ID A0A8T0E3X7_ARGBR Unreviewed; 1240 AA.
AC A0A8T0E3X7;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=Collagen alpha-1(XV) chain like protein {ECO:0000313|EMBL:KAF8764917.1};
GN ORFNames=HNY73_022947 {ECO:0000313|EMBL:KAF8764917.1};
OS Argiope bruennichi (Wasp spider) (Aranea bruennichi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Araneoidea; Araneidae; Argiope.
OX NCBI_TaxID=94029 {ECO:0000313|EMBL:KAF8764917.1, ECO:0000313|Proteomes:UP000807504};
RN [1] {ECO:0000313|EMBL:KAF8764917.1}
RP NUCLEOTIDE SEQUENCE.
RA Sheffer M.M., Hoppe A., Krehenwinkel H., Uhl G., Kuss A.W., Jensen L.,
RA Jensen C., Gillespie R.G., Hoff K.J., Prost S.;
RT "Chromosome-level reference genome of the European wasp spider Argiope
RT bruennichi: a resource for studies on range expansion and evolutionary
RT adaptation.";
RL bioRxiv 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:KAF8764917.1}
RP NUCLEOTIDE SEQUENCE.
RA Sheffer M.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
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:KAF8764917.1}.
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DR EMBL; JABXBU010002231; KAF8764917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8T0E3X7; -.
DR Proteomes; UP000807504; 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 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; 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; 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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KAF8764917.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000807504};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1240
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035813209"
FT DOMAIN 43..233
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 289..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..355
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..436
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..929
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 129321 MW; 5B8B2EB36014342C CRC64;
MRIFHQCLIL TLTFGIVTIS AKRWRNKPGR PKNPKHPRGH PRVQDLLQAI KIPFVTPGVG
FVIGPDGFPA FLLEQEADIK SPYRLHLPPT LFRDFTIGVT LMPKNPKGGY VFAVVNPTDT
VVQLGLKIIS SGESTVNLTL FYTDVDMHLT SQALTTFSVP DFLGMWTRIA IRIAMNNVTL
FYNCEEYASV EVRRIPKKLV FDTASTLYIG QAGPLLSGKF EGGLQELKIY NKPGVAEIYC
EASFQGSGDG RGDVGIEEID VNDDNEQMYP VTTPGKSEQG PPPLIIPPPP GPGPIGIEKV
PGPKGEKGRA GRHGKPGLKG EPGLITEKEL LKLQPKLKGD RGEPGPPGLP GPPGPQGQKG
ECVVAPPRFG ITGGPSELWN EGDYGSGDDQ GAREWLSGVL HPGSPCVCNI SLKHLESLPR
LRGADGLPGP KGDPGAPGLP GPPGIGMPGS DGPKGDEGKP GLPGPQGQKG EPGVDGIPGS
PGPRGMPGPP GPPGLANNHA PFDLDGAYGS GLYPSSGDGP FGPYVGRPGA PGVQGPPGLP
GPPGIRGERG YPGEKGERGE QGPKGDKGNQ GISGFPGEKG DPGLNGRDGI AGLPGLKGER
GEKGDPGPPG IGIPGPPGPP GKPGSAIFRS SDGDGGIDIS LKGEKGEPGE SGPKGSRGKL
GKEGPPGPKG DLGPPGPPGP PGVSTITSTD GEAELLIKGE KGDRGRRGKK GKIGPPGPPG
PAGPPGEIGL PGFPGRPGTP GRPGPKGEPG VSIKGEKGDQ GPPGIGGYMD ADGISVVSIG
PKGEKGDLGP AGPIGPSGLP GEKGEPGRPG RDGRKGEQGP PGPAGSLDDL RTGGKLIPIA
GPPGPPGPPG PRGPPGEAIP GPPGLPGPPG APGGSGLRNP FWTGNDHAGR RAYRGIKGLR
AFSRAKGVQI FPGPPGPPGP PGPPGPPGKP ASDNAPEELR RPTVVPGAVT FKNMDTLLRM
SDISPLGTLA FVLEEESLLV RVSEGWQYVA LGSLVVQSTP SPTKAPTTHA PFSPPVDNLR
LDKAPRLRMA ALNQPFSGDM HGVRGADYEC YRQSRRANLR GTFRAFLASR VQNLDSIVRF
QDAGLPVVNL KGEVIFNAWK DVFTGAGAPF PYPPRIYSFD GRNVLADNRW PQKLVWHGSD
KHGVRDLESY CDAWHSAGLG KVGMASSLLR GRLLDQERYS CNNSFIVLCI EATSQDDYRK
RRKRDIDEDE ADIDDHELTW EEFLQRQKEE ESEEEEIRTI
//
