ID A0A9Q1DQY7_CONCO Unreviewed; 1317 AA.
AC A0A9Q1DQY7;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 08-OCT-2025, entry version 11.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=COCON_G00058270 {ECO:0000313|EMBL:KAJ8278761.1};
OS Conger conger (Conger eel) (Muraena conger).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Congridae; Conger.
OX NCBI_TaxID=82655 {ECO:0000313|EMBL:KAJ8278761.1, ECO:0000313|Proteomes:UP001152803};
RN [1] {ECO:0000313|EMBL:KAJ8278761.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Concon-B {ECO:0000313|EMBL:KAJ8278761.1};
RX PubMed=36758078;
RA Parey E., Louis A., Montfort J., Bouchez O., Roques C., Iampietro C.,
RA Lluch J., Castinel A., Donnadieu C., Desvignes T., Floi Bucao C.,
RA Jouanno E., Wen M., Mejri S., Dirks R., Jansen H., Henkel C., Chen W.J.,
RA Zahm M., Cabau C., Klopp C., Thompson A.W., Robinson-Rechavi M.,
RA Braasch I., Lecointre G., Bobe J., Postlethwait J.H., Berthelot C.,
RA Roest Crollius H., Guiguen Y.;
RT "Genome structures resolve the early diversification of teleost fishes.";
RL Science 379:572-575(2023).
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:KAJ8278761.1}.
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DR EMBL; JAFJMO010000004; KAJ8278761.1; -; Genomic_DNA.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP001152803; Unassembled WGS sequence.
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; 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:SF372; COLLAGEN ALPHA-1(XVI) 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:UP001152803};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1317
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040119073"
FT DOMAIN 96..284
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..386
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..609
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..660
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..856
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1009
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 135396 MW; F254B1DD3B276D3E CRC64;
MAGALPLRVG LLLLLCGPAC VSAQWWGWFF RGQTTAAPVT TATAAVSTLA PTEAQAAAGT
PSRESVTPGV GSAGDNRAPK KRPLKMWRNE RGSTAHLDLT ELIGVPLPPS VSFITGYEGF
PAYSFGPDAN VGRLTKTFVP DPFFRDFAVA VTVKPAGARG GVLFAVTDAF QKLVYLGLAL
TPVEDQTQRI ILYYSERGSS RSQAVASFKV PDMSNRWSRF TLTVEGHEVR LYMDCEEYHR
VAFQRGAGRL RFEASSGIFV GNAGGTGLER FVGSIQQLIL MPDPRAAEVQ CEEDDPYASG
YGSGDDSLDD RETVDEVKKR VDEKELTSPW PEDFQGAPVR APPTQSPYED EEGSYSGDAR
PTEDPTSSQG IVLATETESG PTESSSQGKD QKGSVGTRAP PALLGPRGPP DPLCPPGWGV
LRQDSQALGG PRGLPGQGET QDCQGPMANL GSGAQTELQE NRGRKDSRDW REIRDSREKR
GTLEWGSAGP QDHPAPQDLP ALPDVPTVSM PMVPGSGFGP SMPSGSTVSP LAPPGIPGVP
GHDGKDGEPG KPGLPGPPGA DGAVGLAGEK GGKGDTGLTG PAGPKGEAGV VGIPGLVGPE
GPVGPVGHHG PPGPPGPPGA PGSGLALDLE DLEGSGRLGT ALGTPGPQGP QGPPGLPGVP
GPKGADGTPG VGSKGAPGDP GRVGTPGVPG IPGLRGEKGE MGFAGSKGER GALGLSVTGP
PGAPGPPGPI ISLQDLLLND TDGMFNFTDI QGLPGPMGPE GLPGRAGFPG PRGVKGDTGP
PGIQGPAGLK GEKGESGVTI AADGSLMTGL RGPQGPKGFK GERGFPGPVG LMGPIGPQGP
KGEFGFPGRP GRPGMLGKKG EKGDADSQPG PPGPPGPPGR PGPLNCPKGT VFPVPPRPHC
KTPVNADKDS TDGSDCRGRT GGKGEKGDPG VPGLPGSTDS WHFNGVVGDK GHPGYKGEKG
ERGEAGLTGP PGLPGRSGLV GPKGESVVGR QGLPGGPGQQ GPPGYGRTGP QGPPGPPGPP
GPPPLFGSAV AVPGPPGPPG PPGLGSPVTT YRSVETLFQH MHRSPEGTMA YVSEKSELYI
RVRDGWRKVQ LGELISLPAD SPSPAVLSRT GGLAYSDLIT QGQVYLPGYN ILAHSIHTGP
GLHLVALNAP YSGNMGGTRG ADNQCYQQAR AMGLLTTYRA FLSSHLQDLA TIVKKGDRFN
VPILNLKGEV LFHNWMSIFS GNGGVFQPGI PIYSFDGRNV MTDPSWPQRM VWHGSNADGI
RLTSNYCEEW RTGHMAVTGQ ASLLQSGRIL GQHTRSCSNQ FIVLCIENSY APDAYRT
//
