ID A0A452J0D2_9SAUR Unreviewed; 1658 AA.
AC A0A452J0D2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000033816.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000033816.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGAGP00000033816.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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}.
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DR Ensembl; ENSGAGT00000038305.1; ENSGAGP00000033816.1; ENSGAGG00000024061.1.
DR Proteomes; UP000291020; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; IPR010363; DUF959_COL18_N.
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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 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:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 340..528
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 250..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..841
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..885
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..899
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..919
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1305
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1658 AA; 170455 MW; 8064AA9062534C41 CRC64;
MASEWVWLRN KWQNASPECE TRVQCCWLPG RSCGRVWAKD KTPGVLRSQF PVGVLPCRGR
RAGNRRGWLV GSRAWQGLWL ATPPFSFVHA LRSCRGQTNV SAPGCCLLQD TFPGTVFFMA
PAEQRLCLLL LLICCCSLAE TRFLDWLWGT QKNPTVTTLP PTESQTTELL TSPVATTTQA
AVPATAQPGD QVWSTLSVTR QAPAVETAVP ALAKPAMPQG KEENIAGVGA EILDVAEGIR
SLVQLWDERT TQRTGNTGDP TAVAPLTNPP TSLAAPNSAM GLADHGNMTA NSTGNGHSLL
GTGQPEASLP TPAGPLPAWN RTQALLQKPA AALPEHFSTE VSLLQLIGDP PPEQITQVNG
PDNTHAYVFG PDANTGQVAR YHLPSPFYRD FSLLFHVQPT TNKAGVLFAI TDASQTVIYV
GVKLSAMQDR KQQIIFYYTE PGSESSYAAA TFSVPSLANE WTRFAISVED DEVILYLNCE
EFHRVRFERS PDEMELEDGS GLFVAQAGGA DPDKYQGMIA DLKVTGDHQA ADLQCEEQEE
DTDVASGDFG SGAEERPHLS GRKQGIPAVS RLPEPPPVTS PPTAGETVGK VSVGSQLPTD
QIKVEGLQQV STEARVGTKG EKGAPGEKGE HGPKGDSGSG RVLATGSTKG DKGEKGDLGV
KGSAGFGYPG SKGQKGEPGA QGSPGPAGLP GPPGSTLQRL DGSVVEQVAG PPGPTGPPGP
PGKDGLPGKD GEPGDPGEDG KPGDVGPQGF PGTPGEPGLK GQKGEPGVGA RGPPGLPGPP
GTPGLSSKQD KLGPRGPPGP PGPPGVPGLP GEPGRFGMNR TELPGPPGLP GLPGRDGVPG
AQGPPGPPGK SGLAGQPGLQ GERGDPGDLG LPGAPGPKGG KGEMGLAGAP GETGLAGLPG
PMGPRGPPGP PGPAGPPGPG YEAGFGDMEG SGMPVLSAVP GERGPKGPQG PPGLPGLKGD
AGSPGLPGLP GQKGDHGAPG VDGRPGLEGF PGPQGPKGDK GSQGAKGERG QDGVGSPGPP
GPPGQVIYAL GEEKALASLP GPEGKEGHAG FPGPMGPKGD LGDPGFPGTP GPKGEKGEPG
VIIGPDGTGI SAGTKGDKGE QGLVGPMGPA GPHGRPGQKG EIGFPGRPGR PSMNGLKGEK
GDPGGLGLQG PPGPPGPPGA PGNVASIYDN NAFSESGPPG PPGLPGYQGA PGQKGERGET
GAPGPPGQFP YGLNEFGSTF RGERGDRGDP GLKGEKGEPG EGGLYGPSVS GPPGPQGYPG
LPGPKGDSIR GLPGPPGPQG PPGIGYEGRQ GPPGPPGPPG PPSFPGPHRQ TVSIPGPPGP
PGPPGPPGTS GSLTSYGLRI LPAYQSMLST AQEVPEGWLI FVQDREELYI RVRSGFRRVR
LEEHTSISSP GLDNEVYDKP PSVHYSHGGT ASSGFLHPRR EHNPSSTAQP WRADDSIANH
HRLPDHLPHG AQPQQEPLDS FSPNRRGESI PSAVHRHHDF QPALHLVALN APLSGSMRGI
RGADFQCFQQ ARAVGLTGTF RAFLSSRLQD LYSIVRRADR SGMPIVNLRD EVLFNNWEAL
FSGAEAQFRA GVRILSFDGR DVLRDSAWPQ KNVWHGSDAK GHRLTESYCE TWRTDDSVVT
GQASSLASGK LLEQKVSSCR NAFIVLCIEN SFMTSSKK
//
