ID A0A091LKW2_CATAU Unreviewed; 869 AA.
AC A0A091LKW2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H3 {ECO:0000256|ARBA:ARBA00039924};
DE Flags: Fragment;
GN ORFNames=N323_02707 {ECO:0000313|EMBL:KFP56831.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP56831.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP56831.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP56831.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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: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 EMBL; KL327621; KFP56831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LKW2; -.
DR Proteomes; UP000053745; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000053745};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..119
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 244..427
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP56831.1"
FT NON_TER 869
FT /evidence="ECO:0000313|EMBL:KFP56831.1"
SQ SEQUENCE 869 AA; 97606 MW; 8F1CFBE22E2003A5 CRC64;
VNGIEINSMK IDSKVTSRFA HNVITSQAVN RGNVHKEVVF DVELPKTAFI TNFSMTIDGV
TYPGTIKEKE AAKKQYEKAV SKGQTAGLVK ASGRKTEKFT VSVNIEAASK VTFELTYEEL
LKRQFGKYEM FVKVKPKQLV KDFEIEVNIF EPQGITELEA EGTFITNDLQ NIIKKTFSEK
KGHISFKPTL DQQRTCANCS QSVLDGDFTV RYDVKRTTPD NLQIVNGYFV HFFAPTNLPK
LPKNVIFVID ISGSMSGREI EQTREALLKI LDDIKEDDFF NFILFGSEVH TWKETLIKAT
PENLDEARKF VRGIDTEGMT NLYGGIMRGI DMLNAAHEGN LVPKRSASII IMLTDGQPNV
GISNTQDIQT HVKKAIEGKY PLYNLGFGYG VDYNFLEKMA LENKGLARRI YPDSDAALQL
QGFYDEVSNP MLTDVELNYP ENEISDLTKT SFKHFYDGSE IVVAGRFIDN NQNSLTVDVR
GEGANDALSY TTQQDAEQTA KASQEQEYIF GEYIERLWAY LTIEQLLEKR IAATGEEKEN
LTADALDLSL KYKFVTPLTS MVVTKPEDYD NQDGIANKPI EGIDIFTILL YLRSQVFSNI
LFVCLLSAAP QLSYLYTAHP TWYTSVDGDP HFIISVPQKE DAICFNINEN PGAVLNLIND
PVTGITVNGE LIGDKRANSD AKIQNTYFGK LGIANKHLDL KLTVTSEKIT IQNGNEKTGF
TWLDSVTLQQ EGLTLIINRK KNLVLSMGSG ASFVIVLHQV WKKHPLHQDF LGLYTLESDK
LSEQTHGLLG QFFHPIDFTI LEIHPGSDPK KPDATMIVKN NELTVTRGWQ KDYRRDPQHG
VDIPCWFVHN NGAGLIDGVH TDYIVSSLF
//
