ID A0A672SUN3_SINGR Unreviewed; 953 AA.
AC A0A672SUN3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0000313|Ensembl:ENSSGRP00000106004.1};
GN Name=col15a1b {ECO:0000313|Ensembl:ENSSGRP00000106004.1};
OS Sinocyclocheilus grahami (Dianchi golden-line fish) (Barbus grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=75366 {ECO:0000313|Ensembl:ENSSGRP00000106004.1, ECO:0000313|Proteomes:UP000472262};
RN [1] {ECO:0000313|Ensembl:ENSSGRP00000106004.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSGRP00000106004.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR AlphaFoldDB; A0A672SUN3; -.
DR Ensembl; ENSSGRT00000112662.1; ENSSGRP00000106004.1; ENSSGRG00000052401.1.
DR Proteomes; UP000472262; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 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; IPR048287; TSPN-like_N.
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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000472262};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..953
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025357098"
FT DOMAIN 34..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..627
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 99669 MW; DF047DD43F50A7D4 CRC64;
MKLWLLSWLV GAHLALSSRS SALHVMEERG SKGHLVLTEL VGVPLPPSVS FITGYEGFPA
YNFGPNANVG RLTQSFVPEP FFMDFAIIVT IKPSNSRGGV LFAITDPSQM IVHLGLALTP
VEDKTQRIVL YYSEPGLADT MEVASFKVPD MTQQWYRFTL TVENEEVRLY MDCEEYHSAP
LKRSQQPLSF KQGSGIFVAN AGSTGLERFV GSIQQLVIKP DPRAAEEQCE EDDPSLQASG
DRSGDGDYDE EEHGRHEVIF GQTNTYRPTY PVQAPPTVSP DMDEGEFSGH VTPIDERLLR
GTYKTDETGE STGDGLKGER GEPGPAGPPG PPGSPGPSLP PTHSGQPGQR GPQGPMGPPG
RQGRPGKDGQ PYGFDALGSG FEDVDIDTER LRGPPGPPGP PGKPGPPGPN GPLGALLPGP
PGTPGKDGRD GQPGLRGENG DPGLIGPMGP RGVPGPPGIP GPPGPPGPLS NDMMNTLKGE
RGRDGLSITG PPGPPGPPGP SINFQDLLLN DTAAKLNLTK IRGPPGPMGP EGLPGRAGFP
GPRGPKGEIG FPGIQGPPGL KGERGEPGVS IAADGSVIPG LRGPRGPKGM KGDIGPSGQP
GIVGPIGPPG QKGEYGLPGR PGRAGIAGRK GDKGDSSGPP VMFVSKGAKG NNGHKGQNGE
KGDPGLPGPP GLPGRTGLVG PKGDSIVGPP GDTGPPGHPG LPGYGIPGPQ GPPGPPGPAG
TPSVRTYKNS QTLIRETSQA AEGTLAYVLD KSELYIRELK SFLPDHVFLQ NAHSMPALHL
VALNAPFTGD MHGIRGADYQ CYQQARARGL TSTYRAFLSS HLQDLSSIVK KGDRFGLPVV
NLKGDALFGS WMAMFSGDGA VFDPLTPIYS FDGRNVMTDQ AWPQKLVWHG SNTAGIRMTT
SYCEAWRTGD MAVTGQASLL QTGRLLGQHT RSCSNHFIVL CIENSYIQNP GRN
//
