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Database: UniProt
Entry: A0A9C6X787_FRAOC
LinkDB: A0A9C6X787_FRAOC
Original site: A0A9C6X787_FRAOC 
ID   A0A9C6X787_FRAOC        Unreviewed;       865 AA.
AC   A0A9C6X787;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   28-JAN-2026, entry version 15.
DE   SubName: Full=Collagen alpha-2(IX) chain isoform X1 {ECO:0000313|RefSeq:XP_052130387.1};
GN   Name=LOC113205234 {ECO:0000313|RefSeq:XP_052130387.1};
OS   Frankliniella occidentalis (Western flower thrips) (Euthrips occidentalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Thysanoptera; Terebrantia; Thripoidea; Thripidae;
OC   Frankliniella.
OX   NCBI_TaxID=133901 {ECO:0000313|Proteomes:UP000504606, ECO:0000313|RefSeq:XP_052130387.1};
RN   [1] {ECO:0000313|RefSeq:XP_052130387.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole organism {ECO:0000313|RefSeq:XP_052130387.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_052130387.1; XM_052274427.1.
DR   AlphaFoldDB; A0A9C6X787; -.
DR   GeneID; 113205234; -.
DR   KEGG; foc:113205234; -.
DR   CTD; 104327; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000504606; Unplaced.
DR   GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1116; MACROPHAGE RECEPTOR WITH COLLAGENOUS STRUCTURE; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119,
KW   ECO:0000313|RefSeq:XP_052130387.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000504606}.
FT   DOMAIN          574..620
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          660..825
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..13
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..34
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..104
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..166
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..216
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..498
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..516
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..854
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..865
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  88548 MW;  0EF9A8CCD76FFA5F CRC64;
     MRSLKGDKGD RGLRGPPGES IRGPPGPPGP PGPPGAFYGK GDAFPDEGRA YGRPNQMFGA
     GSPGLQGPPG TCSCNLTSIL GSMNLEMIPG PPGQPGIDGA AGIPGVSGLP GPPGERGAPG
     SRGEKGDRGD IGATGPEGIQ GQKGDPGRDG TPGTPGAPGP PGPPGTSEPN GGYDPSWNSR
     SVLKDSVLGT GYGSSIGRPG SPGPKGEPGS SGSPGFKGER GVQGPKGERG ELGARGAKGD
     RGHQGPQGAQ GFKGEPGSPG IDGQPGVPGD NGRPGSKGDK GDPGAVGSPG PPGPPGVAVY
     NPEEAKFLGG GPSLLGEASS LPGPQGERGE PGVKGEKGDS GDRGLSGIPG INGVQGPAGE
     KGEAGVPGPV GPPGLKGERG ERGPPGAVTS VDGEVVVVKG EKGDGGKRGR RGRPGPPGVP
     GKDGASGDMG LPGWQGLPGR PGPVGMPGLG FQGPKGEKGE PGEITNLLRH RGEPGLPGPM
     GPPGPEGRPG PPGPPGPPSE VKYVPVPGPP GPPGPPGVTE SRGHVFGGEQ LHPRPGSGGG
     IEGLNKAMRN RDSLGHGSSS PPVQEKTTRI VPGAVTYQNK EAMTSRSAET AVGTLAYIID
     EEALLVRVNK GWQYVALGSI LDVTTPPPPT TFHPHVRPPP LESSNLLVNT FYMAADQPAL
     RMAALNEPYS GDMHGVSGAD RACHRQAHRA NMRGTFRAFI SSRVQDLDSI VRPADRNLPV
     INTRGDVLFK SWKELFAGKG GFLSQQHKIY SFNGRDILND FAWPEKVIWH GAHMLGERAM
     DAYCDSWQSD SADKFGLASS LLRGKLLAQE RFSCNHRFAI LCIEAVNPYL SRRRRRSVES
     NDEDDDFLDE DEYEDTLKSV MDEND
//
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