ITIH3_BOVIN
ID ITIH3_BOVIN Reviewed; 891 AA.
AC P56652; A7MB92; Q0V8M9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-891.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP PROTEIN SEQUENCE OF 201-229.
RC TISSUE=Serum;
RX PubMed=7504674; DOI=10.1016/s0021-9258(19)74373-7;
RA Huang L., Yoneda M., Kimata K.;
RT "A serum-derived hyaluronan-associated protein (SHAP) is the heavy chain of
RT the inter alpha-trypsin inhibitor.";
RL J. Biol. Chem. 268:26725-26730(1993).
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 (H1, H2 or H3) and one light chain, bikunin. Inter-
CC alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-
CC alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-
CC inhibitor (P-alpha-I) of H3 and bikunin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR EMBL; BC151419; AAI51420.1; -; mRNA.
DR EMBL; BT026189; ABG67028.1; -; mRNA.
DR RefSeq; NP_001095368.1; NM_001101898.2.
DR AlphaFoldDB; P56652; -.
DR SMR; P56652; -.
DR STRING; 9913.ENSBTAP00000010322; -.
DR PaxDb; P56652; -.
DR PRIDE; P56652; -.
DR Ensembl; ENSBTAT00000010322; ENSBTAP00000010322; ENSBTAG00000007846.
DR GeneID; 508355; -.
DR KEGG; bta:508355; -.
DR CTD; 3699; -.
DR VEuPathDB; HostDB:ENSBTAG00000007846; -.
DR VGNC; VGNC:30335; ITIH3.
DR eggNOG; ENOG502QPS2; Eukaryota.
DR GeneTree; ENSGT00940000154554; -.
DR HOGENOM; CLU_008101_0_0_1; -.
DR InParanoid; P56652; -.
DR OMA; HPIHQDF; -.
DR OrthoDB; 955432at2759; -.
DR TreeFam; TF328982; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000007846; Expressed in liver and 28 other tissues.
DR ExpressionAtlas; P56652; baseline.
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; Glycoprotein; Protease inhibitor; Proteoglycan;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..34
FT /evidence="ECO:0000250"
FT /id="PRO_0000312437"
FT CHAIN 35..651
FT /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT /id="PRO_0000140900"
FT PROPEP 652..891
FT /evidence="ECO:0000250"
FT /id="PRO_0000312438"
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 651
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 CONFLICT 38
FT /note="R -> G (in Ref. 2; ABG67028)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="S -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..229
FT /note="PS -> VV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="E -> K (in Ref. 2; ABG67028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 891 AA; 99551 MW; BF70AAC245557CE8 CRC64;
MALAQWPYLI LALLSGLAVS GFPRNPSLLL GKRSLPGRAV DGIEVYSTKV NCKVTSRFAH
NVVTTRAVNH ANTAKEVSFD VELPKTAFIT NFTLTIDGVT YPGKVKEKEV AKKQYEKAVS
QGKTAGLVKA SGRKLEKFTV SVNVAAGSKV TFELTYEELL KRHKGKYEMY LKVQPKQLVK
HFEITVDIFE PQGISTLDAE ASFITNDLLG SALTKSFSGK KGHVSFKPSL DQQRSCPTCT
DSLLKGDFII TYDVNRESPA NVQIVNGYFV HFFAPQGLPV VPKSVVFVID VSGSMHGRKM
EQTKDALLKI LEDVKQDDYL NFILFSGDVT TWKDSLVPAT PENIQEASKF VMDIQDRGMT
NINDALLRGI SMLNKAREEH TVPERSTSII IMLTDGDANV GESRPEKIQE NVRNAIGGKF
PLYNLGFGNN LNYNFLENMA LENHGLARRI YEDSDANLQL QGFYEEVANP LLTGVEVEYP
QNAILDLTQN SYQHFYDGSE IVVAGRLADE DMNSFKAAVK GHGAINDLTF TEEVDMKEME
KALQERDYIF GDYIERLWAY LTIEQLLDKR KNAQGEEKEI LTAQALELSL KYHFVTPLTS
MVVTKPEDNE NQTAIANKPG EGPLDAEEVP SMAYLTSYQA PQTPYYYVDG DPHFIIQIPE
KDDAICFNID EDPGTVLRLI QDPVTGLTVN GQIIGEKTGR SDSQTRRTYF GKLGIASAQM
DFRIEVTREN ITLWNGDSLS TFSWLDTVMV TQDGLSVMIN RKKNMVVSFG DGVTFVVVLH
QVWKKEPAHH DFLGFYVVNS RGMSAQTHGL LGQFFHPFDF QVSDVHPGSD PTKPDATMVV
KNHQLTVTRG SQKDYRKDIS VGRNVACWFV HNNGQGLIDG IHRDYIVPNL F
