ID A0A3B3E311_ORYME Unreviewed; 997 AA.
AC A0A3B3E311;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Inter-alpha-trypsin inhibitor heavy chain 5 {ECO:0000313|Ensembl:ENSOMEP00000036120.1};
GN Name=ITIH5 {ECO:0000313|Ensembl:ENSOMEP00000036120.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000036120.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000036120.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3E311; -.
DR STRING; 30732.ENSOMEP00000036120; -.
DR PaxDb; 30732-ENSOMEP00000036120; -.
DR Ensembl; ENSOMET00000031513.1; ENSOMEP00000036120.1; ENSOMEG00000023705.1.
DR GeneTree; ENSGT00940000158317; -.
DR OMA; AKKFIYT; -.
DR OrthoDB; 608326at2759; -.
DR Proteomes; UP000261560; 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:SF62; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H5; 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 Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..997
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017299370"
FT DOMAIN 54..181
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 322..506
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 109006 MW; BDAAB98B8A0EDDA7 CRC64;
MTSARARRKM LPLLVLLLSA LSRTEQLQSE LDSEDLEDLD LDLNLDLDLA PRRVPRQVKT
ILAKETKPHI QELSIKTTII SRYAFTAVHC AMLNRHVAAA EGVFQFQIPA DAFISNFTMI
VGGRVYQSEV TAKERKVKQG NGKAKSQESG ENSPEPEVEV FRMAVNIPGR NRAVFLLTYE
QLLQRRLGRY QHVTSLRPLQ LVSRLSLDVT VVDHAPITDL EVLPLQSGRT SSSASSASAG
SNAAAKPELP ITTEIKQQQN VWRITFSPNI VQQARISTSG VLGDFVIRYD VQRELGIGDI
QVLDGHFVHY FAPKDLPAVP KNVVFVIDTS ASMLGAKMRQ TKDALFTILK DLRPGDHFNF
ISFSNKVKVW QPNRLVPVTP LNIRDAKKFI LLLMPTGGTN IDGAIQTSSS VLRDYLSGSD
SGPNSVSLII FLTDGRPTTG EVQSATILGN TRSAVQEKFC IFTIGIGNDV DYRLLERMAL
DNCGMMRRIP EEADASAMLK GFYDEIGTPL LSDIRINYTE STVGYVTQNL FTNYFNGSEI
VIAGKLTNSS AESLHVQVTA SNNDKSIVLE TDVPLQHRQL ETRRHVKEAT AAVAAGAKAP
ASGSLSGLGL PLGSIAEHFA ERVWGFLSVK EGLRSRLRST TSREREDHIQ QATNLSLTYH
FLTPLTNMVV EKPVVLADGT MEPASTAAPG GGEAPPAAND LPGEADGETE HEPLRRLGSQ
TAPLTNVLGK DKRRPAKKPI TISKTSADGD PHFVVEFPLS KLTVCFNING EPGHVLRLVS
DHKHSGVTAN GKLVGAPAPP GSHKQQRTYF SSITIVVDRP RRAYIEVTPR KVILDGRDRI
VLPCHSSAAV DSGVLSVAIV GKANVTVTIG GNISFVILLH HYKNPAPYQT DHLGFYIGNS
KGLSANCHGL LGQFLHQEVG LAELPVEVGA QPSTVLKVKD RSVPVVHKSR RIYSGTQSVD
CWFARNNAAK LIDGRYEDYV APHMFDTGDS PQRTNRM
//