ID A0A6P6KU52_CARAU Unreviewed; 1364 AA.
AC A0A6P6KU52;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen type XVIII alpha 1 chain a isoform X7 {ECO:0000313|RefSeq:XP_026074737.1};
GN Name=col18a1a {ECO:0000313|RefSeq:XP_026074737.1};
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957 {ECO:0000313|Proteomes:UP000515129, ECO:0000313|RefSeq:XP_026074737.1};
RN [1] {ECO:0000313|RefSeq:XP_026074737.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026074737.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026074737.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_026074737.1; XM_026218952.1.
DR CTD; 564123; -.
DR Proteomes; UP000515129; Chromosome 34.
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:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
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 ECO:0000313|RefSeq:XP_026074737.1};
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:UP000515129};
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..1364
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028327753"
FT DOMAIN 64..253
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 255..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..347
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..524
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..564
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..592
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..602
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..652
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..751
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..910
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1002
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1364 AA; 140598 MW; E6F67D5548E0A83D CRC64;
MSKLRFWLCL FILVCLRICH THGWFWFDDS KENVKGTQTP AYLTTIRPTS PPRTEPPRTT
EESGVSLLQL IGDPPPDGVS KVFDHDNSPG YVFDQSSNVG QSAAAHLPNP FFRDFSLIFN
IKPTSSKPGV IFSITDPTQN YMYVGVKLSA VEKGKQYIIF YYTEPDSESS YEAARFSVPS
MVNTWTRFSI SVLNERVSLY FNCDSDPQVM SFERSPDDMD LDAAAGVFVG HASGADPDKF
LGVIGDVRVL KDPGAAERHC EEDEDDFDAG SGDYGASGDG EGRPSIQPTP PSSRPIQQPP
VTSRPHVDKQ LTGVKGEKGD RGEKGDKGER GLAGPKGDSG SGSGGSAKGE KGDAGEKGLK
GSSGFGYPGS KGDRGPPGPP GPPGPPGPSA EVEVRGDGSV MQKVTGPRGP PGPPGPPGPA
GAEGEPGDPG EDGKAGQVGP PGFPGTPGSP GPKGEKGERG ESQPGPRGPP GLPGPPGPPS
RSDRPTFVDM EGSGFDLDSV RAMPGLPGLP GPAGPPGLPG PPGPGSSGSG GFGPPGPPGQ
NGAPGQPGLP GLPGADGKPG LAGPKGEKGD AGELGLPGPV GEKGAKGSSG SPGLPGEGGL
AGLPGPMGPV GPPGPPGPPG PRYHVGFDDM EGSGVHFSSV PGVRGPVGIQ GPPGVPGPQG
TPGVPGIPGE KGSEGPQGND GQPGLDGFPG PQGPKGNKGD RGDRGEPGRD GAGLLGPPGP
PGPPGQIIYR YYENNDETGG ARPQGGAGLP GQAGFPGPVG PKGDQGDPGS PGYGIKGEKG
EPGLILGPDG NPFYLGGVIG QKGESGFPGP VGPPGPAGPP GLKGEFGMPG RPGRPGINGY
KGEKGESGSG SGYGYPGPPG PPGPPGPPGP AVPLDRFGRY EDYSRQYPAM KGEKGDQGSP
GVPGSPGFSS NIDIYALKNE MKGEQGEPGL KGEKGEPGGG FYDPHFGAVQ GPPGNPGPPG
PKGDSIRGPP GPQGPPGSPG VGYDGRPGNQ GPPGPPGPPG SPSLPGAYRP QLSIPGPPGP
PGPPGVPGTG SGVTFLRSYD IMMATARRQS EGALIYILDR NDLYLRVRDG VRQVMLGDYN
PFYGELDNEV AAVQPPPVVH YSQDHTADNG AKQISPPHQP IEFPRREPEN RNPNPPDSRY
PDPRYPPYTE PIQPHRHPVQ PERNPSTPAR RPSPPVNQPE GHIHTSGPGL HLIALNSPQV
GNMRGIRGAD FLCFQQARAV GLKGTFRAFL SSKLQDLYSI VRRSDRETLP IVNFKDQVLF
RSWESLFSDS ESRMKDSAPI YSFDGRDVLR DSAWPEKMIW HGSDGRGHRQ TDNYCETWRA
GDRAVTGLAS SLQAGQLLQQ TSSSCSSSYI VLCIENSYMT QSKK
//
