ID A0A226E197_FOLCA Unreviewed; 901 AA.
AC A0A226E197;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|EMBL:OXA50747.1};
GN ORFNames=Fcan01_14008 {ECO:0000313|EMBL:OXA50747.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA50747.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA50747.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA50747.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA50747.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA50747.1}.
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DR EMBL; LNIX01000008; OXA50747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226E197; -.
DR OMA; YSHERPY; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000198287; 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 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; 2.
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:OXA50747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287}.
FT DOMAIN 578..624
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 661..827
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 88..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..271
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..569
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..889
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 95572 MW; BCC4E6DF77D440E9 CRC64;
MPKIKMTTIH LVHLVTNKFF HCIVAFLFFK GAIQELKLYG MPGVAEVQCD DSLSSFGSTE
GSAGGVDFDG VESEGFYDYP SYDDDYGDFG EDGHLGSGDD SIPPPPPRPP PSPHDTNGTD
HFNLTGLFGS SDAKESGGSK SGVRAFSPDP NKPNNNVPRL VGSNNNNPKT KSFWGTEIKS
PSFYENEPFD TGGVGGVCLC NYTEIVSKLP ETLRGLPGPI GEMGIQGEAG PMGVKGERGL
KGDRGDIGMT GPEGVQGQKG EPGLVGPQGL VGPPGPPGMQ ASPSFLGSDD TLGGPSLMSR
SIMGPKGEVG ESGPSGAKGE RGYMGEKGER GLTGPSGERG LAGPPGVDGY PGRDGAKGSQ
GGKGERGERG LPGPATPISS DMTGILTNTV VEPVKGEPGP QGDRGLPGLK GDKGDIGPAG
PPGPGAAFDY EGDLKVGDKG DIGRRGKRGR PGLPGPRGPS GEIGIPGWPG RPGLAIQGPK
GDKGEPAVLP DNFFKYEVSG TAGKPGPQGP PGPPGPPGKV EYIERTPQYV PVPGPQGPPG
LSIVGEKGEP GPPGPPGDSS SARFSGSESS SKVVPGAVVV LTRESMLKMS QLSPVGTITF
VKDEETLFVR VSEGWKPLLM GALVRAEPIM AHVDLTTESP PVARPPFEVS SLINRIEGPS
LRIAALNDPW SGDMHGVRGA DYACYRQARN ANLQGTFRAF LSSWVQNLDS IVKFSDRNLP
VVNTKGDLLF NSWGEIFQNG GKIQTRPPKL FSFGGKNVMQ DFHWPQKMVW HGADPSGVRA
RQSYCEAWHS DSSSNVGLAS DILKHELLMG QEKIGCNNKL IVLCIEIASQ HHYRRRRRDL
DQNNDVDDEP LKNIQRHDDD LTYEQYTHFL EQYDQHHPHH HPQHHHQHNH STQSPNPLTV
V
//
