ID A0A6P6R4Q5_CARAU Unreviewed; 1278 AA.
AC A0A6P6R4Q5;
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(XV) chain-like isoform X1 {ECO:0000313|RefSeq:XP_026140774.1};
GN Name=LOC113116685 {ECO:0000313|RefSeq:XP_026140774.1};
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_026140774.1};
RN [1] {ECO:0000313|RefSeq:XP_026140774.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026140774.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026140774.1};
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_026140774.1; XM_026284989.1.
DR AlphaFoldDB; A0A6P6R4Q5; -.
DR GeneID; 113116685; -.
DR KEGG; caua:113116685; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000515129; Chromosome 2.
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; 5.
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1278
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028154776"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 228..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..383
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..651
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..953
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..998
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 131643 MW; F1D691C4864C9A23 CRC64;
MLNLLKKMKL WLLLWLVGAH LASDSLSSAL HVMEERGSKD QLVLTELVGV PLPPSVSFIT
GYEGFPAYSF GPHANVGRLT QSFVPEPFFK DFAIIVTVKP SNSRGGVLFA ITDPSQKMVH
LGLALTPVED ETQRIVLYYS ESGLADNMEV ASFKVPDMTQ QWNRFTLTVE HEEVRLYMDC
EEYHSIPLKR SQQPLSFKPG SGIFVANAGS TGMERFVGSI QQLVIKQGPR AAEEQCEEDE
PGLQSSSDGS GDGDYDDEEE HGRREVIFGQ TNEREDKETY RPTFPVQAPP TMLPDMDEGE
VSGHVTPTDE RLLRGTYKTD ETEESTGDGS GQGQKGERGE PGPAGPPGPP GPAGPSLPPI
HSAQPGQRGP QGPVGPPGRQ GTPGKDGQPG SKGEEGKPGK RGPPGLPGLP GESGIKGEKG
DPGVGQPGLP GPPGLPGPPG PAKPTKAPYG FDSLGSGFGD VDIDAERLRG PPGPPGPPGK
PGPPGPNGPL RSLLPGPPGA PGKDGRDGQP GLPGVPGQDG LTGPQGPKGV KGEQGIRGLP
GLKGKNGDPG PIGPIGPRGV PGPPGPPGPP GPLSNNFMMD TLKDLEGSGE SGLFLGAGIS
KGYQGPPGLP GPPGPQGLPG ADGAPGLSIK GEPGSPGKDG ILGLAGLPGA RGPKGDKGSA
GEKGEQGRDG LSITGLPGPP GPPGPIINFQ DLLVNNTASN LNLTKIRGPP GPMGPEGLPG
RAGFPGPRGP KGDIGFPGIQ GPPGLKGEKG EPGISIAADG SVITGLRGPR GPKGMKGDIG
PSGQPGLVGP IGPPGQKGEY GIPGRLGRPG IAGRKGDKGH SSGPPGPPGP PGPPGPPGRV
IGLNRTVFPV PRKPHCKIPV NNNNSQPGNG RVSLGVKGDK GDLGNPGLPG TAVSMFPHDY
VGTNRDNGYK GQKGEKGDPG FPGPPGLPGR TGFVGPKGDS IVGPPGYTGS PGLLGPPGFG
SSGPQGPPGP PGPPGTPSVY GSAASLPGPP GPTGPPGAPG HGNPVKTYLN TQTLIRESSE
GAEGTLAYVI DKSELYIRVP GGWKKVELGK LIPVSQDSST SALSQGLSRP SDHSVPKEHS
QELKSFLSGY HVFSQHAHSV PALHLVALNA PFSGDMHGIR GADYQCYQQA RARGLTSTYR
AFLSSHLQDL SSIVKKGDHF SLPVVNLKGD VLFRSWMSMF SGNGAVFDPL TPIYSFDERN
IMTDQAWPQK LVWHGSSTAG IRMTSNYCEA WRTDDMAVTG QASLLQTGRL LGQHTRSCSN
HFIVLCIENS YIQSPERN
//
