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Database: UniProt
Entry: A0A158P2X0_ATTCE
LinkDB: A0A158P2X0_ATTCE
Original site: A0A158P2X0_ATTCE 
ID   A0A158P2X0_ATTCE        Unreviewed;       838 AA.
AC   A0A158P2X0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JAN-2026, entry version 41.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:XP_012064128.1};
GN   Name=105627455 {ECO:0000313|EnsemblMetazoa:XP_012064128.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012064128.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012064128.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
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DR   EMBL; ADTU01007638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADTU01007639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A158P2X0; -.
DR   EnsemblMetazoa; XM_012208738.1; XP_012064128.1; LOC105627455.
DR   KEGG; acep:105627455; -.
DR   eggNOG; KOG3546; Eukaryota.
DR   InParanoid; A0A158P2X0; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000005205; 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   CDD; cd00247; Endostatin-like; 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; IPR016187; CTDL_fold.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   Pfam; PF01391; Collagen; 3.
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:UP000005205}.
FT   DOMAIN          553..601
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          637..802
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          31..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..256
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..299
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..370
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..404
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..478
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  86213 MW;  E354821D59C90628 CRC64;
     MKIPQGPPGQ KGDPGTCTCN ATALMSSFTM PKMIQGPKGE PGVPGQEGKQ GLMGLTGAAG
     PPGERGLHGP SGAKGDKGDI GIAGPEGSQG QKGEPGRDGI SGEKGAQGPP GPPGKGEFSG
     YDPSWKPRNI YRPEGITMRP GLPGQKGEPG ISGNPGPKGE AGIPGSKGIK GEPGHKGIKG
     DHGKDGPRGI QGFKGEPGAP GAPGLPGAPG ENGRPAEKGD KGDTGPEGKL GPPGPPGPPG
     VSGSGGINVG DLGFGSKGDK GDSGARGYKG DKGTKGEKGN KGDAGPAGIP GINGIQGPQG
     DKGEPGKDGV SGLPGIPGAK GERGERGPPG ATTVANSGDY ITIKGEKGAE GKRGRRGRPG
     PPGPVGPPGK PGNTGEIGLP GWMNSMKGRP GTPGIPGSIG PMGPKGEKGE PGAPSPYGVS
     VGIKGDKGDD GFPGIPGQPG REGQKGSPGP PGPPGIPSKG NYHPVPGPPG PPGPPGPPGL
     SLIGQKGEPG IGRSHVFGER DYYPPRQGAR SSLDELKALR ELKQLKELKE QLGVVTTATR
     GPLESTTKIV PGAVTFQNTE AMTKMSSVSP VGTLAYIIDE QALLVRVNNG WQYIALGSLL
     PITTPAPPTT SPPPANPPFE ASNLINQIPV KADGTGLRMA ALNEPFTGDM HGIRGADYAC
     YRQARRAGLR GTFRAFLSSR VQNVDSIVRL GDRDLPIVNI KGDVLFNSWK EMFNGNGAYF
     SQNPRIYSFN GKNILTDFAW PEKVAWHGSH KLGDRAMDTY CDAWHSSSSD RYGLGSPLTG
     GRLLEQVRYS CDNKFALLCI EVTSELVRRR RNADNRLDDD VEMSENDYME YLEEFMQY
//
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