ID A0A195CWR9_9HYME Unreviewed; 719 AA.
AC A0A195CWR9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:KYN05085.1};
GN ORFNames=ALC62_04074 {ECO:0000313|EMBL:KYN05085.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN05085.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN05085.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN05085.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN05085.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ977185; KYN05085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195CWR9; -.
DR STRING; 456900.A0A195CWR9; -.
DR Proteomes; UP000078542; 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; 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:KYN05085.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078542}.
FT DOMAIN 429..477
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 518..683
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 53..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..179
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 75778 MW; 353DCCFC43926142 CRC64;
MQTYIDGSVR PTREAFSLAM LFQRSNGEIS IIMRMQPSWK PRNIYRPEGI TMRPGLPGQK
GEPGISGNPG PKGEAGIPGS KGVKGEPGYK GVKGDHGKDG PRGIQGFKGE PGAPGAPGLP
GAPGENGRPA EKGFGSKGDK GDSGARGYKG DKGTKGEKGT KGDAGPAGIP GINGIQGPQG
DKGEPGKDGV SGLPGIPGAK GERGERGPPG ATTVANSGDY ITIKGEKGAE GKRGRRGRPG
PPGPVGPPGK PGNTGEIGLP GWMGRPGTPG IPGSIGPMGP KGEKGEPGAP SPYGVSVGIK
GDKGDDGFPG IPGQPGREGQ RGPPGPPGSP GIPSKGNYYP VPGPPGPPGP PGPPGLSLIG
QKGEPGIGRS HVFGERDYYP SRQGARSSLD ELKALRELKQ LKELKEQLGV VTAATRGPLE
STTKIVPGAV TFQNTEAMTK MSSVSPVGTL AYIIDEQALL VRVNNGWQYI ALGSLLPITT
PAPPTTSPPP ANPPFEASNL INQIPVKADG TGWYPRMLRM AALNEPFTGD MHGIRGADYA
CYRQARRAGL RGTFRAFLSS RVQNVDSIVR LGDRDLPIVN IKGDVLFNSW KEMFNGNGAY
FSQNPRIYSF NGKNILTDFA WPEKVAWHGS HKLGDRAMDT YCDAWHSSSS DRYGLGSPLT
GGRLLEQVRY SCDNKFALLC IEVTSELVRR RRDADNRLDD DVEMSENDYM EYLEEFMQY
//