ID A0AAD3R4C1_LATJO Unreviewed; 1079 AA.
AC A0AAD3R4C1;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X2 {ECO:0000313|EMBL:GLD54525.1};
GN ORFNames=AKAME5_000712700 {ECO:0000313|EMBL:GLD54525.1};
OS Lates japonicus (Japanese lates).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=270547 {ECO:0000313|EMBL:GLD54525.1, ECO:0000313|Proteomes:UP001279410};
RN [1] {ECO:0000313|EMBL:GLD54525.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Kochi {ECO:0000313|EMBL:GLD54525.1};
RA Hashiguchi Y., Takahashi H.;
RT "Genome sequencing of akame (Lates japonicus).";
RL Submitted (AUG-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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:GLD54525.1}.
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DR EMBL; BRZM01000020; GLD54525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD3R4C1; -.
DR Proteomes; UP001279410; 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; 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:GLD54525.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP001279410};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 830..877
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 909..1075
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 43..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..200
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..388
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..634
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..822
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 110029 MW; 413AD7DAA348CC2D CRC64;
MPMSYPPICA KRIRLFQGLP YQGDNQVVGA VCGGRVFDRE RERQGSIQQL VLKSDPTAPD
DQCEEDDPYA SGYGSGDDAY EDIEDREEVK KIVEEREYTM PLPELDPTYS TPVQAPPTEM
SPRGDDEDED TEETSGQEEE MTTVIVRSSQ TTTPASILDT SLQVYPGQKG ERGEPGPAGP
PGPPGPPGQA SGEGGAGEPG PRGPQGPQGS SGPPGAPGKD GEPGSKGEPG LPGATGIPGF
PGLQGEPGPK GDKGDPGVGL PGPPGPPGPP GRAKASMFLE GSGFEDFDSD AEIIRGPPGP
PGPPGQPGPP GSPSEDIIHG PPGAPGKDGK DGQKGEPGLP GVDGKDGDPG PAGEKGDKGE
PGVSGQPGPK GDQGPPGFPG LPGSEGPEGQ PGPRGPSGPP GPPGPPGRSF TFDFEDLEGS
AMQSGFGAVL SRGPQGPPGI PGIPGPKGKD GLDGSPGKPG QKGEPGVIGQ PGFPGLEGLK
GAEGPKGDKG DPGQKGEAGR DGLSIPGPPG PPGPPGPVIN LQDLPLNDTD GAFNFSGIFE
AQGPTGPQGP KGDIGIPGVQ GPPGQKGERG EPGFITAADG SMVSGLVGPV GPKGVKGDSG
VPGPPGVTGP MGPPGIKGEF GFPGRPGRPG LMGPKGERGD SVGLRGPPGP PGPPGRPGIF
NCPKGTVFPI PPRPHCKMAL NPDGSIAGNC QTGLKGDKGE RGLPGMPAPL STYLPRGGWG
TRGDQGIKGE KGDKGEAGMP GLPGIPGRQG LVGPKGESVL GPPGRPGVPG SPGIPGYGRP
GPVGPPGPPG PPGPPGSPSR YGSALTIAGP PGPPGPPGPP GPLGNTASLK TFSSRESMMQ
HTVRDAEGTL TYVTTTGSLF LKVSQGWKEI QLGSLIYLSN NIIPQDEPRV AYQIRGDTME
RISSVKERLN LVALNQPHTG DMMGLDVVDR MCYEQAKAMG LPPNYRAFIS SHRQDLVHVV
YPGFRETLPV TNLRGDVMFR NWRSVFNGDG GPINSRIPIY SFDGRDVLAD PFWPQKSIWH
GSTSRGLRVV DKHCEMWRAD HMSVMGQSSS LTSGLLLGQQ TRSCSNEYIV LCIETHKNP
//
