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Database: UniProt
Entry: B9SAC2_RICCO
LinkDB: B9SAC2_RICCO
Original site: B9SAC2_RICCO 
ID   B9SAC2_RICCO            Unreviewed;       557 AA.
AC   B9SAC2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Adhesion regulating molecule, putative {ECO:0000313|EMBL:EEF39452.1};
GN   ORFNames=RCOM_1237900 {ECO:0000313|EMBL:EEF39452.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; EQ973903; EEF39452.1; -; Genomic_DNA.
DR   RefSeq; XP_002522941.1; XM_002522895.2.
DR   AlphaFoldDB; B9SAC2; -.
DR   STRING; 3988.B9SAC2; -.
DR   GeneID; 8282890; -.
DR   KEGG; rcu:8282890; -.
DR   eggNOG; KOG3037; Eukaryota.
DR   InParanoid; B9SAC2; -.
DR   OrthoDB; 5483381at2759; -.
DR   Proteomes; UP000008311; 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; IBA:GO_Central.
DR   GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   CDD; cd13314; PH_Rpn13; 1.
DR   CDD; cd00590; RRM_SF; 1.
DR   Gene3D; 1.10.2020.20; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR   InterPro; IPR044867; DEUBAD_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
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   SUPFAM; SSF54928; RNA-binding domain, RBD; 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:UP000008311}.
FT   DOMAIN          249..361
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          431..534
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..126
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..180
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  62916 MW;  BD4BE8C74A22213B CRC64;
     MPPRTVKRGA AAAGPKRTAR TARGAAKGQS QQLEAAEERP KAEESPTITE NPFFEDKQLL
     EKPISEENRG LEDKIGGESD ANGSALLKKG EDVKDSVQEY EKDERLELDD NEPEEYGGVD
     YDDKEIEQDE VQEVEVGYEV EEEHEEHLGE EEEEGDLVEE ELEDVAEELE EGEEDDEHAG
     EEADHAQMVN AEEEEHHGVF KERRKRKEFE VFVGGLDKDA TEDDLRKVFT RVGFATVEQA
     KKAVTELKNP VETMLEFRAG KMFFEEKKVI PDTRKGLVRI ARGEEGLVHF QWLDRNRNVV
     EDDQIIFPDE AVFEKVNQAS GRVYILKFNT DDRKFFFWMQ EPKAEDDWQL CSSVNYYINR
     PLEFLGEEEP DAYAPLQVSE DMVEDDISSR AGNLVVPNLG AEVSDVSSSS GPVKLEDLQR
     ILSNIGHGGG AGDPDAGLGL GDILKPDLIL PFIDTLPLEE RLASYLPEGQ WTPEDILELL
     QSPPFRQQMD SFTYVLRTGQ IDLSQFGIDP SKYKFTVLSF LEALEDSASP VSEESRQEDK
     DLTSQSCDRN DPMDESH
//
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