ID A0A5E4BIS7_MARMO Unreviewed; 1516 AA.
AC A0A5E4BIS7;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=MONAX_5E019700 {ECO:0000313|EMBL:VTJ69468.1};
OS Marmota monax (Woodchuck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Marmota.
OX NCBI_TaxID=9995 {ECO:0000313|EMBL:VTJ69468.1, ECO:0000313|Proteomes:UP000335636};
RN [1] {ECO:0000313|EMBL:VTJ69468.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:VTJ69468.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABDUW010000463; VTJ69468.1; -; Genomic_DNA.
DR Proteomes; UP000335636; 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 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 3.
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:UP000335636};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1516
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5022695684"
FT DOMAIN 229..417
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 45..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..709
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..720
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..742
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..752
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..784
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..936
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1054
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1516 AA; 153392 MW; 188DD3F0D29D457F CRC64;
MAPHPSRRLG RLLLLLTCCL VPSWANLLTL DWLWSTDIAD SKDTLVSQPQ GSLPVQPAAA
PATRVAPQDD SAEQRTAPAS PRPPLENPKA APSRAPGAPI SATAPAAPAA SPDTREENVA
GVGAKILSIA QGIQSIVQLW NEATPTQSSA GSASAPTDPL ALTGPSGPPE ESGTTLGPHR
GALSSLGTWT AESGTLAVPT QSPPSLDRLQ APLRGHSVPR ESPDSVREEV GLPQLLGEPS
PQQITQIEDP DVGLAYVFGP DTNSGQVARY RVPSPFFPDF SLLFHIRPAS EGPGVLFALT
DAAQAVVLLG VKLSGVHDGH QDISLLYTEL GDSQTRTAAS FRLPAFVGQW TRFALSVDGS
SVALYVDCEE FQRLPFARSP RGLELEPGAG LFVGQAGGAD PDKFQGMIAE LTVRGDPQVS
PLRCLDQEDD DEDGASGDSG SGLEEEEQLP REGAVVALRP SLPQPPPVTS PPLASGSSTE
DSRSEEIRAG TTEAPPEVQT LPGSDLDGTS DESAQRPGSS LERGGLKGQK GEPGAQGLPG
PVGPPGPAGP VVQGSNAQSV PGAQGPPGPP GPPGKDGAPG RDGEPGDPGE DGKPGDTGPQ
GFPGTPGDMG PKGEKGDPGI GPRGPPGPQG PPGPPGPSLR HDKLTFIDME GSGFGGDLES
LRGPRGFPGP PGPPGVPGLP GEPGRFGMNS SHAPGPAGLP GVPGRDGSPG FPGPPGPPGA
PGKEGPPGKT GQKGSLGDTG APGPKGGKGD PGPVGAPGES GFVGAPGPAG PPGPPGPPGP
PGPGPAAGFD DMEGSGAPFR STARGSEGPQ GPPGPPGLKG DPGARGPPGA KGDVGADGAR
GSPGLPGREG PAGPPGPKGD KGSPGERGDP GKDGVGQPGL PGPPGPPGPV VYVSDQDRAV
TSAPGPEGRP GFAGFPGPAG PKGDPGSRGE QGFPGPKGEK GEPGGVLGPD GRTLGPAQKG
AKGEPGFRGP PGPYGRPGYK GEIGLPGRPG RPGVNGLKGE KGEPGDASLG LGMRGMPGPP
GPPGPPGPPG VPLYDSNAFV ESGHPGPRGL QGLPGPSGPK GDKGEVGPPG PPGQFPVDFL
SLEADMKGDK GDLGDTGQKG EKGEPGASGG FFSSSVPGPP GPPGPPGYPG IPGPKGESIQ
GQPGPPGPQG PPGIGYEGRQ GPPGPPGPPG PPSFPGPHRQ TVSVPGPPGP PGPPGPPGTM
GTSSGVRIWA TYQTMLDRAR ELPEGWLVFV AEREELYVRV RNGFRKVLLE ARIPLPSSTD
NEVAVRQPPV VQLHEGNSYP RREHSYSTVR PWRADDTLAS PQRLPDPQPY PGAPHHHGSY
VHLRPARPTA SPAHTHQDFQ PVLHLVALNS PLSGGMRGIR GADFQCFQQA RAVGLAGTFR
AFLSSRLQDL YSIVRRADRG TIPIVNLKDE VLAPSWEALF SGSGGQLKPG ARIFSFDGRD
VLRHPAWPQK SVWHGSDPSG RRLMESYCEA WRTEAAGAMG QASPLLAGRL LEQEATSCRD
AYVVLCIENS FMTSSS
//
