ID A0AA88T7Q5_CHASR Unreviewed; 1928 AA.
AC A0AA88T7Q5;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 08-OCT-2025, entry version 9.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=Q5P01_005832 {ECO:0000313|EMBL:KAK2857097.1};
OS Channa striata (Snakehead murrel) (Ophicephalus striatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Channoidei; Channidae; Channa.
OX NCBI_TaxID=64152 {ECO:0000313|EMBL:KAK2857097.1, ECO:0000313|Proteomes:UP001187415};
RN [1] {ECO:0000313|EMBL:KAK2857097.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Gz {ECO:0000313|EMBL:KAK2857097.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK2857097.1};
RA Liu H.;
RT "Chromosome-level Genome Assembly of Striped Snakehead (Channa striata).";
RL Submitted (JUL-2023) 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:KAK2857097.1}.
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DR EMBL; JAUPFM010000003; KAK2857097.1; -; Genomic_DNA.
DR Proteomes; UP001187415; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 3.
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:UP001187415};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1928
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041681785"
FT DOMAIN 600..789
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 26..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1626..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..81
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..490
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..892
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..934
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..972
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1002
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1027
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1149
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1493
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1541
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1928 AA; 196991 MW; B37FAB9125B7F3FA CRC64;
MLRMQPRLLL MVLCVGSLEA WNWQSETKPT NESLTNTTAG ETTPTKILTT KATTGETVTE
TRPTAKTATE GTSAGTATKA TPEGATSTPA EDLQTGKTSK DATTTEATLA ETTLPEGLQT
DATATVAMTT EASTLNATTM NATPAEAKLA GNLQTETTPE DATTTEAAVV EATLAEDFQT
DATPENAMPT EASTSNATKA VSTVSTPTDA KNKIATTAEM ALAEVMQTET TPKYATTTEA
TLLETTLAED VQTDATPENA TPTEASTSNA TKAVSTVSTP TDAKNKIATT AEMALAEVMQ
TETTPKYATT TEATLLETTL AEDVQTDATP ENATPTEAST SNATKAVSTV STPTDAKNKI
ATTAEMALAE VMKTETTPED ATLAEASTSS ATTANATPAK ITPAEDLQTV STPTDATNAS
ATTAEMTPAE DVPPDETPIM ATPEDATATN AIKANATTAE MMLAEDLQTE GTQTEHTPTN
ATTTNPTKAN TTPAEWTLAE VMQTETTPED ATLAATRLVE AKPTDVTPTR TLLIETSPTE
AAPTETMPET ESTTAIISTV PTNVTAMPRA TEREEVKEGD NLSSLGEELT TVTSGIQVSG
VSLAQLMGDP PPDEITMTYG QRGKPVYVFS SAAVSSKPAL AHVPSPFYRH FSLLFNIKPS
SPDASVLFSI IDGAQKLMHI GVKLSKVQSG RQKVQFFYTE PDSEASYEAA SFDVPSLVDT
WSRFSLAIDE EQVTFYQGCD SEPQVVKFER SPDPMEFDKA AGIFVGQAGR ADTDKFQGEF
AELKVVGNPR AAERLCDDED DSDAASGDFG SGDGDSRMVK HTVKMTAPPS LPVPEPPLGS
SQGARLKESG PSGPSGAKGD KGDKGDKGLK GDKGPAGPKG DSVSLSGSGV SSQAAERGEK
GEKGERGSSG VVYPGKKGER GAEGPPGPPG PPGPAAEVIR LGDGSVVQQV AGPPGPRGPP
GTDGATGPPG ADGEPGDPGE DGKAGPAGPR GAPGSPGTPG AKGQKGELGE GQPGPRGPPG
PPGPPGPGTG QTFVDMEGSG FPDLDKIQGP PGRPGPPGPP GPPGVPGTSV ALGANGPIAI
GPPGPPGQDG APGLPGPAGP PGAPGRPGPS GEKGDCGELG LPGPAGEKGA QGNPGQTGTQ
GQTGLAGLPG PMGPVGPPGP PGPPGPPYRI GFSEQDGYEV INGLPGPPGP QGPPGIAGLP
GKPGLPGNHG DKGAEGPRGA PGLPGVDGFT GRPGEKGAQG EKGEMGLPGR DGGPPGPPGP
PGPPGEILYR ATGEYNDLNW NEGLQGGSGP PGRAGLPGPM GLKGDKGDPG HPGYAPKGEK
GEPGVILGHD GTPLFLSGLA GQPGERGLPG PVGPPGPYGP PGHKGEIGFP GRPGRPGLNG
IKGEKGDSGG GSGYGYPGPP GPPGPPGPPG PPAPLERVGA YQDYSRQYSG LKGEKGDRGL
PGIPGVGTDF DLYTFKNDLK GEPGTSGLKG EKGEPGGGYY DPRYGGSGVG APGLPGPPGP
KGDSIIGPSG PQGPAGPPGP PGRGYDGRPG LPGPPGPPGP SLPGIYRGSQ TISIPGPPGP
PGVPGPPGPS GVVVLRSYDT MTATARRQPE GSLVYIIDQT DLYLRVRNGV RQVQLGAFIA
LPNDNGNEVA AVEPPPVVPY YPDPQSSSGT LTHNSQSSAD SSVQHQDPYR STQTGPGIRD
PRYYPDSQYQ PDPRYPTHAD PRFPSFIDRL NQPDSGYSVQ ERPVYPDPRY AVTPQRRPPP
PAPQIPVHHH TSGPGLHLIA LTSPQTGSMR GIRGADFLCF TQAQAVGMKG TFRAFLSAKL
QDLNSIVRKA DRDHLPIINL KDEVLFDSWE AIFNGDRMKD NVPLYSFDGK NILSDSSWPE
KMVWHGSTSV GQRHVDSFCE TWRVGDRAVS GMASSLQSGS LLQQNSSSCS SSYVVLCIEN
SYIGQSKR
//
