ID A0A9P0LEX0_ACAOB Unreviewed; 911 AA.
AC A0A9P0LEX0;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACAOBT_LOCUS21943 {ECO:0000313|EMBL:CAH1994160.1};
OS Acanthoscelides obtectus (Bean weevil) (Bruchus obtectus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Bruchinae; Bruchini; Acanthoscelides.
OX NCBI_TaxID=200917 {ECO:0000313|EMBL:CAH1994160.1, ECO:0000313|Proteomes:UP001152888};
RN [1] {ECO:0000313|EMBL:CAH1994160.1}
RP NUCLEOTIDE SEQUENCE.
RA Sayadi A.;
RL Submitted (MAR-2022) 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:CAH1994160.1}.
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DR EMBL; CAKOFQ010007191; CAH1994160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P0LEX0; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP001152888; 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 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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1083; MACROPHAGE RECEPTOR MARCO; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP001152888}.
FT DOMAIN 629..674
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 711..877
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..406
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..477
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 93614 MW; A38C2957EE5B2949 CRC64;
MSYLLKGALD QLKIFRDPNM AAQQCKTNFE EFHYLDEDIN NEIYVERTDY DRTYREGSGT
ADDLGVFPPP PPPPDGKDCL QCGKENCCNF IPSDLDKAAG RYRGEKGDRG PRGPPGESIR
GPPGPPGPPG SPGLPAAEGS CSCNITSILA ALPERSSSAY AVEGRAGSPG PPGLPGPAGE
RGPSGHKGDK GDRGERGPQG ASGVQGIKGE PGKDGVQGPP GPPGPPGPVE FENVDESVIG
GPLLRGGVPG PKGEVGKPGP AGPKGDRGAQ GPKGPAGEPG HKGDRGDRGL PGDKGSMGPK
ADRGDPGVDG IPGTPGKSGD KGEKGDLGPP GPPGISVGTT DISSVVPNLA GIKGEPGQKG
EKGDKGSDGE AGVPGVSGSA GASGPPGEKG DPGVDGAVGP VGPPGSKGDK GEKGPPGAVI
VAEGNAQIVT VKGEKGEMGK RGRRGKLGPM GPPGPPGKPG DIGLPGWMGR PGIPGIEGPK
GEKGDSGGPK GDKGDRGQDG TPGKDGAPGP PGPPGPAGPT GPQGIPGPPA SGDAVKYVPV
PGPPGPPGPP GHPGLSIQGP KGEPGIVAAY GEAVRYNLRP GHKSSLDELR ALRELEDLKE
YSGRATAAPP LATHSKEELP VKVVPGALTF HNKEVLGRMT ESSPLGTMAF IIEEDALVIR
VRRGWQYIAL GSLLTTYTPP PLTTMSPPLK LPFEASNLVN HAVRSADGSH LRLAALNEPS
TGNAHGVSGA DYACYREARR AGLRATFRAM LSSRTQNVDS LVRLQDRKLP VVNLHGELLY
HSWAEMFKGD GAPFPQQPAK IYSFSGKNVL NDPTWPLKAV WHGALPNGER ALDFSCDSWH
NSSRDKVGLA ASLRGTGLLE QTPFSCDKKL IMLCIEATSE GQKRKRRDIN LKDENQLLSE
EEYHKLLGSI R
//
