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Database: UniProt
Entry: A0A3Q1JMY8_ANATE
LinkDB: A0A3Q1JMY8_ANATE
Original site: A0A3Q1JMY8_ANATE 
ID   A0A3Q1JMY8_ANATE        Unreviewed;       880 AA.
AC   A0A3Q1JMY8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Inter-alpha-trypsin inhibitor heavy chain 2 {ECO:0000313|Ensembl:ENSATEP00000032019.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000032019.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000032019.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; A0A3Q1JMY8; -.
DR   STRING; 64144.ENSATEP00000032019; -.
DR   Ensembl; ENSATET00000032489.2; ENSATEP00000032019.2; ENSATEG00000022044.2.
DR   GeneTree; ENSGT00940000157945; -.
DR   Proteomes; UP000265040; 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   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:UP000265040};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          21..150
FT                   /note="VIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51468"
FT   DOMAIN          278..461
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
SQ   SEQUENCE   880 AA;  98188 MW;  E6B6DA5B0EFE19B1 CRC64;
     TAAITDPAVI CCLKTRPLNC SDSCFLSQAI RGDDITVKSY RVESRITSRF AHVTVRSSVV
     NSGSKAQSIG FNVQIPKQAF ITNFTMNVNG ITFVGSVKEK TVARNLYTQA RARGKAAGII
     RANSQDMETF KTEVHVPSGS NIEFELHYQE MMHRKLGHYE HNLYLQPGRL VPQFQVDVYI
     FEPKGISMVQ TSNTLGQQFT ELIKVQIIYL MCPQAHIVFK PNLQQQRKCD NCTDSAIDGT
     FTVMYDVKRD SNAGELQVSD GHFVHFFAPT NLSPLPKNIV FVIDVSGSMW GVKMKQTVEA
     MQAILDDLTL DDQFSIIDFN HNVRCWSEDL VSGSSIQIAD AKKYIQNIKP NGGTNINEAL
     MRAVQMLLKA SNQGLIDSRS VSMIILVSDG DPTVGEIKLS AIQKNVRKIM REEFSLFSLG
     IGFDVDFDFL ERIAMENRGI AQRIYANHDA AEQLRTFYSQ VSSPLLRRIA IQFPEDSVSE
     VTQNRFDKYF SGSELVVAGK VLPSESNTLT SFTTASARLD IRMDTGADIA ELDTELVKHQ
     HSFTGFARQM WAYITIKQLI SDRSLAQTAA KKRMVTKQIM SLALEHQFVT PLTALLVESE
     DATERLLADS PRDPKHGCCS ATVLNGSCRP HMCASHPVDN DPHFIVHLPG SNMDVCFNID
     SKPGHILNLV SDRGTGVVVN GQLISSKQVH NSKLSTYFGT ISVDYQPDGV SVTITTDMIA
     MSDGSNNHSF TWAATAEITQ DGINIVKNSH VIVTVNDNIQ VMVLLHRVYK KHPVNVDFLG
     VYIPNDNQYS PVVHGLIGQF SREPEVNVFD IHEGADPLKK EATMEVKGNK LLVTRGWQKD
     YRRDTRQGSN VYCWFIHNSG KGFIDGHYTD YIVPDLHSFL
//
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