ID A0A3B4DXK1_PYGNA Unreviewed; 912 AA.
AC A0A3B4DXK1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000027786.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000027786.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the ITIH family.
CC {ECO:0000256|ARBA:ARBA00010158}.
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DR AlphaFoldDB; A0A3B4DXK1; -.
DR Ensembl; ENSPNAT00000001654.1; ENSPNAP00000027786.1; ENSPNAG00000013361.1.
DR GeneTree; ENSGT00940000154554; -.
DR Proteomes; UP000261440; 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; 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 Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..912
FT /note="Inter-alpha-trypsin inhibitor heavy chain H3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017292035"
FT DOMAIN 29..158
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 318..501
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 912 AA; 102511 MW; 073E9277C910035D CRC64;
MSTMWTVLLL CVSVYLCVPS RSYGAFIISR DVQQKRSVDS ALIEVQSVKI DCKVASRFAH
TVMISTVLNK ANFSQEVFFE VELPKTAFIT NFSMEIDSKM YVGEVKEKEK AKKQYEKAVS
SGQTAGLVKA SGRKMEKFSV SVNIAANSNV TFTLTYEELL QRRFGKYEIM IRVKPKQLVQ
HFEIAADIYE PQGIAFLDYS AAFLTNELLP LVEKTVTDKK AHLSFSPTLD QQRKCPDCDG
TLIDGYFYIN YDVNRVQDLG DIQVQFRIVS LQADVCEHNH LSSTTLLFSL ITVSVFQIVN
GYFVHFFAPA DLQRLPKNVV FVIDRSGSMR GKKMEQTREA LLTILDDLYV EDHFGLISFD
DKIVKWRPSL SKATKENVNA AKEFVKAITA VGWTNINDAV LHAVNILTAA KKNKTVPENS
ASMIILLTDG DPTYGEKNLD TIKHNVQTAI GGNMSLFCLG FGFDVDYSFL DVMAKQNDGL
ARRIYEASDA ILQLQGFYDE VASPLLSEVH FNYPEDKVNS LTGSYFKQLF NGSEIVIAGQ
LNDIQMNDFA VEVSAQGAGN DFVVKGQASA QKWDTIFPDQ EYIFGDFTER LWAYLTIQQL
LDKKDKGTPE EKANATAEAL ELSLKYNFVT PLTSMVVTKP ENEDKPEDAF IADKLTEDQR
KFTGTSIPSQ TVPQTGTVPQ TSYSYASSPV NFGTIFNLVK DPLTGTVVNG QTIGDKKVDP
ANKNNTYFGC FGIIHEKFGI RLMVSTQEIL VSEHGKQTKL FWSDNTSVKG LNMDLQVTKD
RSLTVTLRNS VKFVIMLHKV WKKHPYHQDY LGFYTLDSHL FSQRVHGLLG QFYNGVQFEV
SELFAGKDVD KLDAFMLVKG HRILVTRGWQ KDFRNDVKNG ENVPCWFIHN NGTGLIDGDL
TDYIVSGLFK TN
//