ITIH2_MESAU
ID ITIH2_MESAU Reviewed; 946 AA.
AC P97279;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 94.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9276673; DOI=10.1093/oxfordjournals.jbchem.a021742;
RA Nakatani T., Suzuki Y., Yamamoto T., Sinohara H.;
RT "Molecular cloning and sequencing of cDNAs encoding three heavy-chain
RT precursors of the inter-alpha-trypsin inhibitor in Syrian hamster:
RT implications for the evolution of the inter-alpha-trypsin inhibitor heavy
RT chain family.";
RL J. Biochem. 122:71-82(1997).
RN [2]
RP PROTEIN SEQUENCE OF 55-64; 140-146; 151-156; 424-447; 500-528 AND 577-605,
RP AND SUBUNIT.
RC TISSUE=Plasma;
RX PubMed=8864857; DOI=10.1093/oxfordjournals.jbchem.a021377;
RA Yamamoto T., Yamamoto K., Sinohara H.;
RT "Inter-alpha-trypsin inhibitor and its related proteins in Syrian hamster
RT urine and plasma.";
RL J. Biochem. 120:145-152(1996).
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.
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; D89286; BAA13939.1; -; mRNA.
DR PIR; JC5575; JC5575.
DR RefSeq; NP_001268591.1; NM_001281662.1.
DR AlphaFoldDB; P97279; -.
DR SMR; P97279; -.
DR PRIDE; P97279; -.
DR GeneID; 101837243; -.
DR CTD; 3698; -.
DR eggNOG; ENOG502QPS2; Eukaryota.
DR OrthoDB; 955432at2759; -.
DR Proteomes; UP000189706; 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 1: Evidence at protein level;
KW Direct protein sequencing; Gamma-carboxyglutamic acid; Glycoprotein;
KW Phosphoprotein; Protease inhibitor; Proteoglycan; Reference proteome;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..54
FT /evidence="ECO:0000250"
FT /id="PRO_0000016523"
FT CHAIN 55..702
FT /note="Inter-alpha-trypsin inhibitor heavy chain H2"
FT /id="PRO_0000016524"
FT PROPEP 703..946
FT /evidence="ECO:0000250"
FT /id="PRO_0000016525"
FT DOMAIN 56..185
FT /note="VIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT DOMAIN 308..468
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19823"
FT MOD_RES 282
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P19823"
FT MOD_RES 283
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P19823"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19823"
FT MOD_RES 702
FT /note="Aspartate 1-(chondroitin 4-sulfate)-ester"
FT /evidence="ECO:0000250"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19823"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 510
FT /note="V -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="E -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 106581 MW; CA8BF565458E7B2E CRC64;
MQRLACVLIW LFLLEEQAFE IPANEYSEFA GYSNLVELAP DKFPFVQENR RYQRSLPEES
GEMTDNVDQV TLYSYKVQST ITSRMATTII QSKLVNNSPQ SQNVVFDVQI PKGAFISNFT
MTVNGITFTS TIREKTVGRA LYSQARAKGK TAGWVRSRTL DMENFNTEVN IPPGAKVQFE
LHYQEMKWRK LGSYEHKIHL QPGRLAKHLE VNVWIVELQG MRFLHVPDTF EGHFQGVPVI
SKGQKKSHVS FKPTVAQQRK CPNCTYTAVD GELVVMYDVN REEKVGELEV FNGYFVHFFA
PENLDPIPKN ILFVIDVSGS MWGIKMKQTV EAMKTILDDL RTEDQFSVVD FNHNVRTWRN
DLVSATKTQI TDAKRYIEKI QPSGGTNINE ALLRAIFILN EASNLGMLNP DSVSLIVLVS
DGDPTVGELK LSKIQKNVKQ NIQDNISLFS LGIGFDVDYD FLKRLSNENR GIAQRIYGNR
DTSSQLKKFY NQVSTPLLRN VQFNYPQASV TDVTQNSFHN YFGGSEIVVA GKYDPSKLAE
VQSIITATST NTELVLETLS QMDDLEDFLS KDKHADPNFT KKLWAYLTIN QLLAERSLAP
TAAIKRKITK TILQMSLDHH IVTPLTAMVI ENEAGDERML ADSPPQDHSC CSGALYYGTK
VASASIPSWA SPSPTPVMAM LAVGANRLES TPPPHVIRVE NDPHFIIYLP KSQKNICFNI
DSEPGKILSL VSDPESGILV NGQLIGAKKA ENGKLRTYFG KLGFYFQKED MKIEISTENI
TLINGSSTTS LFWSDTAHLG NQRVLISVKK GKSVTLTLNK EMFFSVLLHH VWKKHPVNVD
FLGIYLPPTN KFSPSAHGLL GQFMNKPNIH IFNERPGKDP EKPEASMEVK GHKLTVTRGL
QKDYRTDIAF GTDVPCWFVH NSGKGFIDGH YKDYLVPQLY SFLKRP
