ID A0A7J6CNP6_9TELE Unreviewed; 1373 AA.
AC A0A7J6CNP6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=G5714_009874 {ECO:0000313|EMBL:KAF4108801.1};
OS Onychostoma macrolepis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Acrossocheilinae; Onychostoma.
OX NCBI_TaxID=369639 {ECO:0000313|EMBL:KAF4108801.1, ECO:0000313|Proteomes:UP000579812};
RN [1] {ECO:0000313|EMBL:KAF4108801.1, ECO:0000313|Proteomes:UP000579812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWU-2019 {ECO:0000313|EMBL:KAF4108801.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF4108801.1};
RA Wang D.;
RT "Chromosome-level genome assembly of a cyprinid fish Onychostoma macrolepis
RT by integration of Nanopore Sequencing, Bionano and Hi-C technology.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF4108801.1}.
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DR EMBL; JAAMOB010000009; KAF4108801.1; -; Genomic_DNA.
DR Proteomes; UP000579812; 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0032836; P:glomerular basement membrane development; 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; 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:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
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:UP000579812};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1373
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029779666"
FT DOMAIN 65..254
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 256..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..285
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..389
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 469..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..536
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..605
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..652
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..676
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..751
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..982
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1005
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 141300 MW; 2B6AECDC38F06B3E CRC64;
MMSKLRCWLC LFILVCLRIH HTHGWFWFDD SKENAKGAQT PAYLTSVRPT SPVRTEPPRT
TEESGVSLLQ LIGDPPPDGV SKVFDDANNP GYVFDQSSNV GQSAAAHLPN PFFRDFSLIF
NIKPTSSKPG VIFSITDPTQ NIMYVGVKLS AVEKGKQSII FYYTEPDSQS SYEAARFSVP
SMVNTWTRFS ISVLNERLSL YFKCDSDPQV IGFERSPDDM DLDAGAGVFV GHASGADPDK
FLGVIGDIRV LKDPGAAERH CEEDEDDFDA NLQGSGDYGA SGDGEGPPSV QPTPPSSRPI
QQPPVTSRLL VEKQQTGAKG EKGDRGDKGD RGLVGPKGDA GSGSVSGGGA KGVKGDAGEK
GIKGNSGFGY PGSKGDQGPP GPPGPPGPTG PSADVEVRGD GSVVQRVAGP RGPPGPPGSP
GPAGADGEPG DPGEDGKAGQ VGPPGFPGTP GSSGPKGEKG DRGESQPGPR GPPGLPGPPG
PPSRSDRPTF VDMEGSGFDL DDVRAMPGLP GLPGPPGPPG PPGPAGTGSS GSGGFGPPGP
PGQNGAPGQP GLPGPSGADG KSGLPGPKGE KGDAGELGLP GPVGEKGTKG SLGSPGLPGE
GGLAGLPGPM GPVGPPGPPG PRYQVGFDDM EGSGVHFSSV PGVRGPIGIQ GPPGAPGPQG
KPGFPGFPGE KGSEGPQGKD GQPGLDGFPG PQGPRGDKGD RGDRGEPGRD GTGLPGPPGA
PGSPGQIIYR YSENYDETGG SGPQGGAGFP GQAGFPGPMG PKGDRGDPGS PGYGTKGEKG
EPGLILGPDG NPLYHGGLTG QKGERGLSGP VGPPGPAGPS GLKGEFGMPG RPGRPGVNGY
KGEKGEPGSG SGYSYAGPPG PPGPPGPPGP AVPLDRFGRY EDYSRPATKG EKGDQGPPGV
PGSPVTPWLK FSSNFDIYAL KNEMKGERGE SGLKGEKGEP GGGFYDPRFG AVQGPPGNPG
LPGPKGDSIR GPPGPQGPPG PPGVGYDGRP GNTGPPGPPG PPGSPSLPGA YRPPLSVPGP
PGPPGPPGIP GTGSGQVTLL RSYDIMMATA RRQTEGALIY ILDRNDLYLR VRDGVKQVML
GDYKPFYGDL DNEVAAVQPP PVVHYSQDHT ANNGAEQISP PHPPIEFPRR EPENRNPNPP
DSRYPDPRYP PNTDNRYTDP VQPHRYPVQP ERNPITPARR PSPPVNQPEG HVHTSGPGLH
LIALNSPQVG NMRGIRGADF LCFQQARAVG LKGTFRAFLS SKLQDLYSIV RKSDRETLPI
VNLKDQVLFR SWESLFSDSE SRMKDNAPIY SFDGRDVLRD SAWPEKMIWH GSSGRGHRQT
DNYCETWRAG DRAVTGLASS LQAGQLLQQT SSSCSGSYIV LCIENSYMTQ SKK
//
