ID A0A8J6L300_TENMO Unreviewed; 1102 AA.
AC A0A8J6L300;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAH0809769.1};
GN ORFNames=GEV33_013022 {ECO:0000313|EMBL:KAH0809769.1};
OS Tenebrio molitor (Yellow mealworm beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrio.
OX NCBI_TaxID=7067 {ECO:0000313|EMBL:KAH0809769.1, ECO:0000313|Proteomes:UP000719412};
RN [1] {ECO:0000313|EMBL:KAH0809769.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stoneville {ECO:0000313|EMBL:KAH0809769.1};
RC TISSUE=Whole head {ECO:0000313|EMBL:KAH0809769.1};
RA Eriksson T., Andere A., Kelstrup H., Emery V., Picard C.;
RT "The yellow mealworm (Tenebrio molitor) genome: a resource for the emerging
RT insects as food and feed industry.";
RL J Insects Food Feed 6:445-455(2020).
RN [2] {ECO:0000313|EMBL:KAH0809769.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Stoneville {ECO:0000313|EMBL:KAH0809769.1};
RC TISSUE=Whole head {ECO:0000313|EMBL:KAH0809769.1};
RA Eriksson T.;
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KAH0809769.1}.
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DR EMBL; JABDTM020027926; KAH0809769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J6L300; -.
DR Proteomes; UP000719412; Unassembled WGS sequence.
DR GO; GO:0005594; C:collagen type IX trimer; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR009057; Homeodomain-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR038717; Tc1-like_DDE_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1116; MACROPHAGE RECEPTOR WITH COLLAGENOUS STRUCTURE; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF13358; DDE_3; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000719412};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1102
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035154160"
FT DOMAIN 616..781
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT DOMAIN 910..1019
FT /note="Tc1-like transposase DDE"
FT /evidence="ECO:0000259|Pfam:PF13358"
FT REGION 106..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..138
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..262
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 120162 MW; 0F249CDB753CC409 CRC64;
MAMVLSSQSR LLVALCFTLL VLAGALAVGS LTGWFHPRIS SEPVPAKLRQ VERSDYDGTF
REGSGSEDFG FIPPPPPPPD GKLCMCNNEN CCNYLLNDIK AVYGNKGDKG EKGPRGPPGE
SIRGPPGPPG PPGLPGPVAP EDHLDLLGRG ERLEYRVIKA IEESGVFKAQ VGYKVPKGNL
ARMVFLENLV LPDLRDPLVR WNSKMLTKRF SVDPWYAQVF QEPKENRENP VLPAQEEKKG
ERGDRGFPGE KGTPGPKGEL GTSGLDGIPG TPGMHGKHGE KGEKGSPGPQ GPPGPPGISY
NGDMTSIIPG AQGVKGEPGE KGVKGDKGEE GEAGIPGVPG MHGTPGSSGE KGDPGIDGAI
GPVGSPGTKG EKGERGPPGS IITPNGNEEI ITIKGDKGEM GRRGRRGKPG PPGPAGPPGK
VGPIGEIGLP GWMVNLRVYF YIRVDRVLQD YQEFRDQKVK KEMPPKGDKG DRGERGQDGI
PGRDGRDGNP GPPGLPGAAP SDETVRYIPV AGPPGPPGPP GQPGISITGP KGEPGNYPYG
EPTYNLRPGR STASPPIFTV PEQEVTARIV PGAVTFQDHD AMIKMSSASP VGTLAYVIEE
EALLVRVNNG WQYIALRMAA LNEAYTGDVH GVRGADYSCY REARRAGLRG TFRAFLSSRV
QNVDSIVRLA DRKLPVSNLR GEVLFNSWSE MFKGDGAPFP HPPRIYSFNG KNVLTDLSWP
HKAVWHGALV NGERALDTSC DAWHSASRDK VGLAGSLKGP RLLEQTSYSC DKKLILLCIE
ATSELFVQRK RRDVDNRTKR MPLVSVDIAR TLALIEDGRS IRYAANAIKA TVTTVHRAIR
RFHETGQYTR RPGSGRRKAT THRDDRFLVS NILRDRQMTA VMIRNQLQEV WQVNTSKRPK
THPKPSEPFH GGSIMIWGGI SFEAHKDLVL VENGSLNAHR YIREILEPHV VPYGPFIGED
FVFMHDNARP HIAHCVSLYL DPVGIYRMDW PACSPDLNPI EHVWDKLGRQ IRSRPVGDEK
SKKSVTHKIP KFRLSWGSQR YGIQHETENH TTLQTSTGDF VKSRKSVRSQ ENAATKFTQS
RFSRPAQPGK QKREFITYPK KI
//
