ID A0AAY5E9X7_ELEEL Unreviewed; 779 AA.
AC A0AAY5E9X7;
DT 05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 1.
DT 28-JAN-2026, entry version 5.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=MMP15 {ECO:0000313|Ensembl:ENSEEEP00000053334.1};
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000053334.1, ECO:0000313|Proteomes:UP000314983};
RN [1] {ECO:0000313|Ensembl:ENSEEEP00000053334.1, ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Myers G., Meyer A., Fedrigo O., Formenti G., Rhie A., Tracey A., Sims Y.,
RA Jarvis E.D.;
RT "Electrophorus electricus (electric eel) genome, fEleEle1, primary
RT haplotype.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSEEEP00000053334.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSEEEP00000053334.1}
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; A0AAY5E9X7; -.
DR Ensembl; ENSEEET00000060585.1; ENSEEEP00000053334.1; ENSEEEG00000028279.1.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000314983; Chromosome 1.
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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; 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; 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:UP000314983};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 24..205
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 245..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..577
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 84242 MW; 430BEFD31EEE01F9 CRC64;
MASIIKTQYN NPNLPKWEPK QESGVSLLQL IGSLPPNQVT RVEGPDGRVA YLFEGRASAG
LPARAHLPSP FYRDFSLVFH LRPISDEAGV IFAITDSDQK LMHVGVKLSA VEGTTRRVVF
YYSHPGSNKS VEVASFEVPH QPGEWSHYSL AVNQDQVTFY GDCSTEPRVA TFERSPDDLQ
LDMGAGIFVG QGGAADPDKF KVCSTPLNEL LTPPCPLYNP YMCVLSVFLL GLVYNTMPAV
LQGSPGSGYP GSKGDPGPPG PPGPPGPPGP VAEVIHPGEG KVIERLVGPL GPAGPDGPPG
APGPSGPKGD RMPTKLTNKS YIYIHTLLTN VNMLSKNEWK GEQGSKGQKG EPGGGQYSPH
YGPGEGRLGS PGPPGPRGES VAGPPGPPGH PGPPGIGYPG RPGTPGPAGP PGPPGPAGPG
AHRPSQCEKH RNTLSFDTMA TATRHHPEGT LVYVIDNTDF YVRVRDGVRK VMLGEYTPFP
SPVDSHIAVV EPPPDVLYSP DSSVILPDPD RHPPYDLRYS TDLRHPLPTD PRHSDPQYSG
PRYSDSRYLD PRYPAPAGSA EPEPRHQPHQ PHGRHAYHSG SRYYVTPVHR PIAPEARAPT
HTHSSGPALH LIALNSPKKG DMQGIRGVDH QCFLQAQAAG FKSTFRAFLS SQLQDLHSIV
HRNDRHHIPV VNLKDEEVFS NWESIFNASD GRMRENTRIY SFDGRDVLED DAWPEKLVWH
GSCVAGLRQT DSYCEAWRTN NHAVTGMASS LRNGRLLQQT ARSCSSSYVV LCVENSYIA
//
