ID A0A8C3SWN7_CHESE Unreviewed; 1590 AA.
AC A0A8C3SWN7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Chelydra serpentina (Snapping turtle) (Testudo serpentina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelydroidea; Chelydridae; Chelydra.
OX NCBI_TaxID=8475 {ECO:0000313|Ensembl:ENSCSRP00000019418.1, ECO:0000313|Proteomes:UP000694403};
RN [1] {ECO:0000313|Ensembl:ENSCSRP00000019418.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCSRP00000019418.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR Ensembl; ENSCSRT00000020299.1; ENSCSRP00000019418.1; ENSCSRG00000014583.1.
DR Proteomes; UP000694403; Unplaced.
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 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 InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR010363; DUF959_COL18_N.
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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 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 Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000694403};
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..1590
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034095307"
FT DOMAIN 209..397
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 130..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..731
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..913
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 161410 MW; 72AE8ADA1A55A005 CRC64;
MAPAEQRLCL LLLLTCCCSL AEARLFDWLW GSEKAPKVMP LPPTENLATE EQTVEPLTSP
VAITATAQPG DQVWSTRSVM TQAPAVDTAG PALAPPSGPQ GKEENIAGVG AEILDVAEGI
RSLVQLWDET STQRTGDTGE PTAAAPLTTT RSSLAAPSSA VGPAGRGNVT ANSTEASLPR
PAGPPPAWNR TRALLQTPAA APPEHFRGEV SLLQLIGDPP PEQITKVTGP DNTLAYVFGL
DANTGQVARY HLPSPFYRDF SLLFHVQPTT NKAGVLFAIT DASQTVIYVG VKLSAVQNTK
QQIIFYYTEP GSESSYAAAT FSVPSLANEW TRFAISVEDD EVVLYLNCEE FRRVRFERSP
DEMELEDGSG LFVAQAGGAD PDKYQGVIAD LKVTSDLQAA DLQCEEQDED TDVASGDFGS
GVEERPHLSG REQGTPAVSR LPEPPPVTSP PTAGETVEKV RVGSQLQTEQ IHGEGPQQVS
TGARVGPKGE KGAPGERGER GSKGDSGTGG ALAAGSTKGD KGEKGELGVK GSAGFGYPGS
KGQKGEPGDQ GSPGPAGPPG PSGSTVQRLD GSVVEQVAGP PGPTGPPGLP GEDGLPGKDG
EPGDPGEDGK PGDVGPQGFP GTPGEPGLKG QKGEPGAGAR GPPGLPGPPG TPGLSSKQDK
LTFIDMEGSG FGGDLESFRG PRGPPGPPGP PGVPGLPGEP GRFGMNSTEL PGPPGLPGLP
GRDGIPGAQG LPGPPGPPGK HGSAGQPGLR GERGDPGDLG LPGGPGHKGD KGEMGLAGAP
GETGLAGLPG PMGPRGPPGP AGPPGPGYEA GFGDMEGSGM PFLSAVPGER GPEGPQGPPG
LPGLKGDTGS PGLPGLPGQK GDHGAPGVDG RPGLEGFPGP QGPKGDKGGQ GAKGERGHDG
VGSPGPPGLP GPPGQVIYAS GEERALAGLP GLEGRQGHAG FPGPVGPKGD SGDPGFPGTP
GPKGEKGEPG AIIGPDGTGI SAGTKGDKGE QGLVGPMGPA GPHGRPGLKG EIGFPGRPGR
PSMNGLKGEK GDSGGLGLQG PPGPPGPPGA PGSVPVSVYD NNVFSESGPP GPPGLPGFQG
APGQKGERGD TGTPGPPGQF PYDLSEFGST FRGEKGDQGD PGLKGEKGEP GGGGLYGPSV
SGPPGPQGYP GLPGPKGDSI RGVPGPPGPQ GPPGIGYEGR QGPPGPPGPP GPPSFPGPHR
QTVSIPGPPG PPGPPGPPGT SGSLTSSGLR ILPAYQSMLS AAQEVPEGWL IFVQDREELY
VRVRSGFRRV RLEEHTAVSS PGLDNEVYDK PPSVHYSHGG TASSGFLHPR REHNPSSTAR
PWRADDSVAN HHRLPDHSPH SAQPQQEPLD SYSPNRRGES APSAVHTHHD FQPAVSTAQP
QPPCPAAAPA RREPSCVRGR RSSGLSQPAA AQYRQCMERG SWAQTIRDWG WGPAPQGMQS
PAVRLRAGAK AKGHAQLYHA PNPHPHPFVQ HCAQPAPRPR EEAASQRVGW QESMGRGRDA
AALGWFWGCC WYWLGTPGIS VLVPGTIPCV RPWEHPAEML LVALEEVTSA GGSYVGAFPG
AGAVAGSPSA TVSSWRWEDT TGSWGQRLWG
//
