GenomeNet

Database: UniProt
Entry: A0A8S1C2X8_9INSE
LinkDB: A0A8S1C2X8_9INSE
Original site: A0A8S1C2X8_9INSE 
ID   A0A8S1C2X8_9INSE        Unreviewed;       804 AA.
AC   A0A8S1C2X8;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 14.
DE   RecName: Full=Collagenase NC10/endostatin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CLODIP_2_CD05047 {ECO:0000313|EMBL:CAB3362315.1};
OS   Cloeon dipterum.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Palaeoptera; Ephemeroptera; Pisciforma; Baetidae; Cloeon.
OX   NCBI_TaxID=197152 {ECO:0000313|EMBL:CAB3362315.1, ECO:0000313|Proteomes:UP000494165};
RN   [1] {ECO:0000313|EMBL:CAB3362315.1, ECO:0000313|Proteomes:UP000494165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T., Gomez Garrido J.;
RL   Submitted (APR-2020) 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:CAB3362315.1}.
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DR   EMBL; CADEPI010000008; CAB3362315.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8S1C2X8; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000494165; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494165}.
FT   DOMAIN          523..570
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          610..776
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          14..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..53
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..63
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..203
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..379
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..420
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..434
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   804 AA;  83291 MW;  44EE2E9A84A51122 CRC64;
     MHLWCNNTFL NCSDGLKGEK GEKGERGPPG EVLRGPPGPP GEPGYGGNGG GDFLSGEGIS
     RGPIGPPGPP GTCTCNTSMI FGPDGQIPDL IPGPPGMPGR DGKTGQPGLS GLPGPTGERG
     APGQRGEKGD RGDGGPQGLE GQPGQKGEPG RDGTPGLQGL PGPPGSPGNS DYTNYDPGWR
     PRGNLKDSLL GGSGFSQGMG RPGSPGPKGE KGDGGPHGPR GERGVPGNKG DRGEAGTRGQ
     KGDKGHQGSI GYQGFKGERG EPGIDGMPGM PGENGLPGGR GDKGDMGPMG PPGPPAINAA
     SLIAGDNLLS TEKGDKGDKG DTGYPGVDGK DGYPGTKGEP GELISTDGKS LKGDRGERGK
     RGKRGEPGPP GPPGPPGPVG PRGDFGLPGW GVKGDKGDSG SKGEPGEGEG LLPKGLHYVP
     VPGPPGPPGP PGPPGISIQG EKGDAGPPGE PGFHSYRPPS PVYGDPTLTG KHGSARGSLE
     ELRFIKQMKD MKDGLAPMIH HSGHQHHHEA PPPPPQVKIV PGAVTFQNAE TMIKMSSASP
     VGTIAFLLDE EALLVRVKSG WQYIALGNLV SVDSTVPPEV MTTTEPTIVP PFKPQLKVSN
     QLKTVDGPHL RIAALNEPTS GNMHGVRGAD YNCYRQARRA NLRGTFRAFL ASRVQDLDSI
     VRSSDRDLPV LNIKGDVLFN SWNELFNGDG ALFLGQSRIY SFSGRNILTD QTWPLKAIWH
     GSQLLGERAV DTYCEAWHSE SMDKLGLGSS LLKGRLLGQE RFTCDQKLIV LCVEATSIAR
     SRRSIPEDKI LSESDYNALI SGVN
//
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