ID A0A6P6JRQ1_CARAU Unreviewed; 1273 AA.
AC A0A6P6JRQ1;
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 isoform X2 {ECO:0000313|RefSeq:XP_026062378.1};
GN Name=LOC113045878 {ECO:0000313|RefSeq:XP_026062378.1};
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_026062378.1};
RN [1] {ECO:0000313|RefSeq:XP_026062378.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026062378.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026062378.1};
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_026062378.1; XM_026206593.1.
DR AlphaFoldDB; A0A6P6JRQ1; -.
DR GeneID; 113045878; -.
DR Proteomes; UP000515129; Chromosome 27.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 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 ECO:0000313|RefSeq:XP_026062378.1};
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}.
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 229..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..437
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..550
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..646
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..785
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..807
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..832
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..945
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..981
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1064
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 131138 MW; 97CA5EC8D55EAD98 CRC64;
MPRLLRKMKL WLLSWLVGAH LALIYRSSAL HVMEERGSRG HLVLTELVGV PLPPSVSFIT
GYEGFPAYSF GPNANVGRLT QSFVPEPFFM DFAIIVTVKP SNSRGGVLFA ITDPSQRIVH
LGLALTPVED KTQRIVLYYS ESGLADTMEV ASFKVPDMTQ QWNRFTLTVE HEEVRLYMDC
EEYHSAPLKR SQQPLSFEQG SGIFVANAGS TGLERFVGSI QQLVIKPDPR AAEEQCEEDD
PSASGDRSGD GDYDDEEEHG RHEVISQTNV REDKEKTHRP TYPFQAPPTV SPDMDEGEFS
GHVTPTDERL LTGTYKTDET GESTGDGSGQ RQKGERGEPG PTGPPGPPGP PGPSLPPTHS
GQPEQRGPQG PMGPPGRQGR PGKDGQPGLK GEEGKPGQKG PPGPPGLPGE SGVKGEKGDP
GVGLPGPQGP PGPPGPSKPI KVPYGFDALG SGFEDVDMDT ERLRGPPGPP GPPGKPGPPG
PNGALLPGPP GAPGKDGRDG QPGLRAPPGQ DGLTGQQGPK GAKGEQGIRG PSGPKGENGD
PGLVGPMGPR GVPGPPGIPG PPGPPGPLSN NFMVDTLKDL EGSGESRLFL GAGISKGYHG
PPGNPGPPGP QGPPGTDGAP GLSVKGEPGS PGQDGIPGLA GLPGARGPKG DKGNPGEKGE
RGRDGLSITG PPGPPGPPGP TINFQDFLLN DTAAKLNLTK IRGPPGPMGP EGLPGKAGFP
GPRGPKGEIG FPGIQGPPGL KGEKGEPGVS IAADGSVITG LKGPRGPKGM KGDIGPSGRP
GILGPIGPPG QKGEYGLPGR PGRAGIAGRK GDKGDSSGPP GPPGPPGPPG PPGRVIGLNG
TVFPVPPRPH CKIPVNNNNS QQGSGRASLG VKGDKGDVGN PGLPGTAVPL FPHGHVGAKG
DDGYKGQKGE KGDPGLPGSP GLPGRPGLVG PKGDSIVGPP GDTGPSGPPG LPGYGIPGPQ
GPPGPPGPPG TPSAYGSAAS LPGPPGPQGP PGAPGNGNPV RTYKNIQTLI RETNQAAEGT
LAYVIDKSEL YIRVRGGWKK VELGELIPVP QDSSSSALSQ GLSRPSDRSV PRVTSQELKS
LQPDYHVFLQ NSHSVPALHL VALNAPLRGD MHGIRGADYQ CFQQARARGL TSTYRAFLSS
HLQDISSIVR KGDRFSLPVV NLKGDVLFSS WMAMFSGDGA VFDPLTPIYS FDGQNVMTDE
AWPHKVVWHG SNNAGIRMTT SYCEAWRTGD MAVTGQVSLL QTGRLLGQHT RSCSNHFIVL
CIENSYIQNP GKN
//
