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Database: UniProt
Entry: L8GSN9_ACACF
LinkDB: L8GSN9_ACACF
Original site: L8GSN9_ACACF 
ID   L8GSN9_ACACF            Unreviewed;       398 AA.
AC   L8GSN9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   08-OCT-2025, entry version 33.
DE   SubName: Full=Adhesion regulating molecule region protein, putative {ECO:0000313|EMBL:ELR15116.1};
GN   ORFNames=ACA1_215980 {ECO:0000313|EMBL:ELR15116.1};
OS   Acanthamoeba castellanii (strain ATCC 30010 / Neff).
OC   Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC   Acanthamoebidae; Acanthamoeba.
OX   NCBI_TaxID=1257118 {ECO:0000313|EMBL:ELR15116.1, ECO:0000313|Proteomes:UP000011083};
RN   [1] {ECO:0000313|EMBL:ELR15116.1, ECO:0000313|Proteomes:UP000011083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Neff {ECO:0000313|EMBL:ELR15116.1,
RC   ECO:0000313|Proteomes:UP000011083};
RX   PubMed=23375108; DOI=10.1186/gb-2013-14-2-r11;
RA   Clarke M., Lohan A.J., Liu B., Lagkouvardos I., Roy S., Zafar N.,
RA   Bertelli C., Schilde C., Kianianmomeni A., Burglin T.R., Frech C.,
RA   Turcotte B., Kopec K.O., Synnott J.M., Choo C., Paponov I., Finkler A.,
RA   Soon Heng Tan C., Hutchins A.P., Weinmeier T., Rattei T., Chu J.S.,
RA   Gimenez G., Irimia M., Rigden D.J., Fitzpatrick D.A., Lorenzo-Morales J.,
RA   Bateman A., Chiu C.H., Tang P., Hegemann P., Fromm H., Raoult D., Greub G.,
RA   Miranda-Saavedra D., Chen N., Nash P., Ginger M.L., Horn M., Schaap P.,
RA   Caler L., Loftus B.;
RT   "Genome of Acanthamoeba castellanii highlights extensive lateral gene
RT   transfer and early evolution of tyrosine kinase signaling.";
RL   Genome Biol. 14:R11-R11(2013).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KB008036; ELR15116.1; -; Genomic_DNA.
DR   RefSeq; XP_004337129.1; XM_004337081.1.
DR   AlphaFoldDB; L8GSN9; -.
DR   STRING; 1257118.L8GSN9; -.
DR   GeneID; 14915644; -.
DR   KEGG; acan:ACA1_215980; -.
DR   VEuPathDB; AmoebaDB:ACA1_215980; -.
DR   OMA; RSPQFMQ; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP000011083; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:TreeGrafter.
DR   GO; GO:0061133; F:endopeptidase activator activity; IEA:TreeGrafter.
DR   GO; GO:0070628; F:proteasome binding; IEA:TreeGrafter.
DR   CDD; cd13314; PH_Rpn13; 1.
DR   FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR   Gene3D; 1.10.2020.20; -; 1.
DR   Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR   InterPro; IPR044867; DEUBAD_dom.
DR   InterPro; IPR006773; Rpn13/ADRM1.
DR   InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR   InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR   InterPro; IPR032368; RPN13_DEUBAD.
DR   InterPro; IPR038108; RPN13_DEUBAD_sf.
DR   PANTHER; PTHR12225; ADHESION REGULATING MOLECULE 1 110 KDA CELL MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR12225:SF0; PROTEASOMAL UBIQUITIN RECEPTOR ADRM1; 1.
DR   Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR   Pfam; PF16550; RPN13_C; 1.
DR   PROSITE; PS51916; DEUBAD; 1.
DR   PROSITE; PS51917; PRU; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011083}.
FT   DOMAIN          29..143
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          257..362
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          180..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..232
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..368
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  41638 MW;  A3F1CBAB363979EA CRC64;
     MKVQSNFKYL RNVVGTRIYT RILNPCMFGP QKPLVEFKAG KMLIRGKMVI PDKRKGKIEL
     AQSPDDQLMH FRWKDRSTGQ VETDLIIFPD EAVFKKVKQC TTGRVFLLEW KSTERRLFFW
     MQEPSDEKDA ELCEKVNKAL NSPPAAEGGE AGAGGVPGLA GMSQEQLLAM MGMGGLGGMG
     GGGGARRGSA RGAAAASAPP SGAQPAAGGA RSAAPTPSTP APTTTARSTD ASIGEQQLQN
     ILRELGAAQG GGAGAAGGQA PEDVDLSSVM TSEALLPLLS NPAVAEQLLP YLPEGQRNPE
     ELRELVRSPQ FHQALQAFNS ALQSGALADV LPALGLPASA AGGGVQDFLR ALQEQSQRQS
     GGQQQQQGGS QGGNEPAGGE KKDDKDGSSG KDGDMDTS
//
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