ID A0A3P8PYZ7_ASTCA Unreviewed; 1363 AA.
AC A0A3P8PYZ7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000022266.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000022266.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000022266.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSACLT00000022783.1; ENSACLP00000022266.1; ENSACLG00000015120.1.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000265100; Chromosome 23.
DR Bgee; ENSACLG00000015120; Expressed in anal fin and 5 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01391; Collagen; 3.
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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1363
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017935830"
FT DOMAIN 29..218
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 224..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..870
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..983
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1363 AA; 140172 MW; BA1EB75E7CF70443 CRC64;
MRARDRCWTC ILALLVAAQA QSQQTEVSGI SLLQLIGEPP LEEFTTTYGP NGEPAYRFTP
SVVPGQRALV HVPSPFYRHF SLLFHVKPST PAASILFSIT DATQKLMYVA VKLSAVKAGR
QKVQFFYTEP DSEASYEAAS FEVPSMVDTW SRFSLSVMEE QVAFYHGCDS EPQVVKFERS
PDPMDLDPAS VLFVGHAGRA DNGKFLGDMA DLRLVGNPRS AERLCDYEDD SDTGSGDYGS
GDGERRQMGG SMKTTPPPFR PLPEPPLISS HINTLAQTDV WYQPSVEYSR QDFSKPGLLG
SRGTIGAKGE KGDRGEKGSK GDQGPVGAKG DSGVSSGSGF SAQGGVQGQK GEKGEKGDLG
KGYTGKKGDR GAQGPPGPPG PTGPAAEVVR LGDGSIVQQL AGPPGPPGLP GSDGPAGPPG
ADGEPGDPGE DGRAGPPGLQ GVPGIPGGPG AKGEKGERGE GQPGPRGPPG PPGPPGPGTG
DRPTFVDMEG SGFPDLDKIR GPHGPPGLPG PPGPPGIPGT SVAVGLDGPI AVGPPGPPGQ
DGAPGLPGPP GPPGLPGPPG PAGGKGDSGD LGLPGPAGEK GSQGEPGQVG TSGQTGLAGL
PGPMGPVGPP GPPGPPGPPY RIGYGDQDGY EVLSGLPGLR GEPGPQGPPG IAGHPGNPGL
PGTPGSKGAE GPRGPPGIPG LNGSTGEKGP KGDSGEKGER GLPGRDGGPP GPPGPPGPPG
QIIYQPGGDY NDLYWNEAGQ VGPGIPGRAG FPGPMGPKGE KGNPGPPGYA PKGEKGEPSV
ITGPDGRPLF LGGLTGQPGE RGSPGPMGFP GPQGPQGQKG EIGFPGRSGR PGLNGAKGEK
GDAGSGSGYG YPGPPGPPGP PGPPGPPVPI DRLGGYDYSR YYAVKGEKGD RGPPGFGSNI
DIYSLKNELK GESGVKGEKG EPGGGYYDPR YGGSGVGAPG VPGPPGPKGD SIIGPPGPQG
PPGPPGRGYD GPPGPPGPPG PPGASLDGSY RGTQTISIPG PPGPPGPPGV PGVTSGVTVL
RSYETMTATA RRQPEGSLVY ILDQTDLYLR VRDGVRQVQL GEYIAFPRED GNEVAAVEPP
PVVPYFQDHH SHTGTSTNHF NQPHESPAQP HAEPDYKPTY VDPRYQPDSR YQSEPRYPEL
TDPRFPSYTD RLNSPDNRYY VVDTRYPITT PRRPPPRQPQ SPVHYHTSGP VLHLIALNSP
QTGSMRGIRG ADFLCFTQAQ GIGMKGTFRA FLSSRLQDLH SIVRKTDRHN LSVVNLKDEV
LFDSWDDIFS GGRMKENVSI YSFDGKDVLH DNTWPEKMVW HGSTSRGERH VDSFCETWRV
GEHALTGMAS PLQSGSLLQQ SSSSCSSSNV VLCIENSAGH SRR
//
