKRM KLEWAEKASV SAKALQMSLD YQFVTPLTSM
TIRGMADKDG LEPVIDKPLE DSQPLEMLGP RRKFVLSASQ PSPTHPSSSI QKLPDRVTGV
DTDPHFIIRV PQKEDTLCFN INEEPGVVLS LVQDPDTGFS VNGQLIGNEA RCPGKHEGTY
FGRLGIANPA TGFQLEVTPQ NITLNPGSGG PVFSWRDQAS LRQDEVVVTI NRKRNLGVVR
EDGGTFEVVL HRLWKGSAIH QDFLGFYVLD SHRMSARTHG LLAQFFHPFD YKVSDIHPGS
DPTKTDATMV VKNRQLTVTR GLQKDYSKDP RHGLKVTCWF IHNNGDGLID GVHTDYIVPD
IF
