ID A0A7N8YPZ8_9TELE Unreviewed; 899 AA.
AC A0A7N8YPZ8;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000066960.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000066960.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMAMP00000066960.1}
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}.
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; A0A7N8YPZ8; -.
DR Ensembl; ENSMAMT00000037453.1; ENSMAMP00000066960.1; ENSMAMG00000022394.2.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005594; C:collagen type IX trimer; 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; 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:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 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:UP000261640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 18..198
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 199..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..233
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..310
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..506
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..530
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 94748 MW; F7DD3441CD5E1986 CRC64;
MRLSKELVIL MLPSKESGLS LLELIGDPPP DEITKVYGPR GEAYVFTSAA VSGQPALAHI
PNPFYRHFSL LFHIKPSSPA ASVLFSITDG PQRLMYIGVK LSAVQSGRQK VQFFYTEPDS
EASYEAASFD VPSLVNTWSR FSLSVFEDQV IFYHGCDSEP QVVKFERSPD PMELDKAAGI
FVGQAGGADT DKFQVVGAKG EKGDNGVKGS KGDIGPAGPK GDSGSSSGAS PQSGGRGQKV
THLSGSSGFG YPGNKGERGP QGPPGPPGPP GPAAEVVRLG DGSVVQQVAG PPGPPGSPGL
DGAAGLPGTD GEPGDPGEDG KAVRVCCSRS QGPAGPRGSP GTQGTAGTPL LFDLLILTNS
HTWLECLFTS GTNCPNFGEK GEPGIILGPD GRSMYLGGLV GQPVKTILFY LCVSQGPPGP
PGPPGPPGPP IPVDRIGVSR NVKYSTVGEK GDRGPPGIPG VGSNFDFHTL KHELKGETGS
PGLKGEKGEP GGGFYDPRYG GIGAPGHPGP PGPKGDSIVG PPGPQGPPGH PGRGYDGQPG
PPGPPGPPGP SLPGVTVLRS YDSMTATARR QPEGTLVYII DQTDLYLRVR DGVRQVQLGS
YIALPSEDGN EVAAVEPPPV FPYYPDQTSH SSQSSPDSPV QPDPYQPTDP RYVANPDSRH
QPDPRYPSPT DPRFPSYADR INQPDGRFSV QERPTYPDPH YAVTPQRRPP PPVPQTPVHH
HTSGPGLHLI AVNSPQTGSM KGIRGADFLC FTQARAIGMK GTFRAFLSAK LQDLHSIVRK
ADRDSIPVVN LKDEVLFDSW DAIFRGGRMK DNVPIYSFEG KDVLRDSTWP EKMMWHGSTS
AGLQHVDSFC ETWRVDDRAL TGMASSLQSG SLLQQTSSSC SSSHAVLCVE NSYMGQSKR
//
