ID A0A026WGC2_OOCBI Unreviewed; 789 AA.
AC A0A026WGC2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JAN-2026, entry version 47.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:EZA55023.1};
GN ORFNames=X777_04487 {ECO:0000313|EMBL:EZA55023.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA55023.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA55023.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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DR EMBL; KK107231; EZA55023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026WGC2; -.
DR OMA; YSHERPY; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
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 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; 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 SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:EZA55023.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT DOMAIN 499..547
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 588..754
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 31..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..157
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..421
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 81266 MW; 4B457B89382C9FF4 CRC64;
MKIPQGPPGQ KGDPGTCICN ATALMSSFTM PKMIQGPKGE PGVPGQEGKQ GLMGLTGAAG
PPGERGLQGP SGAKGDKGDI GVLGPEGPQG QKGEPGRDGI PGEKGAQGPP GPPGKGEFSG
YDTDGITMRP GLPGQKGEPG TSGNPGPKGE AGIAGAKGIK GEPGHKGAKG DHGKDGPRGI
QGFKGEPGAP GAPGLPGAPG FGTKGDKGDA GARGYKGDKG TKGEKGDKGD SGPAGIPGIN
GIQGPQGDKG EPGKDGVSGL PGIPGAKGDR GERGPPGATT IANSGDYITI KGEKGAEGKR
GRRGRPGPPG PVGPPGKPGV TGEIGLPGWM GRPGTPGIPG SIGAMGPKGE KGEPGAPSPY
GVSVGIKGDK GDDGFPGIPG QSGRDGQRGP PGPPGPPGQP SQGNFIPVPG SPGPPGPPGP
PGISLRGEKG EPGIGGIGRV HVFGERDYYG TRQGPRSSLD ELKALRELKQ LKELKEQLGV
VTAATRGPLE STTKIVPGAV TFQNTEAMTK MSSVSPVGTL AYIIDEEALL VRVNNGWQYL
ALGTLLPITT PAPPTTAPPP ANPPFEASNL INQIPVKADG IGWYPRMLRM AALNEPFTGD
MHGTRGADYA CYREARRAGL RGTFRAFLSS RVQNVDSIVR LGDRDLPIVN IKGDVLFNSW
KEMFNGNGAY FSQNPRIYSF NGKNILTDFG WPDKVAWHGS HKLGDRAMDT YCDAWHSSSS
DRYGLGSPLT GGRLLEQVRY SCDNKFALLC IEVSSEVIRR RRSINQRPND DVEMTENDYI
EYLEELVQY
//