ID A0A7J6DEF4_9TELE Unreviewed; 1265 AA.
AC A0A7J6DEF4;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=G5714_001757 {ECO:0000313|EMBL:KAF4117204.1};
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:KAF4117204.1, ECO:0000313|Proteomes:UP000579812};
RN [1] {ECO:0000313|EMBL:KAF4117204.1, ECO:0000313|Proteomes:UP000579812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWU-2019 {ECO:0000313|EMBL:KAF4117204.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF4117204.1};
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:KAF4117204.1}.
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DR EMBL; JAAMOB010000002; KAF4117204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J6DEF4; -.
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: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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 5.
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}.
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 229..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..520
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..652
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..686
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..813
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..975
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..985
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1265 AA; 129944 MW; BABC39080642ABE8 CRC64;
MLKLLRKMKL WLLSWLIGAH LALSYRSSAL LVMEERGSKG HLVLTELVGV PLPPSVSFIT
GYEGFPAYNF GPNANVGRLT QSFVPEPFFM DFSIIVTVKP SNSRGGVLFA ITDPSQRIVH
LGLALTPVED KTQRIVLYYS EPGLPDTMEV ASFKVPDMTQ QWNRFTLTVE HEEVRLYMDC
EEYHSAPLKR SQQPLSFKQG SGIFVANAGS TGLERFVGSI QQLVIKPDPR AAEEQCEEDD
PSLQASGDRS GDGDYDDEEE HGRHEVIFGQ TNVREDKEKT HRPTYPVQAP PTVSPDMDEG
EFSGHVTPID ERLLRGTYKT DETGESTGDG SGQGQKGERG EPGSAGPPGP PGPPGPSLPP
THSGQPGQRG PQGPMGPPGR QGRPGKDGQS GRKGEEGKPG QRGPPGLPGL PGESGVKGEK
GDSGVGLPGP PGPPGPAGPS KPIKVPYGFD ALGSGFEDVD IDTERLRGPP GPPGPPGKPG
PSGPNGPLGA LLPGPPGTPG KDGRDGQPGL RGLPGPDGLT GQQGPKGAKG EQGTRGPSGP
KGENGDSGLI GPMGPRGVPG PPGIPGPPGP PGPLSNNFMM DTLKDLESSG ESGLFLGAGI
SKGYLGPPGL PGPPGSQGLP GADGAPGLSV KGEPGSPGQD GIPGLAGLPG ARGPKGDKGS
PGEKGERGRD GLSITGPPGP PGPPGPTINL QDLLLNDTAA KLNLTKIRGP PGPMGPEGLP
GRAGFPGPRG PKGEIGFPGI QGPPGLKGEK GEPGVSIAAD GSVIPGLRGP RGPKGMKGDI
GLSGRPGIVG PIGPPGQKGE YGLPGRPGRA GIAGRKGDKG DSSGPPGPPG PPGPPGPPGR
VIGLNGVNNN NSQQGDGRAS LGVKGDKGDV GNPGLPGTAV PLFPHGYVGA KGDNGYKGQK
GEKGDPGLPG PPGMPGRTGL VGPKGDSIVG PPGDTGSPGA PGQPGYGIPG PQGPPGPPGP
PGTLSAYGSA ASLSGPPGPP GPPGAPGHGN PVRTYKNSQT LIRETSQAAE GTLAFVIDKS
ELYIRVRGGW KKVELGELIP VPQDSSSSAL TQGLSRPSDR SVPRVHSQEL KSFLPDYHAF
LQNAHSMPAL HLVALNAPFS GDMHGIRGAD YQCYQQARAR GLTSTYRAFL SSHLQDLSSI
VKKGDRFGLP VVNLKGDVLF SSWMAMFSGD GAVYDPLTPI YSFDGRNVMT EQAWPQKLVW
HGSNTMGIRM TTSYCEAWRT GDMAVTGQAS LLQTGRLLGQ HTRSCSNHFI VLCIENSYIQ
NPGRN
//
