ID A0A6P6MBI9_CARAU Unreviewed; 1217 AA.
AC A0A6P6MBI9;
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 isoform X3 {ECO:0000313|RefSeq:XP_026094055.1};
GN Name=col15a1a {ECO:0000313|RefSeq:XP_026094055.1};
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_026094055.1};
RN [1] {ECO:0000313|RefSeq:XP_026094055.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026094055.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026094055.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR RefSeq; XP_026094055.1; XM_026238270.1.
DR AlphaFoldDB; A0A6P6MBI9; -.
DR CTD; 792366; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000515129; Chromosome 49.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_026094055.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000515129};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1217
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028087957"
FT DOMAIN 35..223
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..949
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 338..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..574
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..618
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..764
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..841
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..900
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1217 AA; 125280 MW; 94D0B75F1A833EF0 CRC64;
MGRARDASLL SRVWCWSFIT VCLCSSASER VSSAQLDLTE LIGVPLPPSV AFITGFEGFP
AYSFGPDANV GRLTRSFIPD PFYRDFSIIV TARPSSRRGG MLFAITDALQ KIVHLGVSLA
PVEDGSQRVV LYYTEPGAAH TQEAASFKMG DLTGRWARFT LAVQGEEVRL YMDCEEHHRV
AFRRSPDGLT FQPSSGIFIG NAGGTRLERF VGSIQQLLLS ADPSAPNEQC EEDDPYASGF
GSGDDIYDDT ETPNEVKKVV EEREYTMPED IESGPMRAPP TESPSSITET DDEDLEEGSG
EDIIISSGPK EPIRSEGALQ DRNVITMQKG EKGERGPQGP PGPAAPHTPG EPGPRGPQGP
AGPPGEPGQD GQPGVPAKDG APGETGPPGF PGLPGDPGPK GDKGDPGVGI PGPPGPPGPP
GTFKYPGGID GSGSSFVDED SETELIRGPP GPPGPQGRPG PPGPSVGAQP GPTGPPGAPG
RDGETGKPGL PGENGRDGQT GKDGEKGQKG EAGLPGLMGP KGDAGQPGLP GQTGSEGPRG
QPGPPGPPGQ GFSFDMMDLE GSGLDGSSGF RPVLPRGPPG LPGLPGPPGP QGKEGAVGPP
GVSVKGEPGA RGGDGQPGSS GPPGPQGERG EKGDMGQKGE RGQDGVGLPG PPGPPGPLIN
LHELMLNDTE GIFNLSQIFE AQGPLGPRGP KGDTGAPGFQ GPPGLKGQKG EPGTVSGVHA
PQGPTGLKGD RGVPGPPGQT GPIGPAGPKG EFGFPGRPGR PGVNGRKGEK GDSVALPGPP
GPPGPPGRPG IFSCPRGTVF PVPPRPRCKM PVNSDSTQEG ASRDLPSSSS SSSSSSSSSS
SGNTLGTRVT AEKGDQGFGG EKGEAGMPGL PGRSGSAQGA KGESITGPPG HPGPRGPPGA
PGLGRIGVAG PPGPPGPPGP PGQHTSGVMI PGPPGPPGPP GRAADASSAV RTCVSLQALR
QQSSAVEDGT LTLVLDSSKL YIKVPGGWRE VQLGGLIETH SPVLSQDDAG PLILTPHIRN
TPITHSGNAL RLVALNTPLT GNLGSIHSVN KLCRTQAQAM GIRDDYKAFL SHHLQDLIDT
VQPMYRTNMP IVNLRGELLF KNWDSIFSDH LLPPGVPLYS FDGRDVLSDP FWPQKALWHG
SSERGERLSS LNCESWRASD MAITGQASFL YSGLLNQQTR SCSNRFIVLC IETSHDHRTM
EELHTARDRH RRWFHGY
//
