ID   A0A151WYK8_9HYME        Unreviewed;       961 AA.
AC   A0A151WYK8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JAN-2026, entry version 33.
DE   SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:KYQ52963.1};
GN   ORFNames=ALC60_07689 {ECO:0000313|EMBL:KYQ52963.1};
OS   Mycetomoellerius zeteki.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Mycetomoellerius.
OX   NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ52963.1, ECO:0000313|Proteomes:UP000075809};
RN   [1] {ECO:0000313|EMBL:KYQ52963.1, ECO:0000313|Proteomes:UP000075809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ52963.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYQ52963.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex zeteki WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ982649; KYQ52963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151WYK8; -.
DR   STRING; 64791.A0A151WYK8; -.
DR   Proteomes; UP000075809; 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; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF914; OTOLIN-1; 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:KYQ52963.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT   DOMAIN          676..724
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          765..930
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          31..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..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        512..527
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..579
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..601
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   961 AA;  101143 MW;  EB89E4E8C82F3850 CRC64;
     MKIPQGPPGQ KGDPGTCTCN ATALMSSFTM PKMIQGPKGE PGVPGQEGKQ GLMGLTGAAG
     PPGERGLHGP SGAKGDKGDI GIAGPEGSQG QKGEPGRDGI PGEKGAQGPP GPPGKGEFSG
     YDLSRIIRYF PETDTRQRET QREMVGHIFS RGIVEWQSII TILSMISRSE VHENAREGVS
     QAIVGPRRSV RLPVLLLLRV PKRQLQRSCS HSRSDKKFVE WEWNAYRPAG NKKLCTLIFH
     VKVSGSGSIP ETRFWPQERK EISALSRGRN DPVAPQTVNL PPEMQSFFTL FSCPEGITMR
     PGLPGQKGEP GISGNPGPKG EAGIPGSKGI KGEPGYKGVK GDHGKDGPRG IQGFKGEPGA
     PGAPGLPGAP GENGRPAEKG FGTKGDKGDS GARGYKGDKG TKGEKGNKGD AGPAGIPGIN
     GIQGPQGDKG EPGKDGVSGL PGIPGAKGER GERGPPGATT VANSGDYITI KGEKGAEGKR
     GRRGRPGPPG PVGPPGKPGN MGEIGLPGWM GRSGTPGIPG SIGPMGPKGE KGEPGAPSPY
     GVSVGIKGDK GDDGFPGIPG QPGREGQRGP PGPPGPPGIP SKGNYYPVPG PPGPPGPPGP
     PGLSLIGQKG EPGIGRSHVF GERDYYPPRQ GARSSLDELK ALRELKQLKE LKEQLGVVTA
     ATRGPLESTT KIVPGAVTFQ NTEAMTKMSS VSPVGTLAYI IDEQALLVRV NNGWQYIALG
     SLLPITTPAP PTTSPPPANP PFEASNLINQ IPVKADGTGW YPRMLRMAAL NEPFTGDMHG
     IRGADYACYR QARRAGLRGT FRAFLSSRVQ NVDSIVRLGD RDLPIVNIKG DVLFNSWKEM
     FNGNGAYFSQ NPRIYSFNGK NILTDFAWSE KVAWHGSHKL GDRAMDTYCD AWHSSSSDRY
     GLGSPLTGGR LLEQVRYSCD NKFALLCIEV TSELKSRPCL IATGKEALKN KHFYDYLEAF
     R
//