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Database: UniProt
Entry: A0A8T0BR95_SILME
LinkDB: A0A8T0BR95_SILME
Original site: A0A8T0BR95_SILME 
ID   A0A8T0BR95_SILME        Unreviewed;      1254 AA.
AC   A0A8T0BR95;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 13.
DE   RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN   ORFNames=HF521_017960 {ECO:0000313|EMBL:KAF7708903.1};
OS   Silurus meridionalis (Southern catfish) (Silurus soldatovi meridionalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Siluridae; Silurus.
OX   NCBI_TaxID=175797 {ECO:0000313|EMBL:KAF7708903.1, ECO:0000313|Proteomes:UP000606274};
RN   [1] {ECO:0000313|EMBL:KAF7708903.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SWU-2019-XX {ECO:0000313|EMBL:KAF7708903.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAF7708903.1};
RA   Zhang Y., Wang D., Peng Z.;
RT   "Chromosome-level assembly of Southern catfish (Silurus meridionalis)
RT   provides insights into visual adaptation to the nocturnal and benthic
RT   lifestyles.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KAF7708903.1}.
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DR   EMBL; JABFDY010000004; KAF7708903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8T0BR95; -.
DR   Proteomes; UP000606274; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 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; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000606274};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1254
FT                   /note="Thrombospondin-like N-terminal domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035790157"
FT   DOMAIN          36..224
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          221..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..352
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..496
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..575
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..616
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..651
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..795
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..819
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..901
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..933
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..980
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1254 AA;  128991 MW;  48E2E36B53E9C9BE CRC64;
     MAIRVSPWCW LYLSALGLLH PATGFQLQDE RSSSNQLDLT ELIGVPLPPS VSFITGFEGF
     PAYSFGPDAN VGRLTRSFIP DPFFHDFAII VTAKPTTRHG GVLFAITDAL QKIVHLGVAL
     APVEDGSQRV VLYYTEPGTA RTQEAASFKM GDLTGHWARF TLAVQGDEVK LYMDCEEHHR
     VAFHRSQKGL TFEPSSGIFV GNAGGTRLQR FVGSIQQLVL TPDPRAPDEQ CEEDDPYASG
     YGSGDNEYDD TETPDEVKKV HEEREYPPDE DQTLPVRAPP TEASSEGPFD DEDLEEGSSG
     QDVVPIDREP SRTEKAVYNK GDDYPLTMPV HKGEKGDRGP AGPPGPPGPP GTPSSSGPKG
     DISSWVGQPG ARGPPGPPGP TGAPGKDGLP GSRGEDGKSG ETGVPGFPGI PGDPGIKGEK
     GDAGIGLPGI PGPPGPPGRS GAPRYVDAID GSGFEDFDSD TEVIRGPPGP PGPPGQPGPP
     GPPQGLLPGP MGPPGAPGKD GLMGVPGIPG ISGKYGEPGN DGQKGDKGDT GLPGHAGQKG
     DTGQPGLPGS PGTAGPEGPK GEPGPAGPPG PPGPPSRFNF DLLDSEGSGV GGGSGFGQNI
     PRGPPGIPGL PGPPGPKGKD GVNGLPGTSE KGEPGPAGPE GKPGQSGLPG KNGEKGEKGE
     MGQKGERGLD GVSIPGPPGP PGPVINLQDL MLNDTEGLYN FTGIFDPQGP LGPRGPKGDR
     GIPGVPGHPG LKGEKGEPGL TIGPDGSLLS GPQGPKGLKG DHGVHGLPGA MGPVGPSGPK
     GEFGFPGRPG RPGLNGRKGE KGDSNGLQGP PGPPGPPGRP GIFNCPKGTV FPIPPRPHCK
     TSTNGNSTSE GASCSTSGAK GEKGERGLPG PPGTTITMLG AGSVGDKGDY GLRGEKGEKG
     EAGMPGAPGQ PGTSGVVGPK GDSIIGPPGR PGLQGPPGSP GIGRPGATGL RGPPGPPGYS
     SAAAIPGPPG PQGPPGPPGP AGGGFGSIKK YPTLYAMKSY VVEVGTLSMV TDTGKLYLKV
     QGGWKEILLG GLIEVNSPAV LSQDDAQPLI LTPQLSNTHK THTGSALRLV ALNTPLTGDL
     GSIHSVNKQC RLQAQAMGIR DDYKAFLSHH LQDLIDIVQL PYRTSLPIVN LRGEVLFKNW
     ESIFSHHALP AGIPLYSFDG RDVMSDPFWP QKAIWHGSSE RGRRLDDKNC ESWRAGDMAI
     TGQASFLYSG LLNQQTRSCS NQFIVLCIEI NPDHNTVEEL KRAQYRHRRW HHRY
//
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