ID A0A812ELF1_ACAPH Unreviewed; 1150 AA.
AC A0A812ELF1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=COL18A {ECO:0000313|EMBL:CAE1328305.1};
GN ORFNames=SPHA_77843 {ECO:0000313|EMBL:CAE1328305.1};
OS Acanthosepion pharaonis (Pharaoh cuttlefish) (Sepia pharaonis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Sepiida; Sepiina; Sepiidae; Acanthosepion.
OX NCBI_TaxID=158019 {ECO:0000313|EMBL:CAE1328305.1, ECO:0000313|Proteomes:UP000597762};
RN [1] {ECO:0000313|EMBL:CAE1328305.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Farmed {ECO:0000313|EMBL:CAE1328305.1};
RA Li R., Bekaert M.;
RL Submitted (JAN-2021) 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:CAE1328305.1}.
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DR EMBL; CAHIKZ030005524; CAE1328305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A812ELF1; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000597762; 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; 2.60.120.200; -; 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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1089; COLLAGEN TYPE III, PUTATIVE-RELATED; 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.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000597762}.
FT DOMAIN 814..862
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 898..1064
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 136..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..242
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..284
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..295
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..349
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..687
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 119954 MW; F56AABC197D6FD42 CRC64;
MVVKIEKPGI SYIFAVVDSR EMVIQLGVRV ASLSNNAHNV SLYYTPLGVG APYTIRSNVL
ASFRLYNLLG HWAQINFRVK DDTVHVYVNG TRLGEHIVQR SPLSIEDGST IYIGQAGRLL
RGTFVGALQE LKLHSNPDEA EYNDDAYVDD GSGSGSGTDD TDDLINKVSR PPYPRYFKGD
KGEKGERGPP GLPPMISPPP PPPPSARKGE PGIPGAIGLP GVVGQKGQKG EAGGYSGHGA
VGPKGEKGDI GPKGNPGTGL MGPPGQPGKP GIGLKGEPGV GIPGERGSPG IIGPRGLPGP
PGPPGRGGYH STLIDSDSSG DFEYSGVRGV QGPPGPAGRP GYPGEPGRAG VDGKDGVNGW
PGEPGPEGPK GESGRAGYPG EPGIMGQKGE PGRDGANGIP GAHGPPGPPG PPGLSSSVVS
GDDLFEDLSI DASGERSYTR RGVVGEPGLP GHKGEKGDRG ENGYPGETGV QGEKGEIGYN
GIDGRKGEKG EPGVGLRGPP GMPGPPGKSE DTEFKDMTSK IMGMKGDKGD SGRNGLDGIP
GLPGQDGEPG RPGPPGKPGM MMEDTREGCR ECVGEKGDIG PVGPKGDVGR PGPRGVRGSK
GDIGMPGFPG RPGVQGRKGQ PGYGLKGRKG EQGLPGPPGV SIYAGSNGHG GSMKGEKGDR
GYTGREGPPG PPGPPGFPSG LPNPGSGDLD MTFKFFKGDK GDRGRDGIPG RINDIDLSRL
RGPQGPQGRP GPPGPPGLSG NGLTADGLRA PKGERGPKGP KGEPGIGIRG PAGVPGHPGL
SIPGRPGPPG PPGPAGSGSS STYNDRASSG SNGVVTFRNE EELQSVALSV PVGTLAFVMD
TEMLLIRLKE SWAQIEYGNR IPLPTPKPET QKPPIPIQPA RHPGSFSLLR SHEKGSRLHL
IALNEPMRGD MNGISGADGA CYRQAKYSQY KGTYRAFLSS KVQDMRTLIF FKKDRSIPIV
NLMGEVLASS WNDLFDRFGG FFNSSVPIYS FDGSNVLNSI RWPQKILWHG TDPDGKRVKE
NICDGWISDS QTKTGLGSSL VDNKLLGSEE YTCNNAFVVL CISISSGDIH NGVAREENPS
ELMFMPKDQT LSKMINSNDF FFLSFRISLP LILKHFFFLN HFAIFPTKFK PSLQQEMIST
PSLCPVLLLV
//
