ID A0A6P6Q299_CARAU Unreviewed; 1478 AA.
AC A0A6P6Q299;
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 alpha-1(XVIII) chain-like isoform X8 {ECO:0000313|RefSeq:XP_026127157.1};
GN Name=LOC113108335 {ECO:0000313|RefSeq:XP_026127157.1};
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_026127157.1};
RN [1] {ECO:0000313|RefSeq:XP_026127157.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026127157.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026127157.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_026127157.1; XM_026271372.1.
DR GeneID; 113108335; -.
DR Proteomes; UP000515129; Chromosome 9.
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; 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 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1478
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028385110"
FT DOMAIN 31..220
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..251
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..316
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..463
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..504
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..595
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..649
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..675
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..718
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..734
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..775
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..864
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..984
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1049
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1478 AA; 152050 MW; 00263EF2CF294A77 CRC64;
MARRCLAFLE RFLCCVFIAL SPAASQRRES GVTLLQLIGD PPPDGVSKVF DDANNPGYVF
DQSSNVGQSA AAHLPNPFFR DFSLIFNIKP TTSKPGVIFS ITDPTQNFMY VGVKLSAVEK
NKQYIIFYYT EPDSQSSYEA ARFPVPSMVN TWTRFSISVL KERVSLYFNC DSDPQVMNFE
RSPDDMDLDA GAGVFVGHAS GADPDRFLGV IGDIRVLKDP GAAERHCEED EDDFDVNLQG
SGDYGASGDG EGPPSVQPTP PSSRPIQQPP VTSRPLDEKQ QTGSVDSSWQ ASGSYGDSRQ
TSGSYSSSRK TSGSYGDSRK TSVSYGDSRQ ISGSYGDSEQ TSGSYGYSQT NSGSYGDSRQ
SSGSYDGSRQ TSGSYGDSRQ TLDSVGVSRQ TSGSYDDSRR ASNSLSTSGS AGDGVRYSVE
SRLGPAGSTG AKGDRGEKGA KGDRGVMGQK GDAGTGSVSG GGAELVKGDA GEKGMKGNPG
FGYPGLKGDR GLPGPPGPPG PPGPSAEVEV TRDGSVVERV AGPRGPPGPP GPPGPAGADG
EPGDPGEDGK AGQVGPPGFP GTPGSSGLKG EKGDRGESQP GPRGPPGLPG PPGPPSLSDR
PTFVDMEGSG FDLDSVRAMP GLPGLPGPPG PPGPPGPAGT GSSGSGGFGP PGPPGQNGAP
GQPGLPGPSG ADGKPGLPGP KGEKGDAGEL GLPGPVGEKG TKGSPGSPGL PGEGGLAGLP
GPMGPVGPPG PPGPSYHVGF DDMEGSGVHF SSVPGVRGPM GVQGPPGDPG PQGKTGLPGL
PGEKGSEGPQ GKDGQPGLDG FPGPQGPRGD KGDRGDRGEP GRDGNGLPGP PGPPGPPGQI
NYHYSENYDE TGRPGPRGGA GLPGQAGFPG PVGPKGDRGE PGSPGYGIKG EKGEPGLILG
PDGNPFYPGG LISQKGERGL PGPIGPPGPA GPSGLKGEFG MPGRPGRPGV NGYKGEKGES
GSGSGYGYPG PPGPPGPPGP PGPAVPLDRF GRYEDHSRNY PAMKGEKGDQ GAPGVPGSPG
FSSNFDIYAL KNEMKGERGE IGLKGEKGEP GGGFYDPRFG AVQGPPGNPG LPGPKGDSIR
GPPGPQGPPG TPGVGYDGRP GDPGPPGPPG PPGSPSLPGA YRPQLSIPGP PGPPGPPGTP
GSGSGQVAFL RSYDIMMATA RRQTEGALIY VLDRNDLYLR VRDGIRQVML GDYKPFYGEV
DNEVAAVQPP PVVHYSQDHT ANNGAEQISP PHPPIEFPRR EPENRNPNPP DSRYPDPRYP
PYTDPVQPHR YPVHPERNPS TPARHPSHSV NQPEGHVHTS GPGLHLIALN APQVGNMRGI
RGADFLCFQQ ARAVGLKGTF RAFLSSKLQD LYSIVRKSDR ETLPIVNLKD QVLFRSWESL
FSDSESRMKD NAPIYSFDGR DVLRDSAWPE KMIWHGSSGR GHRQTDNYCE TWRAGDRAVT
GLASSLQAGQ LLQQTSSSCS SSYIVLCIEN SYMTQSKK
//
