ID A0A9P0LET2_ACAOB Unreviewed; 899 AA.
AC A0A9P0LET2;
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:CAH1994161.1};
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:CAH1994161.1, ECO:0000313|Proteomes:UP001152888};
RN [1] {ECO:0000313|EMBL:CAH1994161.1}
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:CAH1994161.1}.
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DR EMBL; CAKOFQ010007191; CAH1994161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P0LET2; -.
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 617..662
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 699..865
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..573
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 289..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..396
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..416
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..487
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 92229 MW; 4BF6D92B15858492 CRC64;
MSYLLKGALD QLKIFRDPNM AAQQCKTNFE EFHYLDEDIN NEIYVERTDY DRTYREGSGT
ADDLGVFPPP PPPPDGKDCL QCGKENCCNF IPSDLDKAAG RYRGEKGDRG PRGPPGESIR
GPPGPPGPPG SPGLPAAEGS CSCNITSILA ALPERSSSAY AVEGRAGSPG PPGLPGPAGE
RGPSGHKGDK GDRGERGPQG ASGVQGIKGE PGKDGVQGPP GPPGPPGPVE FENVDPSWKT
RGPFKESVIG 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 GRATAAPPLA
THSKEELPVK VVPGALTFHN KEVLGRMTES SPLGTMAFII EEDALVIRVR RGWQYIALGS
LLTTYTPPPL TTMSPPLKLP FEASNLVNHA VRSADGSHLR LAALNEPSTG NAHGVSGADY
ACYREARRAG LRATFRAMLS SRTQNVDSLV RLQDRKLPVV NLHGELLYHS WAEMFKGDGA
PFPQQPAKIY SFSGKNVLND PTWPLKAVWH GALPNGERAL DFSCDSWHNS SRDKVGLAAS
LRGTGLLEQT PFSCDKKLIM LCIEATSEGQ KRKRRDINLK DENQLLSEEE YHKLLGSIR
//
