ID A0A8T2PX25_9TELE Unreviewed; 1154 AA.
AC A0A8T2PX25;
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};
DE Flags: Fragment;
GN ORFNames=JZ751_000831 {ECO:0000313|EMBL:KAG9355987.1};
OS Albula glossodonta (roundjaw bonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Albuliformes; Albulidae; Albula.
OX NCBI_TaxID=121402 {ECO:0000313|EMBL:KAG9355987.1, ECO:0000313|Proteomes:UP000824540};
RN [1] {ECO:0000313|EMBL:KAG9355987.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HI-2016 {ECO:0000313|EMBL:KAG9355987.1};
RA Pickett B.D.;
RT "Applications of and Algorithms for Genome Assembly and Genomic Analyses
RT with an Emphasis on Marine Teleosts.";
RL Thesis (2021), BYU ScholarsArchive, Provo, UT, USA.
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:KAG9355987.1}.
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DR EMBL; JAFBMS010000001; KAG9355987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8T2PX25; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000824540; 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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; 6.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000824540};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 13..198
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 199..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..513
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..526
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..567
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..579
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..816
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..843
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..973
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KAG9355987.1"
SQ SEQUENCE 1154 AA; 116774 MW; 7D8915A283D55BF9 CRC64;
MLFLLSERGS KGHLDLTELI GVPLPPSISF ITGYEGFPAY SFGPDANIGR LTKTFVPDPF
FRDFAIIVTI KPSARGGVLF AITDAFQKVV YLGLTLTAVE DGTQKISLLY TEPDSAQEVA
SFKVPDMSGS WSRFTLTLQE DEVRLYMDCE EYHTVTIHRN SHQLSFEPGS GIFVGNAGAT
GLEKFEGSIQ QLVIKPDPRA AEEQCEEDDP YASGDASGDD MLDDRETADE VKKRVLEIVS
SRMEDALNGP VRAPPTDLPY GEEGEEYSGQ LSPTKEPSAA PVIMLTEETG PRHEEELRRT
SSGIGQKGER GEQGPPGPPG PRGPPGPSVD DGSLGRGQPG RMGPQGPTGP PGAPGSPGRD
GLPGRRGEDG QPGQRGPSGF PGLRGESGAK GEKGDRGVGV PGPPGPPGPP GPSSPAKFPG
GADAYGSGFG DFDSDAEVVQ GPPGPPGPPG KPGPPGPRGP PSGLIPGPPG PPGPPGRDGN
EGFIGMPGQP VFEEWFSGSG SESGFSSGFA SGEGAPGLDG GPGQKGAKGE KGDIGITGPV
GLKGDPGAPG VTGPPGPAGR LGERGLPGPQ GPPGPPGPPG KGFSLDAEDV EGSGRRAVLG
GPGPKGPVGP PGLPGPPGPK GQPGKDGPPG VGVKGERGDR GPVGEPGLAG LPGLRGVKGD
KGNLGQKGER GPDGLSVTGP PGPPGPPGES INLQDLFFND TEGLFNFTML RGPPGPMGPE
GLPGVAGFPG PRGPKGSIGL PGLKGHAGQK GEKGEPGVTI AADGSLMSSQ RGPPGPRGPK
GERGLPGPAG LMGPIGPHGP KGEYGFPGRP GRPGMMGRKG DKGESSGPPG RPGPPGPPGP
PGPVIGLNGV TAYRESAQES SGAQRGSMGL KGEKGDMGLP GQPGTSGSAI PKGFVGEKGN
EGYKGEKGER GETGAIGPPG PPGRSGLVGP KGESIVGPQG EPGLPGPPGP SGHGRPGPRG
PPGPPGPPGP PPLYGSTVAL PGPPGPPGLP GSPGTGNPVT TYLNVDTLLR ETYRVAEGTM
GYILDRGELY VRVREGWRKI QLGELVPIPS DSPSSSNSQV LGRVPERTRF RPPSQALQSL
LPGHSILPQT VNSDPGLRLV ALNAPFAGDM RGIRGADFLC YQQARAMGMV TTYRAFLSSH
LQDLATIVKK SDRF
//
