ID A0A6P6N8R3_CARAU Unreviewed; 1188 AA.
AC A0A6P6N8R3;
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 X2 {ECO:0000313|RefSeq:XP_026104624.1};
GN Name=LOC113076180 {ECO:0000313|RefSeq:XP_026104624.1};
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_026104624.1};
RN [1] {ECO:0000313|RefSeq:XP_026104624.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026104624.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026104624.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR RefSeq; XP_026104624.1; XM_026248839.1.
DR AlphaFoldDB; A0A6P6N8R3; -.
DR GeneID; 113076180; -.
DR Proteomes; UP000515129; Unplaced.
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 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; 1.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
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..1188
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027857354"
FT DOMAIN 35..223
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 225..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..314
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..391
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..581
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..754
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..918
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 122461 MW; E18989148DBCA3EF CRC64;
MGPVLSRVWC WTFLSICSSG IGFQRLDSEQ DSSAQLDLTE LIGVPLPPSV SFVSGLEGFP
AYSFGPDANV GRLTRSFIPD PFYRDFSIIV TARPSSRRGG VLFAITDALQ KIVHLGVSLA
PVEDGSQRVV LYYTEPGAAH TQEAASFKMG DLTGRWARFT LAVQGEEVRL YMDCEEQHRV
AFRRSPDGLT FQPSSGIFIG NAGGTRLERF LGSIQQLLLT PDPSALNEQC EEDDPYASGY
GSGDDIYDDM ETPDEVKKVF EEREYVMSED VESGPMRAPP TESPSFSTET DDEDLEEGSG
EDIIIISEPI RSEGASQDRN VITMQKGEKG ERGPPGPPGS TTPHTPGEPG PRGPQGAPGE
PGRDGRPGDP GKGGAPGEAG PPGFPGLPGD PGPKGDKGDP GVGIPGPPGP PGPPGTYKYS
EHSGSGDVDL DSDAELIQGP PGPPGPPGPP GPSVGAHPGP IGPPGAPGRD GEKGKPGVPG
EHGQNGQPGK DGEKGQKGEA GLPGITGPKG DAGQPGLPGQ TGTEGPKGQS GPPGPPGPPG
TGFSFDMMDL EGSGLDESSG FRPVLPRGPP GLPGLPGPPG PQGKEGAVGP PGVSVKGEPG
AKGDDGQTGA PGLPGRQGEG GEKGDKGQKG ERGLDGISLP GPPGPPGPPG PIINLQLMLN
DTEGIFNLSG IFEPQGPLGP RGLKGDTGVP GVQGSPGLKG QKGEPGIVSG VHAPQGPKGL
KGDCGVPGPP GQTGPVGPKG EFGFPGRPGR PGVNGRKGEK GDSVGLPGVP GPPGPPGRAG
PFSCPTATVF PVPPRPGCKT PVTSGSTQEG ASRDRHLPSS SSSGHTLGNK VTTDPGSRGE
TGETGMSGRP GSAGAKGESI TGPPGHPGPR GPPGAPGFGR IGVAGPPGPP GPPGPPGPPG
QLRPGVMIPG PPGPPGPPGR AAEASSAVRK YVSVQAMSQQ SSAVERGTLS FVTDSSKLYI
KVPGGWREVQ LGGMIEMYPV LSQDDAEPLI LSPPLRHTPR THTRSTLRLV ALNTPLTGNL
GSIHSVNKLC RTQAQAMGIR DDYQAFLSHH LQDLIDTVQP MYRANMPIVN LRGEVLFRSW
HSIFSSHLLP PGVPLYSFDG RDVMSDPFWP QKALWHGSSE RGERLSSLNC ESWRAGDMAI
TGQASFLYSG LLNQQTRSCS NRFIVLCIQT SHEHQTLPQL HRRLQHRS
//
