ID A0A0Q3RDQ8_AMAAE Unreviewed; 970 AA.
AC A0A0Q3RDQ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Inter-alpha-trypsin inhibitor heavy chain H2 {ECO:0000313|EMBL:KQK83641.1};
GN ORFNames=AAES_57515 {ECO:0000313|EMBL:KQK83641.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK83641.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK83641.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK83641.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the ITIH family.
CC {ECO:0000256|ARBA:ARBA00010158}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK83641.1}.
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DR EMBL; LMAW01001392; KQK83641.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3RDQ8; -.
DR Proteomes; UP000051836; 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 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:SF14; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H2; 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 Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 80..209
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 334..517
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 667..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 109046 MW; 01284FF244B38262 CRC64;
MRREDLVSGT YAGSSQEXRR KKMKHLICFL ALFLISGVGS FDLVIDEIPD EVENLIDLEI
XGFPSSPKMR NGRYQRSTSD WGYVGDLVED DDKIGLYSYK VQSTITSRLA NTMIQAKMVN
NAKRPQHIVF DVQVPKGAFI DNFTMDXNGI TFTSQIREKS EARKMYAQAK AKGKAAGIVR
SNALDMENFK TEVNVPPGTR IQFELHYHEM IRRKLSSYEH TVSVKPGRLA KHMEVDVRII
EPQGLRYVHV PNSLGDHFDG ITTISKGEKK AHVSFKPTMA QQRKXPTCSS TAVDGNFVVQ
YDVNRETTGG ELEIFNGYFI HFFAPENLDP LPKNILFVID VSGSMWGLKM KQTIEAMKAI
LSELRAADQF SLIDFNHNVR CWRDNLVSAT PSQVEEAKKY IQAIHPNGGT NINEALLRAT
FILNEAQNLG MLDPNSVSMI VLVSDGDPTV GELKLTTIQK NVKQSIKDEF SLFCLGIGFD
VDYDFLQRIA TDNRGMAQRI FGNQETSAQM KNFYNQVSTP LLKKIQFNYP QESVSDVTQS
SFHNYFGGSE IVVAGKVDTD NLQHLESIVT ATAANAELVM ETLRDVEELD GFMKKDRYAD
PEFTRKLWAY LTVNQMLAER NTAPTAALKR NITKSILQMS LDHHIVTPFT AMLIENAEKD
EIMLADQPKD PRRGCCPGTL GLTPNAPNNN RGIPPWANIT AVPVSFMPEQ RSPPVSSLSI
NRVDNDPHFI IHLPKSQRNI CFNINSEPGK ILNLVSDPGT GVVVNGQIVG AKRTENKKLN
TYXGKIGFYF KNKGLKVEIT TETITLKDGT YSITLTWADT GHIIRKQLLI SVKRENNVTI
TVGEEMSFMV LLHRVWKHHP VNVDFLGIYI PPENQFSPET HGLIGQFASE PEVAIHHQTP
GQPPEKPQAI MEVKGNKLTV TRGLQKDYRT DRVAGTEVQC WFVHNSGKGF IDGHYRDYLV
PHLYSFLKKP
//