ID A0A8C6ZRE8_NOTPE Unreviewed; 1253 AA.
AC A0A8C6ZRE8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Nothoprocta perdicaria (Chilean tinamou) (Crypturus perdicarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Nothoprocta.
OX NCBI_TaxID=30464 {ECO:0000313|Ensembl:ENSNPEP00000016088.1, ECO:0000313|Proteomes:UP000694420};
RN [1] {ECO:0000313|Ensembl:ENSNPEP00000016088.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSNPEP00000016088.1}
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; ENSNPET00000016487.1; ENSNPEP00000016088.1; ENSNPEG00000011989.1.
DR Proteomes; UP000694420; 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 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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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:UP000694420};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 20..208
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 352..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..922
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 131480 MW; 64CAFFD26D1B3475 CRC64;
RRPLCVPQRR LLSPQNLSTE VSLLELIGDP PPEEIQKIYG PDNNPGYVFG PNANTGQVAR
YHLPSPFYRD FSLLFHIQPT TPRAGVLFAI TDSLQSIIYV GVKLSELRAG KQQIIFYYTE
PGSKSSYAAA TFTVPTLLNQ WTRFAISVEE DEVXLYLDCE EHERVRFERS PDEMELEDGS
GLFVAQAGGA DPDKYQGVIA DLKLKGDPRA AEHQCEEEED DAEEVSTRQL PAPFDVCFGG
KIFGIPGLVD AVPVTSPPVA VGSMPGIAAG SLPQAERTRV LDTLLISAAG NAAPSXQLCP
LALASPRRTL HWLVGKGGSC GAKLGCAGAV PPCRWMQDNA FPFLLQGSAG FGYPGSKGQK
GEPGEPGPPG SAPDGSGTER LNXPPGPTGP PGPPGKDGAP GRDGEPVSKA APVRRRLPSS
SSSSGDPGED GKPVSRAVTQ GSTPVLPGSP LQCCTFGLHF QTFIDMEGSG FGGDPDTLRG
PRGPPGPPGP PGVPGLPGEP GRFGMNRTDL PGPPGLPGRD GSPGPPGPAG PPGPPGTDGM
VGQPGPKGER GDVGDLGLPG APGPKGSKGE TGPAGAPGEM GLAGLPGPIG PRGQPGPPGP
PGPPGPGYEA GFGDMEGSGL PFAAGTPGPR GPEGPQVAPP FSKYLWQLPY ICFLFQGPKG
DRGSPGEKVS AGLVPAGDTS PSVDVGLWRL NACIFQGERG RDGVGLPGPP GLPGPPGQVI
YLSNEDVSDG SLLHGESLVR PIPVSFQGEK GEPGVIISPD GTIIAANVKG EKVSAHDVPF
PRLLGPNVPP KEGLPVITVC KEGGVFSLQG LPGPPGPPGP PGPPGNVIYD NSNVSSTIVA
SFLRCFHQFP GQKGEKGDVG APGPPGEQFY LCRLRREMCM GGISCIVGPP GPPGPQGPPG
VGYEGRQGPP GPPGPPGPPS FPGPHRQSEY FPQHSPAPCP QLRAVPTYQA MLSAAHELSE
GWLVFLADRQ ELYVRVRNGF RKVLLEEHTL ISSSALVSPL PHSSPRGPLH PLRNHSPPPT
ARPWRGDEIV ANQHRLPEQP ALHHGTQHQQ ELLNSYYINR RPDPAPVAAH VHQDFQPALH
LVALNAPLSG SMRGIRGADF QCFQQAREVG LLGTFRAFLS SRLQDLYSIV RRADRSTVPI
VNLRDEVLFS NWEALFAGSE APLRPGARIL SFDGRDVLRD SAWPQKSVWH GSDAKGRRLP
DSYCETWRTE ERAAMGQASS LSAGKLLEQA ASSCQHAFVV LCIENSFMTA SKK
//
