ID A0A3Q1FC22_9TELE Unreviewed; 945 AA.
AC A0A3Q1FC22;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Inter-alpha-trypsin inhibitor heavy chain 2 {ECO:0000313|Ensembl:ENSAPOP00000014578.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000014578.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000014578.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q1FC22; -.
DR STRING; 80966.ENSAPOP00000014578; -.
DR Ensembl; ENSAPOT00000023036.1; ENSAPOP00000014578.1; ENSAPOG00000017466.1.
DR GeneTree; ENSGT00940000157945; -.
DR InParanoid; A0A3Q1FC22; -.
DR OrthoDB; 608326at2759; -.
DR Proteomes; UP000257200; 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: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:UP000257200};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..945
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018703096"
FT DOMAIN 48..177
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 302..485
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 945 AA; 105562 MW; 6563978F801CB087 CRC64;
MRRLLLLLGL LVLRQGSCFE FVIDGEWEDE TSHIQDHRER HKRAILTSEE QEDFEAIRGD
DITVKSYKVE SRITSRFAHT TVRSSVVNSG SKAQSIGFNV QIPKRAFITN FTMNVNGITF
VGSVKEKTVA RNLYAQARAR GKAAGIIRAN SQDMETFKTE VHVPPGSNIE FELHYQEMMH
RKLGFYEHSL YLQPGRLVPQ FQVDVYIYEP KGISSVQAPN TLGVQFSDLI KVTSTKDKAH
IVFKPNLQQQ RKCDNCTGSA IDGVFTVKYD VNRDSNAGEL QVSDGHFVHF FAPSNLSPLS
KNIVFVIDVS GSMWGVKMKQ TVEAMQAILD DLTIDDNFSV IDFNHNVRCW SEELVPGSSI
QVADAKKYIQ NIKPNGGTNI NEALMRAVQM LVKASNQGLI DSRSVSMIIL VSDGDPTVGE
IKLSTIQKNV KRVMREEFSL FSLGIGFDVD YDFLERIANE NRGMAQRIYA NHDAAEQLRT
FYSQVSSPLL RRITIQFPED SVSEVTQNRF DKYFSGSELV VAGRVLPSDT NTLSSITTAA
AARLDLTLET DADTTQLDME LAKQQHSFTG FARQMWAYLT IKQLISERSL APTAVKKRKI
TQRIMTLAVE HQFVTPLTAL LVESEDAKER LLADSPKDPK HGCCSGGGLG AGSASNNLAP
VRVVYQPPPW VQMTTQAPPS QANKGPEDWT LPQQVNLVDN DPHFIVHLPG SDTYVCFNID
SKPGHILNLV SDSGTGVVVN GQLIRSNHKN KINTYFGIVS IYYQPEGVSV TVSTNSIDMT
DGRNNHSFTW GATADISQDG VRISIVRNSQ VTITINNNIQ VMVLLHRVWK KHPVNVDFLG
VYIPNNNQYS PLVHGLIGQF SREPFPEVSV YDIHEGADPL KNEATMEVKG NKLLVTRGWQ
KDYRSDTKRG SNVYCWFIHN SGKGLIDGHY TDYIVPGLNS FLQMP
//
