ID A0A2I3H3Q4_NOMLE Unreviewed; 880 AA.
AC A0A2I3H3Q4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
GN Name=ITIH3 {ECO:0000313|Ensembl:ENSNLEP00000038120.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000038120.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000038120.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000038120.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037051}.
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:0000256|ARBA:ARBA00038801}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the ITIH family.
CC {ECO:0000256|ARBA:ARBA00010158}.
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DR EMBL; ADFV01173474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01173475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01173476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01173477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01173478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01173479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01173480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3H3Q4; -.
DR STRING; 61853.ENSNLEP00000038120; -.
DR Ensembl; ENSNLET00000032914.1; ENSNLEP00000038120.1; ENSNLEG00000007191.2.
DR GeneTree; ENSGT00940000154554; -.
DR InParanoid; A0A2I3H3Q4; -.
DR OMA; FNVIRFD; -.
DR Proteomes; UP000001073; Chromosome 4.
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 CDD; cd01461; vWA_interalpha_trypsin_inhibitor; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR010600; ITI_HC_C.
DR InterPro; IPR013694; VIT.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10338; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10338:SF115; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H3; 1.
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; vWA-like; 1.
DR PROSITE; PS51468; VIT; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..880
FT /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014121395"
FT DOMAIN 32..161
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 287..470
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 880 AA; 98504 MW; D9141C5461BAD30F CRC64;
MASAWWPCLI LALLSSLAAS GFPRSPFRLL GVSLPPLCHL GVANGIEVYS TKINSKVTSR
FAHNVVTTRT VNRADTAKEV SFDVELPKTA FITNFTLTID GVTYPGNVKE KEVAKKQYEK
AVSQGKTAGL VKASGRKLEK FTVSVNVAAG SKVTFELTYE ELLKRHKGKY EMYLKVQPKQ
LVKHFEIEVD IFEPQGISML DAEASFITND LLGSALTKSF SQKKGHVSFK PSLDQQRSCP
TCTDSLLDGD FTITYDVNRE SPGNVQIVNG YFVHFFAPQG LPVVPKNVAF VIDISGSMAG
RKLEQTKEAL LRILEDMKEE DYLNFILFSG DVSTWKEHLV QATPENLQEA RTFVKSMEDK
GMTNINDGLL RGISMLNKAR EEHRVPERST SIVIMLTDGD ANVGESRPEK IQENVRNAIG
GKFPLYNLGF GNNLNYNFLE NMALENHGFA RRIYEDSDAD LQLQGFYEEV ANPLLTGVEM
EYPENAVLDL TQNTYQHFYD GSEIVVAGRL VDEDMNSFKA DVKGHGVSVD RAWKCEVDMK
EMEKALQERD YIFGNYIERL WAYLTIEQLL EKRKNAHSEE KENLTARALD LSLKYHFVTP
LTSMVVTKPE DNEDERAIAD KPGEEAPGVS PFSNVSPVDG DPHFIIQVPE KDDALCFNID
EAPGTVLRLI RDPVTGLTVN GQIIGDKRGS PDSKTRKTYF GKLGIANAQM DFQVEVTTEK
ITLWNRAVPS TFSWLDTVTV TQDGLSMMIN RKNMVVSFGD GVTFVVILHQ VWKKHPVHRD
FLGFYVVDSH RMSAQTHGLL GQFFQPFDFK VSDIRPGSDP AKPDATLVVK NHQLIVTRGS
QKDYRKDASI GAKVVCWFVH NNGEGLIDGV HTDYIVPNLF
//
