ID A0A671MT08_9TELE Unreviewed; 1010 AA.
AC A0A671MT08;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen, type XV, alpha 1b {ECO:0000313|Ensembl:ENSSANP00000033695.1};
OS Sinocyclocheilus anshuiensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000033695.1, ECO:0000313|Proteomes:UP000472260};
RN [1] {ECO:0000313|Ensembl:ENSSANP00000033695.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSANP00000033695.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A671MT08; -.
DR Ensembl; ENSSANT00000035882.1; ENSSANP00000033695.1; ENSSANG00000016968.1.
DR Proteomes; UP000472260; Unassembled WGS sequence.
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; 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; 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:UP000472260};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 17..205
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 204..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..412
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..643
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..728
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..751
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 105185 MW; 22F1DD61B98ED20B CRC64;
SLSSALHVMA ERGSKGHLVL TELVGVPLPP SVSFITGYEG FPAYNFGPHA NVGRLTQSFV
PEPFFKDFAI IVTIKHSNSR GGVLFAITDP SQKIVHLGLA LTPVEDKTQR IVLYYSEPGL
ADTMEVASFK VPDMTQQWSR FTLTVEHEEV RLYMDCEEYH SAPLKRSQQP LSFKLGSGIF
VANAGSTGLE RFVGSIQQLV IKQDPRAAEE QCEEDDPSLQ SSGDGSGDGD GDYDDEEEHG
RREVIFGRTN EKEDKEKTHR PTFPVQAPPT MLPDMDEGEV SGHVTPVDQR LFPLELCQGS
GQGQKGERGE PGPAGPPGPP GPPGPSLPPI HPGQPGRRGP QGPVGPPGRQ GRPGKDGHPY
GFDALGSGSG DVDIDTELLR GPPGPPGPPG KPGPPGPNGP LRGLLPGPSG APGKDGRDGQ
PGLPVSMFFS FQLNQMVCVP SVFLALSHTK THSLSLSLSL SLSLSFHSSG VPGSPGPPGP
PGPLSNNFMM DTLKGEQGRD GLSIIGLPGP PGPPGPIINF QDLLLNDTAA KLNLSKIRGP
PGPMGPEGLP GRAGFPGPRG PKGEIGFPGI QGPPGLKGEK GEPGVSIAAD GSLITGLRGP
RGPKGMKGDI GPSGQPGIVG LIGPPGQKGE YGLPGRPGRP GIAGRKGDKG HSSGPPGPPG
PPGPPGPPGR VIGLNGDAKG DIGYKGQKGE KGDPGLPGPP GLRGKTGLVV PKGDSIVGPP
GDTGSPGLPG LPGYGSPGPQ GPPGPPGPPG TPSAYGSAAN IPGPPGHPGP PGAPGHGNLV
RTYKNTQTLI RETSQGAEGT LAYVIDKSEL YIRELKSFLP GYHVFPQHAH SVPALHLVAL
NAPFSGDMHG IRGADYQCYQ QAHARGLTSP YRAFLSSHLQ DLSSIVKKGD HFSLPVVNLK
GDVLFNSWMS MFSGNGAVFD PLTLIYSFDG RNVMTDQAWP QKLVWHGSST AGIRMTTNYC
EAWRTGDMAV TGQASLLQTG RLLGQHTHTC SNHFIVLCIE NSYIQSPGRN
//
