ID A0A8C5MBY2_9ANUR Unreviewed; 572 AA.
AC A0A8C5MBY2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE SubName: Full=Collagen type XV alpha 1 chain {ECO:0000313|Ensembl:ENSLLEP00000012333.1};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSLLEP00000012333.1};
OS Leptobrachium leishanense (Leishan spiny toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pelobatoidea; Megophryidae; Leptobrachium.
OX NCBI_TaxID=445787 {ECO:0000313|Ensembl:ENSLLEP00000012333.1, ECO:0000313|Proteomes:UP000694569};
RN [1] {ECO:0000313|Ensembl:ENSLLEP00000012333.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLLEP00000012333.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A8C5MBY2; -.
DR Ensembl; ENSLLET00000012820.1; ENSLLEP00000012333.1; ENSLLEG00000007830.1.
DR GeneTree; ENSGT00940000158302; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000694569; 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 GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
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 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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000694569}.
FT DOMAIN 323..366
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 402..567
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..115
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 59726 MW; 4479B33ACB2CB6D1 CRC64;
MITLNDLLLN DTEGLLNNTD FQLQPGPPGL DGRPGVPGFP GPRGHKGDNG NVGSGGVKGE
KGEPGAIIAE DGSLIAQLLG QKGEPGMMGP PGPMGPPGQP GMKGEFGFPG RPGRPGLNGV
KGPKGETGSS SLGPRGLPGP PGPPGQIVYI KGTVYPVPPR PHCKMPADAT NGVQNICGHK
GEKGSFGLPG TKGHKGDTGP PGPPGYPVPN QFLNHYLPSI KGERGEKGDS NNGLFIQGPP
GSPGRHGERG PKGDSVIGPR GQPGVPGLPG PPGYEIIGPP GPPGPPGPPG PPAIYGSAPA
PGPPGPPGQP GIPGSKNLAT ATRNIDDMLQ KTHLTLEGTL MYLSESSELY VRVRGGWRKV
QLGEFISLPA DSPPPPAISG HGYQPLPALS PGINMNYGTP NLHLVALNSP FTGDVRADLQ
CFQQARAVGL TSTYRAFVSS HLQDLHSVVR KADRFNLPIV NLKGQILFDN WESIFSGNGG
QFNAQIPIYT FDGINVMTDS TWPQKIIWHG SSLTGIRLVH NYCEAWRTSE MAVSGQASSL
RSGKLLDQKS YSCSNKFIVL CIENSYMTDT RK
//