ID A0A672M2F6_SINGR Unreviewed; 1215 AA.
AC A0A672M2F6;
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 type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSSGRP00000030701.1};
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:ENSSGRP00000030701.1, ECO:0000313|Proteomes:UP000472262};
RN [1] {ECO:0000313|Ensembl:ENSSGRP00000030701.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSGRP00000030701.1}
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; A0A672M2F6; -.
DR Ensembl; ENSSGRT00000032970.1; ENSSGRP00000030701.1; ENSSGRG00000017274.1.
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; 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 1.
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1215
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025444388"
FT DOMAIN 65..254
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 322..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..384
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..465
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..534
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..836
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..859
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 127387 MW; 56E6CAC338A2B329 CRC64;
VMSKLRFWLC LFILVCLRIC HTHSWFWFDD SKENVKGAQT PAYLTTVRPT SPPRTEPPRT
TEESGVSLLQ LIGDPPPDGV SKVFDHDNSP GYVFDQSSNV GQSAAAHLPN PFFRDFSLIF
NIKPTSSKPG VIFSITDPTQ NIMYVGVKLS AVEKGKQYII FYYTEPDSQS SYEAARFSVP
SMVNTWTRFS ICVLNERVSL YFSCDSDPQV IPFERSPDDM DLDAGAGVFV GHASGADPDK
FLGFIGDIRV LKDPGAAERH CEEDEDDFDA NSVNSILFNL EQFLKLYCYH YSYCPWCERA
FTYALISLAF WFQGSSGFGY PGSKGDRGHP GPPGPPGPPG PSAEVDVRGD GSVVQRVTGP
RGPPGPAGPP GPAGAEGEPA MPGLPGLPGP PGPPGLPGPP GPGSSGSGGL GPPGPPGQNG
APGQLVSLRD MVHVYTIGLD LLCWNKGAKG SSGSPGLPGE GGLAGLPGPM GPVGQPGPPG
PPGPSYHVGF DDMEGSGVHF SSVPGVRGPV GIQGPPGAPG PHGKPGFPGF PGVKGSEGPQ
GKDGQPGLDG FPGPQGPTGN KGDRGDRGEP GRDGAGLLGP PGPPGPPGQI IYRYTENGGA
GLPGQAGFPG PMGPKGDRGE PGSPGYGIKG EKGEPGLILG PDGNPLYLGG LASHKGESGL
PGPVGPLGPA GPPGLKGEFG MPGRPGRPGV NGYKGEKGEP GSGSGSGSGF AYTVSTPQAL
EFENKWPPGP PGPAVPLDRF GVSAFSMKGE KGDQGAPGVP GSPGFSSNFD IYALKNEMKG
EHGESGLKGE KGEPGGGFYD PRFGAVQGPP GNPGPTGPKG DSIRGPPGPQ GPPGPPGVGY
DGRPGNPGPP GLPGPPGSPS LPGAYRPQLS IPGPPGPPGP PGVPGTGSGV IFLRSYDIMM
ATARRQSEGA LIYILDRNDL YLRVRDGVRQ VMDNEVAAVQ PPPVVHYSQD HTADNGAEQI
SPPHQPIEFP RREPENRNPS PPDSRYPDPR YPPYTDNRYI DPVQPHKYPV QPERNPITPA
RRPSPPVSQP EGHTHTSGPG LHLIALNSAQ VGNMRGIRGA DFLCFQQARA VGLKGTFRAF
LSSKLQDLYS IVRKSDRETL PIVNLKDQVL FRSWESLFSD SESRMKDNAP IYSFDGRDVL
RDSAWPEKMI WHGSSDRGHR QTDNYCETWR AGDRAVTGLA SSLQAGQLLQ QTSSSCSSSY
IVLCIENSYM TQSKK
//
