ID A0A4U5U2L3_COLLU Unreviewed; 1100 AA.
AC A0A4U5U2L3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 16.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|EMBL:TKS67621.1};
GN ORFNames=D9C73_001055 {ECO:0000313|EMBL:TKS67621.1};
OS Collichthys lucidus (Big head croaker) (Sciaena lucida).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Collichthys.
OX NCBI_TaxID=240159 {ECO:0000313|EMBL:TKS67621.1, ECO:0000313|Proteomes:UP000298787};
RN [1] {ECO:0000313|EMBL:TKS67621.1, ECO:0000313|Proteomes:UP000298787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JT15FE1705JMU {ECO:0000313|EMBL:TKS67621.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TKS67621.1};
RA Cai M., Xiao S.;
RT "Genome Assembly of Collichthys lucidus.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM014079; TKS67621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5U2L3; -.
DR STRING; 240159.A0A4U5U2L3; -.
DR Proteomes; UP000298787; Chromosome 2.
DR GO; GO:0005587; C:collagen type IV trimer; 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 FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
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: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.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:TKS67621.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000298787}.
FT DOMAIN 766..812
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 926..1094
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 145..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..627
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..641
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 119171 MW; D51CB2A81EFAB935 CRC64;
MKDTWTRFAI AVRDEKVMFY LNCDIDPQVM RIERSPDEME LEAGAGVFVG QAGGADPEKF
LGVIGELRVV GDPRAAERHC EEDEDDSDVQ ATPSTFHFLW SPGLDFPGHQ GQLGLKEKGV
TEGIEERKET GVLLGRRENL VLAPAHEVEP VEKRENQEKR EQREVQALAT KERRESPALK
GRPVLLGLQG LQMRFQSAVM DQLLPGSLDH EDHLDHQVPQ DPRDQQELME SQVLMDHEAS
QESQETLDSE ERREIVEMVS LAPGDHQDHQ DPQDLDSDLD CQAHQVLLAP LVLLVLLLQA
QDLLLGHLDH QERMEHPVNR ACLVCQVLME FQEFLVPKEK RVTQASWVFQ EQLERSKTPT
FPFSPICCPH YLSSSYFPKS SHLQGAQGEP GLAGPPGDTG LAGLPGPMGP VGPPGPPGPP
GSSYRVGFDD MESSGGGFFN GLPGVRGPEG RQGKPGFPGL PGPKGNDGLM GRDGQPGLDG
FPGPQGDPGR DGTGLPGPPG PPGPPGQIIY QTSGNLDGSF GSVGSEGPIG PKGDRGDPGP
PGYSVKGEKG EPGLIIGPDG NLLTLEGLTG VKGDRGPAGP VGPPGQYGPT GLKGEIGMPG
RPGRPGVNGY KGEKGEPGGG SGYGYPGVPG PPGPPGPPGP ANPFDRFNQL KVKKEIVASK
EFQESQNELK GERGEAGVKG EKGEAGGGYY DPRFGGAQGP SGPPGKPGLP VSSEGSKGRC
CNRPSWTSGP TRNTRHWLLT GVQVLQDHLD LQDHPHSLEH IDPITVTVLR SYDTMLATAR
RQTEGSLIYI IDKADLYLRV RDGLRQVMLG DYNPFFRDLE NEVAEVQPPP VILYPQSQDQ
SQNNGAGHYS QGGSVVRPIE PPPQPPVDRY PPRYDPIFPD PRNTGHTDGR LATQQTENRY
PVTPQRRPHP PVPQPGGHVE ASGTGLHLIA LNTPQTGNMR GIRGADFLCF QQARAVGLKG
TFRAFLSSKL QDLYTIVRRT DRDSLPIMNL KDQVLFSSWE SIFGDEAFKM RQNVPIYSFD
GRDILRDSAW PEKMVWHGSS NKGHRQTDHY CETWRAGDRA VTGLASSLQS GHLLQQTSSS
CSGSYIVLCI ENAFTSHSKK
//
