ID I3MXE4_ICTTR Unreviewed; 1298 AA.
AC I3MXE4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Inter-alpha-trypsin inhibitor heavy chain family member 6 {ECO:0000313|Ensembl:ENSSTOP00000016789.2};
GN Name=ITIH6 {ECO:0000313|Ensembl:ENSSTOP00000016789.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000016789.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000016789.2}
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 EMBL; AGTP01103034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01103035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01103036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000016789; -.
DR Ensembl; ENSSTOT00000022906.2; ENSSTOP00000016789.2; ENSSTOG00000026991.2.
DR eggNOG; ENOG502QPS2; Eukaryota.
DR GeneTree; ENSGT00940000162980; -.
DR InParanoid; I3MXE4; -.
DR TreeFam; TF328982; -.
DR Proteomes; UP000005215; 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:SF155; INTER-ALPHA-TRYPSIN INHIBITOR HEAVY CHAIN H6; 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:UP000005215};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1298
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012836256"
FT DOMAIN 21..150
FT /note="VIT"
FT /evidence="ECO:0000259|PROSITE:PS51468"
FT DOMAIN 283..469
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 616..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..876
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 141426 MW; FAEA4551026D8D2A CRC64;
MSGWRYLICV SFLLTIFLEL TCQGPPGPSS SSTKLLMTSY SIRSTVVSRY AHTLVTSVLF
NPHAEAHEAI FDLDLPHLAF ISNFTMTINN KVYVAEVKEK RQAKKIYEEA YHQGKTAAHV
GIRDRESEKF QISTSLAAGT EVTFALAYEE LLQRHQGQYQ LMISMRPGQL VSKLNVEVTV
SERTGISYVH VPPLRTSRLH TNHRTSEADS PPSTRIEKGE TCVQIIFCPT LQDQSAFSSS
GIMADFMVQY DVVMEDIIGD VQIYGGYFIH YFAPRGLQPV EKNVVFVIDV SGSMFGTKMK
QTKKAMNVIL SDLQANDYFN IISFSDTVSV WKAGGSIQAT IQNVHSAKDY LDHMEADGWT
DINAALLAAA SVLNHSNQEP GRGPSMGRIP LIIFLTDGEP TAGVTTPSVI LSNIRQALGH
RVSLFSLAFG DDADFPLLRR LSLENRGVAR RIYEDTDAAL QLEGLYEEIS MPLLADVRLD
YLGGMVGTSS WALFPNYFGG SELVVAGQVQ PGEQELGIHL AARGPKGQLL VARHSEGATN
SSQKAFGCPG EPALNIALFI RRLWAYVTIR ELLEARFQAR DTTTRHLLAA KILNLSLEYN
FVTPLTSLVM VQPKEASEEA KRQQSTTAGP TTIMPSYSSS HGLGTGTAQP ALVPKVSPKS
RPIKPTSTAM DSTKMSSSNE LEPLGQSSSA LSTSAHPKPK TPVQDFGTLA HPTLKTKPVA
LTPSNSSTLL LTKSGTPSHQ NPDVTSPMNS KTQVLPLSSG ILAQTKGDSP SHSQPGVVTS
QSPKSLSQPR PGVSILPIPK HLPHTRPKIT APKTPNNLPH PRPGILLPKI PKILSPLKPS
TLPHQTSINL SLSKPGTPTP HTPKTPLPPR PARPRFPPSQ SFNTFSNTVS SSTGPSSTMT
TSVLEEPLPA PLTPTLPSLL PTGRLWPQKD LLLRPQGTRQ ALGPSVLGVP TMVLPNNSSS
KQEGSPPNLP ILLPSSTLSE AISLLLLPEE LELLSESMVE SKFVESLNPP AFYTFLTPDK
DGNPHWDGDS EEILGGTGGS MDTQGSSVGS AKGTFPRIFT FSSSVDGDPH FVIHIPHSED
RICFTLDGRP GDLLQLIEDP KAGLHVSGKL LGAPPRPGHK DQTRTYFQII KITTDKPLAY
TITISRSSIS VQGESTLRLS WDQPALVRKP QLKLQVAAAA RLTLHIGNYL EFLILRHRYR
HPSTLQLPHL GFYVANGSGL SSSARGLIGQ FQHRDIQLVR GPNGPCLRRH QDPDVPVVLG
KRLLKESPRL LPRWASCWLV KRSHVEQLLG QPYLAYVL
//