ID A0A9R1UB64_9HYME Unreviewed; 1126 AA.
AC A0A9R1UB64;
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(XVIII) chain isoform X4 {ECO:0000313|RefSeq:XP_011315029.1};
GN Name=Mp {ECO:0000313|RefSeq:XP_011315029.1};
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_011315029.1};
RN [1] {ECO:0000313|RefSeq:XP_011315029.1}
RP IDENTIFICATION.
RC STRAIN=USDA-PBARC FA_bdor {ECO:0000313|RefSeq:XP_011315029.1};
RC TISSUE=Whole organism {ECO:0000313|RefSeq:XP_011315029.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_011315029.1; XM_011316727.1.
DR AlphaFoldDB; A0A9R1UB64; -.
DR GeneID; 105273967; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000694866; Unplaced.
DR GO; GO:0005588; C:collagen type V 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 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 2.
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_011315029.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694866};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1126
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040472713"
FT DOMAIN 33..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 238..779
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 436..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..565
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1126 AA; 118938 MW; 09888D033F488240 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 SPHDEGITMR PGLPGQKGDA GMPGHPGPKG ESGITGSKGT
KGEPGLKGTK GDHGKDGSRG VQGFKGEPGA PGTPGFPGAP GENGRPAEKG DKGDSGPEGK
QGPPGPSGHV NFGTGGLAGS GTGNGEKGER GESGPRGFKG DLGTKGEKGN KGDSGPSGLP
GINGVQGPQG DKGEPGRDGS AGVPGTGGSK GDRGERGPPG ATTIAGSGDY VTIKGEKGTE
GKRGRRGRPG PPGPPGKSGS AGEIGLPGWP HNSYKGRAGT LGIPRSPGPV GPKGDKGESC
LVNECSSGSG MKGEKGADGF PGAPGRDGQR GLPGPPGPPG ISLIGQKGEP GIGRNHMFGE
RDYYGPRQGA RSSLDELKVI RELKQLKELK EHLGAGKPPT RGAHEVTTKI VPGAVTFQNS
DAMTKMSSVS SVGTLAYIID EEALLVRVNH GWQYIALGSL LPITTVPPPT TVLPPTNPPF
EASNLINQIP MKTDGTGWYP KMLRMAALNE PISGDMHGVR GADYACYRQA RRAGLRGTFR
AFLSSRVQNV DSIVRLDDRD LPIVNIKGDV LFNSWKEMFN GHGAYFSQNP RIYSFNGKNI
LADLAWPEKI VWHGSHKFGD RAMDTYCDAW HSGNSDRYGL GSPITAGRLL EQVRYSCDNK
FALLCIEVTS ESARRRRSIN DNIDNSDNDD LSEQEYQNYL DHITNN
//
