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Database: UniProt
Entry: A0A672JW81_SINGR
LinkDB: A0A672JW81_SINGR
Original site: A0A672JW81_SINGR 
ID   A0A672JW81_SINGR        Unreviewed;       899 AA.
AC   A0A672JW81;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS   Sinocyclocheilus grahami (Dianchi golden-line fish) (Barbus grahami).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Sinocyclocheilus.
OX   NCBI_TaxID=75366 {ECO:0000313|Ensembl:ENSSGRP00000000411.1, ECO:0000313|Proteomes:UP000472262};
RN   [1] {ECO:0000313|Ensembl:ENSSGRP00000000411.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSGRP00000000411.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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DR   AlphaFoldDB; A0A672JW81; -.
DR   Ensembl; ENSSGRT00000000467.1; ENSSGRP00000000411.1; ENSSGRG00000000274.1.
DR   InParanoid; A0A672JW81; -.
DR   OMA; GTKQTNI; -.
DR   Proteomes; UP000472262; 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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; 1.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472262};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..240
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          238..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..365
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..422
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..600
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  96700 MW;  B497DD0C7F1D4D01 CRC64;
     MLYLVKSRSP GIGLGLCFWT IILISCIPAS GCVRTRLLTL FSVCAERDSS AQLDLTELIG
     VPLPPSVSFV TGLEGFPAYR FGPDANVGRL TRSFIPDPFY HDFSIVVTAR PSSRHGGVLF
     AVTDALQKII HLGVSLAPVE DGSQRVVMYY TEPGAAHTQE AASFKMGDLT GRWARFTLAV
     QGEEVKLYMD CEEQHRVAFR RSPDPLTFQP SSGIFIGSAG GTRLERFLGS IQQLLLTPDP
     SAPNEQCEED DPYASGYGSG DDIYEDTETP DEVKKVVEER EYVMVRDTIS PLILSRAQSL
     HDKLSSDLFM QIFLCFSVTA EPIRSEGASQ DRNVITMQKG EKGERGPPGP PGPAAPHTPG
     EPGPRGPQGE PGRDGRPVST ASSTIAVKSS LLQNLVLRLI FIVLDSHQGP PGPPGPPGPP
     GPSVGAHPGP IGLPGVPGRD GEKGKRGVPG EPGAKGDDGQ AGAPGLPGRQ GEGGEKGDMG
     QKGERGIDGI CLPGSPGPPG PPGPIINLHE LMLNDTEGIF NLSGIFEPQG PLVRSLSLPC
     LLFVHGLISM FWCFSETVQM DSFQCNAVKC LIMLFCEQGA KGESIIGPPG HPGPRGPPGA
     PGFGRTGVAG RPGPPGPPGQ HGSGVMIPGP PGPPGRPGRA TEASSTVGKY VSLQAMRQQS
     SVLEDGTLSF LIDTSKLYMK VPGGWREVQV TPQMRSAEPL ILSPQLRHTP RTHTGSALRL
     VALNTPLTGN LGSIHSVNKL CRTQAQAMGI RDDYKAFLSH HLQDLIDTVQ PMYRTNTPIV
     NLRGELLFKS WHSIFSSHLL PPRVPLYSFD GRDVMSDPFW PQKAVWHGSS ERGKRLSALN
     CESWRAGDMA ITGQASFLYS GLLNQQTRSC SNRFIVLCIE TSHDHQTLQE RHRRWHHRS
//
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