ID A0A287CSM2_ICTTR Unreviewed; 1247 AA.
AC A0A287CSM2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=Col18a1 {ECO:0000313|Ensembl:ENSSTOP00000024263.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000024263.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000024263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSSTOP00000024263.1}
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 EMBL; AGTP01106268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01106277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287CSM2; -.
DR Ensembl; ENSSTOT00000039163.1; ENSSTOP00000024263.1; ENSSTOG00000027467.2.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000005215; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 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; IPR001791; Laminin_G.
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; 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.
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:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 25..213
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 215..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..448
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..549
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..574
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..738
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..884
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 128938 MW; A1B5157CF93C8E05 CRC64;
MFECLPSRNR VWRHLLLFAD SVREEVGLPQ LLGEPPPQQI SQMEDPDVGL AYVFGPDTNS
GQVAQYRVPS PFFPDFSLLF HIRPTTESPG VLFALTDAAQ AVVLVGVKLS GVRDGHQDIS
LLYTQPGDSQ TRTAASFRLP AFVGQWTRFA LSVDGSSVAL YVDCEEFQRL PFARSPRGLE
LEPGAGLFVG QAGGADPDKF QGMIAELTVR GDPQVSPLRC LDQEDDDEDG WGRAAPEHLP
APGLLPGSQG RLPQPPPVTS PPLASGSGSE DSRSEEIRAG TTETLPGSDL DGTRDESARR
PGSSLERGGL KGQKGEPGVQ GLPGPVGPPG PAGPVVQGSN AQPVPGAQGP PGPPGPPGKD
GAPGRDGEPH PVFQGDTGPQ GFPGTPGDMG PKGEKGDPGI GPRGPPGPPG PPGPSLRHDK
LVSLPGEPGR FGMNSSHVPG PAGLPGVPGR DGSPGLPEGP PGKMGQKGSL SGFVGAPGPA
GPPGPPGPPG PPGPGLAAGF LTCWTLCSFQ GEVGADGARG FPGLPGREGT AGGPGNSPGG
ELAPGGLGGC PHPPRLSGDE PPHRAAPLSA AASSFLQGPK GDKGSPGERV SVGQRGARGP
AVDSAHTHDA PQAPWIQEPP PEPVGSGPGR GPVIQGWACG FFFQGDPGKD GVGQPGLPGP
GVLLVDTWAV SVSIPGPGCP GTPCPPGEKG EPGGVVGPDG RTLGPAQKGA KVRAAPPGPY
GRPGYKGEIG IPGRPGRPGV NGLKGEKGEP GDASLGLGMK GVPGPPGPPG PPGPPGVPIY
DSNVSLQGLP GPSGPKGDKG EVGPPGPPGQ FPVDLLSLEA EMKVCALWLG GQWPRCPPPG
SRTLRAAFPL QGEKGDLGDT GQKGEKGDSS VPGPPGPPGP PGYPGIPVRL GPSSPREPPE
STQPKPHPGW ALIPSPTPGA PEVASGQQEP MQAWVPQVRI WATYQTMLDR ARELPEGWLV
FVAEREELYV RVRNGFRKVL LDARIPLPPG TDNEVAVRQP PVVQLHEGNP YPWREHPYST
VRPWRADDTL ASPQRLPDPQ PYPGAPHHHG SYVHLRPARP TASPAHTHQD FQPVLHLVAL
NSPLSGGMRG IRGADFQCFQ QARAVGLAGT FRAFLSSRLQ DLYSIVRRAD RGTVPIVNLK
DEVLAPSWEA LFSGSGGQLK PGARIFSFDG RDVLRHPAWP QKSVWHGSDP SGRRLTESYC
EAWRTEATGA MGQASPLLAG RLLEQEATSC RHAHVVLCIE NSFMTSS
//
