ID A0A9R1TUL8_9HYME Unreviewed; 1109 AA.
AC A0A9R1TUL8;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=Collagen alpha-1(IX) chain isoform X7 {ECO:0000313|RefSeq:XP_011315033.1};
GN Name=Mp {ECO:0000313|RefSeq:XP_011315033.1};
OS Fopius arisanus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC Opiinae; Fopius.
OX NCBI_TaxID=64838 {ECO:0000313|Proteomes:UP000694866, ECO:0000313|RefSeq:XP_011315033.1};
RN [1] {ECO:0000313|RefSeq:XP_011315033.1}
RP IDENTIFICATION.
RC STRAIN=USDA-PBARC FA_bdor {ECO:0000313|RefSeq:XP_011315033.1};
RC TISSUE=Whole organism {ECO:0000313|RefSeq:XP_011315033.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_011315033.1; XM_011316731.1.
DR AlphaFoldDB; A0A9R1TUL8; -.
DR GeneID; 105273967; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000694866; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; 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 CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_011315033.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694866};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1109
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040251861"
FT DOMAIN 33..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 238..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..281
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..578
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1109 AA; 116798 MW; A00D21BB9D37B6A8 CRC64;
MLLSFRVVLL ISAVLSSWRA RADYLSDKNE VYDLLSAAVL TTEDKNQYVD DGVDGFLAFG
FRPGSEVKQP YRLCLPEKLS GEFTIVATFK PMSLRTSYLF AVLNPFDTIV QLGLRITDGP
SPNQNVSLIY TNSDEHSHSE EIAQFTVTKL TRKWSKIVIR VSTTDVALYL NCHEVARQRV
TRIPQELVFD TASALYIAQA GPHIQEKYDG LLQTLRLYSG LPQDLVRCSD IELFPTHAGS
GDYSDPLEGG LLDFDKFEQG EDNDKNENNP PPFITPPPPN PDGRGLKGEK GDKGERGESV
RGSPGPPGPP GNLYDLNDDA KRIQPQGPPG PKGEPGTCTC NATDLRMNFM MPKMIEGPKG
EPGVSGKEGK QGDRGLTGSA GPPGERGLPG SAGPKGDRGE LGMTGPEGPQ GQKGEPGRDG
IAGEKGNPGP PGPPGKADDF SPHDPLWIRT GMSPVSREGI TMRPGLPGQK GDAGMPGHPG
PKGESGITGS KGTKGEPGLK GTKGDHGKDG SRGVQGFKGE PGAPGTPGFP GAPGENGRPA
EKGDKGDSGP EGKQGPPGPS GHVNFGTGGL AGSGTGNGEK GERGESGPRG FKGDLGTKGE
KGNKGDSGPS GLPGINGVQG PQGDKGEPGR DGSAGVPGTG GSKGDRGERG PPGATTIAGS
GDYVTIKGEK GTEGKRGRRG RPGPPGPPGK SGSAGEIGLP GWPHNSYKGR AGTLGIPRSP
GPVGPKGDKG ESCLVNECSS GSGMKGEKGA DGFPGAPGRD GQRGLPGPPG PPGISLIGQK
GEPGIGRNHM FGERDYYGPR QGAGKPPTRG AHEVTTKIVP GAVTFQNSDA MTKMSSVSSV
GTLAYIIDEE ALLVRVNHGW QYIALGSLLP ITTVPPPTTV LPPTNPPFEA SNLINQIPMK
TDGTGLRMAA LNEPISGDMH GVRGADYACY RQARRAGLRG TFRAFLSSRV QNVDSIVRLD
DRDLPIVNIK GDVLFNSWKE MFNGHGAYFS QNPRIYSFNG KNILADLAWP EKIVWHGSHK
FGDRAMDTYC DAWHSGNSDR YGLGSPITAG RLLEQVRYSC DNKFALLCIE VTSESARRRR
SINDNIDNSD NDDLSEQEYQ NYLDHITNN
//
