ID A0A6I9WIY6_9HYME Unreviewed; 971 AA.
AC A0A6I9WIY6;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain isoform X8 {ECO:0000313|RefSeq:XP_011642996.1};
GN Name=LOC105430905 {ECO:0000313|RefSeq:XP_011642996.1};
OS Pogonomyrmex barbatus (red harvester ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Pogonomyrmex.
OX NCBI_TaxID=144034 {ECO:0000313|Proteomes:UP000504615, ECO:0000313|RefSeq:XP_011642996.1};
RN [1] {ECO:0000313|RefSeq:XP_011642996.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_011642996.1; XM_011644694.2.
DR AlphaFoldDB; A0A6I9WIY6; -.
DR GeneID; 105430905; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000504615; 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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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_011642996.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000504615};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 680..728
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 770..935
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 67..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..91
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..219
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..531
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 971 AA; 100408 MW; 959BF1B05A61EF2C CRC64;
MAMVISPRSK IVTLSLLIGI ITLVALIITG VIGIWSGKSE KTNGTQTKMI SSKLQQITGY
AAMQHISRDA DEDKSEESNP PPFITPPPPN PDYKGPKGEK GDKGEKGESV RGPPGPPGPP
GRDEDWLMKI PQGPPGQKGD TGSCTCNATA LMSSFTMPKM IQGPKGEPGV PGQEGKQGLM
GLTGAAGPPG ERGLQGPSGA KGDKGDIGIP GPEGPQGQKG EPGRDGIPGE KGAQGPPGPP
GKGEFSGYDP SWKPRNIYRP EGITMRPGLP GQKGEPGTSG SPGPKGESGI PGSKGIKGEP
GHKGAKGDHG KDGPRGIQGF KGEPGAPGAP GLPGAPGENG RPAEKGDKGD TGPEGKPGPP
GPPGPSGIGG PGGINVGDLG FGIRGDKGDS GARGYKGDKG TKGEKGDKGD SGPAGIPGIN
GIQGPQGDKG EPGKDGVSGL PGIPGTKGER GERGPPGATT IANSGDYITI KGEKGAEGKR
GRRGRPGPPG PVGPPGKPGI TGEIGLPGWM NTIKGRPGTP GIPGSIGPMG PKGEKGEPGA
PSPYGVSLGI KGDKGDDGFP GIPGQPGRDG QRGPPGPPGP PGAPSQGKYI PVPGPPGPPG
PPGPPGLSLI GQKGEPGIGR SHVFGERDYY GPRQGARSSL DELKALRELK QLKELKEQLG
VVTAATRGPL ESTTKIVPGA VTFQNTEAMT KMSSVSPVGT LAYIIDEQAL LVRVNNGWQY
IALGSLLPIT TPAPPTTSPP PANPPFEASN LINQIPVKAD GTGQWYPRML RMAALNEPFT
GDMHGIRGAD YACYRQARRA GLRGTFRAFL SSRVQNVDSI VRLGDRDLPI VNIKGDVLFN
SWKEMFNGNG AYFSQNPRIY SFNGKNILTD FAWPEKVAWH GSHKLGDRAM DTYCDAWHSS
SSDRYGLGSP LTGGRLLEQV RYSCDNKFAL LCIEVTSELG RRRRSAGNRP DDDIEMTEND
YMEYLEELMQ Y
//
