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Database: UniProt
Entry: F4X517_ACREC
LinkDB: F4X517_ACREC
Original site: F4X517_ACREC 
ID   F4X517_ACREC            Unreviewed;       801 AA.
AC   F4X517;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   28-JAN-2026, entry version 52.
DE   SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:EGI58474.1};
GN   ORFNames=G5I_13440 {ECO:0000313|EMBL:EGI58474.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI58474.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL888680; EGI58474.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4X517; -.
DR   eggNOG; KOG3546; Eukaryota.
DR   InParanoid; F4X517; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000007755; 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   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; 4.
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:EGI58474.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT   DOMAIN          514..562
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          598..763
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          31..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..246
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..289
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..360
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..442
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..464
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  81702 MW;  70B7001A18DF7B60 CRC64;
     MKIPQGPPGQ KGDPGTCTCN ATALMSSFTM PKMIQGPKGE PGVPGQEGKQ GLMGLTGAAG
     PPGERGLHGP SGAKGDKGDI GITGPEGSQG QKGEPGRDGI SGEKGAQGPP GPPGKGEFSG
     YDPEGITMRP GLPGQKGEPG ISGNPGPKGE AGIPGSKGIK GEPGYKGIKG DHGKDGPRGI
     QGFKGEPGAP GAPGLPGAPG ENGRPAEKGD KGDTGPEGKL GPPGPPGPPG VSGSGGINVG
     DLGFGTKGDK GDSGARGYKG DKGTKGEKGN KGDAGPAGIP GINGIQGPQG DKGEPGKDGV
     SGLPGIPGAK GERGERGPPG ATTVANSGDY ITIKGEKGAE GKRGRRGRPG PPGPVGPPGK
     PGNTGEIGLP GWMGRPGTPG IPGSIGPMGP KGEKGEPGAP SPYGVSVGIK GDKGDDGFPG
     IPGQPGREGQ KGPPGPPGPP GIPSKGNYYP VPGPPGPPGP PGPPGLSLIG QKGEPGIGRS
     HVFGERDYYP PRQGVVTTAT RGPLESTTKI VPGAVTFQNT EAMTKMSGVS PVGTLAYIID
     EQALLVRVNN GWQYIALGSL LPITTPAPPT TSPPPANPPF EASNLINQIP VKADGTGLRM
     AALNEPFTGD MHGIRGADYA CYRQARRAGL RGTFRAFLSS RVQNVDSIVR LGDRDLPIVN
     IKGDVLFNSW KEMFNGNGAY FSQNPRIYSF NGKNILTDFA WPEKVAWHGS HKLGDRAMDT
     YCDAWHSSSS DRYGLGSPLT GGRLLEQVRY SCDNKFALLC IEVTSELVRR RRKSTWRSSC
     NTEYSHLRPS FRNAKIESLC K
//
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