ID A0A671T5U7_9TELE Unreviewed; 1333 AA.
AC A0A671T5U7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like {ECO:0000313|Ensembl:ENSSANP00000103914.1};
GN Name=LOC107660582 {ECO:0000313|Ensembl:ENSSANP00000103914.1};
OS Sinocyclocheilus anshuiensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000103914.1, ECO:0000313|Proteomes:UP000472260};
RN [1] {ECO:0000313|Ensembl:ENSSANP00000103914.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSANP00000103914.1}
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 Ensembl; ENSSANT00000110283.1; ENSSANP00000103914.1; ENSSANG00000050911.1.
DR Proteomes; UP000472260; 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; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1060; COLLAGEN ALPHA-1(IV) CHAIN; 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:UP000472260};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1333
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025525045"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..252
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..274
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..320
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..500
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..520
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..559
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..569
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..718
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..943
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1333 AA; 136914 MW; 6B268D9AFE18CD22 CRC64;
MARRCLAFLE RFLCCVFIAL SPAASLWREE SGVSLLQLIG DPPPDGVSKV FDDANNPGYV
FDQRSNVGQS AAAHLPNPFF HDFSLIFNIK PTSSKPGVIF SITDPTQNIM YVGVKLSAVE
KGKQYIIFYY TEPDSQSSYE VARFSVPSMV NTWTRFSISV LNERVSLYFN CDSDPQVISF
ERSPDDMDLD AGAGVFVGHA SGADPDKFMG VIGDIRMLKD PGAAERHCEE DEDDFDANLQ
GSGDYGASGD GEGPPSVQPT PPSSQPIQQP PVTSRPLVEK QQTGAKGEKG DRGEQGAKGD
RGLVGPKGDA GSGSVSGGGA KEVKGDAGEK GIKGNPGFGY PGSKGDRGPP GPPGPPGPAG
PSAEVEVRGD GSVLQRVAGP RGPPGPSGPP GPAGADGEPG DPGEDGKAGQ VGPPGFPGTP
GSLGLKGEKG ERGESQPGPR GPPGPPGPPS RSDRPTFVDM EGSGFDLDSV PAMPGLPGLP
GPPGPPGPPG TGSSGSGGFG PPGPPGQNGA PGQLGLPGPS GADGKPGLPG PKGEKGDAGE
LGLPGPVGEK GAKGSSGSPG LSGEGGLAGL PGPMGPVGPP GPPGPPGPSY HVGFDDMEGS
GVHFSSVPGV RGPVGIQGPP GAPGPQGKPG FPGFPGEKGS EGPQGKDGQP GLDGFPGPQG
PRADKGDRGD RGEPGRDGNG LPGPPGPPGP PGQIIYRYSE NYDETGGPGP QGGAGFPGQA
GFPGPMGPKG DRGEPGSPGY GIKGEKGESG LILGPDGNPH YLGGLTGQKG ERGLSGPVGS
PGPAGPFGLK GEFGMPGRPG RPGVNGYKGE KGEPGSGSGY DYPGPPGPPG PPGPPGPAVP
LDRFGRYEDY SRHYPAMKGE KGDQGAAGVP GSPGFSSNID IYALKNEMKG EHGEPGLKGE
PGGGFYDPRF GAVQGPPGNP GLPGPKGDSI RGPPGPQGPP GPPGVGYDGR PGNPGPPGAP
GPPGSPSLPG AYRPPLSIPG PPGPPGPPGI PGTGSGVAFL RSYDIMMATA RRQTEGALIY
ILDRNDLYLR VRDGVRQVML GDYKPFYGGL DNEVAAVQPP PVVHYSQDHT ANNGAEQISP
PHPPIEFPRR EPENRNPNAP DSRYPDQRYP PYTDNKYTDP VQPHRYPVQP ERNPITPARH
PSPPVNQPEG HVHTSGPGLH LIALNSPQVG NMRGIRGADF LCFQQARAVG LKGTFRAFLS
SKLQDLYSIV RKSDRETLPI VNFKDQVLFR SWESLFSDSE SRMKDNAPIY SFDGRDVLRD
SAWPEKMIWH GSSGRGHRQT DNYCETWRAG DRAVTGLASS LQAGQLLQQT SSSCSSSYIV
LCIENSYMTQ SKK
//
