ID A0A3Q1IQ18_ANATE Unreviewed; 1350 AA.
AC A0A3Q1IQ18;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 27-NOV-2024, sequence version 2.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000019808.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000019808.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSATEP00000019808.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSATEP00000019808.2}
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 RefSeq; XP_026219152.1; XM_026363367.1.
DR AlphaFoldDB; A0A3Q1IQ18; -.
DR STRING; 64144.ENSATEP00000019808; -.
DR Ensembl; ENSATET00000020151.3; ENSATEP00000019808.2; ENSATEG00000013793.3.
DR GeneID; 113164195; -.
DR GeneTree; ENSGT00940000165423; -.
DR OMA; WEECATA; -.
DR Proteomes; UP000265040; Chromosome 2.
DR GO; GO:0005594; C:collagen type IX trimer; 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 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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
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:UP000265040};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1350
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043859532"
FT DOMAIN 30..219
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 227..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..309
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..344
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..421
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..661
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..801
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..932
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1350 AA; 137727 MW; 7AD20A088E12AF02 CRC64;
MPLCSRWTKT CIFILLVVTQ TGSQPRDESG TSLLQLIGDP PPNGITKDYG PRGEAVYVFT
SDTVTGQPAL SHVPNPFYRH FSLFFNIKPS TPAASVLFSI TDGAHKLMHI SVKLSAVQSG
RQTVQFFYTE PDAEASYEAA SFDVPSLVDT WSRFSLAVSE DEVMFYHGCD SEPQIVKFER
SPDPMELDPA AGIFVGQAGG ADPDKFQGEI AELKVVGNSR AAERLCDDED DIEAASGDFG
SGEGDRRQTG HTVIKQPVKT TAAPSRPVPE PPLISSQGTT LKESDVKYKQ QSADYSQSGS
TGPRGPSGPK GDKGDRGEKG SKGDEGPAGP KGDSGSRSDS GVSSQAGERG QKGEKGVKGS
SGFGYPGNKG ERGAQGPPGP PGPPGPAAEV VRLGDGSVVQ QVAGPPGPSG PPGLDGAAGR
PGADGEPGDP GEDGKSGPAG PQGSPGKPGT PGAKGQKGEL GEGQPGPRGP PGPPGPPGPG
TGSTFVDMEG SGFPDLDKYR GSRGLPGPPG PPGPPGIPGT SVALGPNGPV AFGPPGPPGQ
DGVPGLPGPP GPPGAPGPSG ARGEKGDCGE LGLPGPAGEK GSQGEPGQTG TSGQIGLAGL
PGPIGPVGPP GPPGPPGPPY RAGFSDQDGY EVINGLPGLT GPPGPQGPPG VAGLPGQPGL
PGNHGDKGAE GPRGPPGIPG IDGVPGQAGE KGERGEKGEM GRPGRDGGPP GPPGPPGPPG
EIISRSTGED GPGTPGRAGF PGPMGPKGDK GDSGPPGYAP KGQKGEPGII LGPDGTPMYL
GGLAGQPGDA GPPGPVGPPG PSGLKGEIGF PGRPGRPGLN GIKGEKGDSG SGSGYGYPGP
PGPPGPPGPP GPSVPVDRLG GYEDYSRYYP TLKGEKGDRG PPGIPGVGSN SDFYTFKNEL
KGETGSPGVK GDKGEPGGGY YDPRYGGVGA PGVPGPPGPK GDSIIGPSGP PGPIGPPGIG
YDGRPGPPGP PGPPGPSLSD IYRGTQTITI PGPPGPPGVP GLPGHAGVTV LRSYDTMTAT
ARRQPEGSLV YIIDQTDLYL RVRDGVRQVQ LGTFIALPSD DGNEVAAVEP RQDISYYPDH
HSNTDTHYPH VTQTNPQNPD PRNHPDSQYQ PDPRYPSSTD PRFPSYAERL NHPDGRYSVH
TVQEQPVYPD ARYAVTPQRR PPPPVQTPVH HHNSGPGLHL IALNSPQTGS MRGIRGADFL
CFTQAQAIGM KGTFRAFLSA RLQDLYSIVR KTDRDHLPIV NMKDETLFDN WEAIFSGSRM
KDNVPIYSFD GKDVLTDSAW PEKMVWHGST SAGQRHIDSY CETWRVGDRA LSGMASSLQS
GSLVQQSSSS CSSSYVVLCI ENSYMGQSKR
//
