ID A0A6P6Q138_CARAU Unreviewed; 1479 AA.
AC A0A6P6Q138;
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 X7 {ECO:0000313|RefSeq:XP_026127156.1};
GN Name=LOC113108335 {ECO:0000313|RefSeq:XP_026127156.1};
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_026127156.1};
RN [1] {ECO:0000313|RefSeq:XP_026127156.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026127156.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026127156.1};
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_026127156.1; XM_026271371.1.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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..1479
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028154069"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1300
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 282..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..464
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..596
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..650
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..676
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..719
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..735
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..865
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..985
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1092
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1116
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1479 AA; 152179 MW; 7FA1BFA8590590C9 CRC64;
MARRCLAFLE RFLCCVFIAL SPAASQRREE SGVTLLQLIG DPPPDGVSKV FDDANNPGYV
FDQSSNVGQS AAAHLPNPFF RDFSLIFNIK PTTSKPGVIF SITDPTQNFM YVGVKLSAVE
KNKQYIIFYY TEPDSQSSYE AARFPVPSMV NTWTRFSISV LKERVSLYFN CDSDPQVMNF
ERSPDDMDLD AGAGVFVGHA SGADPDRFLG VIGDIRVLKD PGAAERHCEE DEDDFDVNLQ
GSGDYGASGD GEGPPSVQPT PPSSRPIQQP PVTSRPLDEK QQTGSVDSSW QASGSYGDSR
QTSGSYSSSR KTSGSYGDSR KTSVSYGDSR QISGSYGDSE QTSGSYGYSQ TNSGSYGDSR
QSSGSYDGSR QTSGSYGDSR QTLDSVGVSR QTSGSYDDSR RASNSLSTSG SAGDGVRYSV
ESRLGPAGST GAKGDRGEKG AKGDRGVMGQ KGDAGTGSVS GGGAELVKGD AGEKGMKGNP
GFGYPGLKGD RGLPGPPGPP GPPGPSAEVE VTRDGSVVER VAGPRGPPGP PGPPGPAGAD
GEPGDPGEDG KAGQVGPPGF PGTPGSSGLK GEKGDRGESQ PGPRGPPGLP GPPGPPSLSD
RPTFVDMEGS GFDLDSVRAM PGLPGLPGPP GPPGPPGPAG TGSSGSGGFG PPGPPGQNGA
PGQPGLPGPS GADGKPGLPG PKGEKGDAGE LGLPGPVGEK GTKGSPGSPG LPGEGGLAGL
PGPMGPVGPP GPPGPSYHVG FDDMEGSGVH FSSVPGVRGP MGVQGPPGDP GPQGKTGLPG
LPGEKGSEGP QGKDGQPGLD GFPGPQGPRG DKGDRGDRGE PGRDGNGLPG PPGPPGPPGQ
INYHYSENYD ETGRPGPRGG AGLPGQAGFP GPVGPKGDRG EPGSPGYGIK GEKGEPGLIL
GPDGNPFYPG GLISQKGERG LPGPIGPPGP AGPSGLKGEF GMPGRPGRPG VNGYKGEKGE
SGSGSGYGYP GPPGPPGPPG PPGPAVPLDR FGRYEDHSRN YPAMKGEKGD QGAPGVPGSP
GFSSNFDIYA LKNEMKGERG EIGLKGEKGE PGGGFYDPRF GAVQGPPGNP GLPGPKGDSI
RGPPGPQGPP GTPGVGYDGR PGDPGPPGPP GPPGSPSLPG AYRPQLSIPG PPGPPGPPGT
PGSGSGQVAF LRSYDIMMAT ARRQTEGALI YVLDRNDLYL RVRDGIRQVM LGDYKPFYGE
VDNEVAAVQP PPVVHYSQDH TANNGAEQIS PPHPPIEFPR REPENRNPNP PDSRYPDPRY
PPYTDPVQPH RYPVHPERNP STPARHPSHS VNQPEGHVHT SGPGLHLIAL NAPQVGNMRG
IRGADFLCFQ QARAVGLKGT FRAFLSSKLQ DLYSIVRKSD RETLPIVNLK DQVLFRSWES
LFSDSESRMK DNAPIYSFDG RDVLRDSAWP EKMIWHGSSG RGHRQTDNYC ETWRAGDRAV
TGLASSLQAG QLLQQTSSSC SSSYIVLCIE NSYMTQSKK
//
