ID   A0A9E7JJH4_9LILI        Unreviewed;       555 AA.
AC   A0A9E7JJH4;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   SubName: Full=Adhesion regulating molecule {ECO:0000313|EMBL:URD83039.1};
GN   ORFNames=MUK42_19025 {ECO:0000313|EMBL:URD83039.1};
OS   Musa troglodytarum (fe'i banana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=320322 {ECO:0000313|EMBL:URD83039.1, ECO:0000313|Proteomes:UP001055439};
RN   [1] {ECO:0000313|EMBL:URD83039.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:URD83039.1};
RA   Wang J.;
RT   "The Musa troglodytarum L. genome provides insights into the mechanism of
RT   non-climacteric behaviour and enrichment of carotenoids.";
RL   Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the mago nashi family.
CC       {ECO:0000256|ARBA:ARBA00009270}.
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DR   EMBL; CP097503; URD83039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9E7JJH4; -.
DR   OrthoDB; 340431at2759; -.
DR   Proteomes; UP001055439; Chromosome 10.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035145; C:exon-exon junction complex; IEA:InterPro.
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   GO; GO:0008380; P:RNA splicing; IEA:InterPro.
DR   CDD; cd11295; Mago_nashi; 1.
DR   FunFam; 1.10.2020.20:FF:000002; 26S proteasome regulatory subunit RPN13; 1.
DR   FunFam; 3.30.1560.10:FF:000001; Protein mago nashi homolog; 1.
DR   Gene3D; 1.10.2020.20; -; 1.
DR   Gene3D; 3.30.1560.10; Mago nashi; 1.
DR   Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR   InterPro; IPR044867; DEUBAD_dom.
DR   InterPro; IPR004023; Mago_nashi.
DR   InterPro; IPR036605; Mago_nashi_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; PF02792; Mago_nashi; 1.
DR   Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR   Pfam; PF16550; RPN13_C; 1.
DR   SUPFAM; SSF89817; Mago nashi protein; 1.
DR   PROSITE; PS51916; DEUBAD; 1.
DR   PROSITE; PS51917; PRU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP001055439}.
FT   DOMAIN          275..396
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          430..531
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          180..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  62036 MW;  DACD922A93A88D4F CRC64;
     MRRLNRQNGK TAPLKRVLRR EAVAVVPAAT ATMAASGAGG DQDEFYLRYY VGHKGKFGHE
     FLEFEFRPDG KLRYANNSNY KNDTMIRKEV FVSPAVLREC RRIIADSEIM REDDNNWPPP
     DRVGRQELEI VMNNEHISFT TSKIGSLVDV QGSQDPEGLR VFYYLVQIIL IKHSRHRNVW
     KSSTRHETRS TQPSESGFHE PLQPDMSATT PDTSLFTDQG AMTTNTPSPR ALKSPPGNLR
     PKSAFPRRGT DISTLFESKL ESAIDYILEV QRDWIVNDGE RCSAAGKMVL NGTRVVPDTR
     KGLVRIGRSE EGLVHFQWLD RTQNVVEDDQ IIFPDEAVFE KVSQSSERVY LLKFRHDNLM
     GEDEAEASVP PQMSDTSDNT VEDDFSSRAG NLVDQNIAGE LGGEVTSSAR PVQLADLQRI
     LRSIQPADAI EDPDAGLGLG DILKPDLVLP LIETLPIEQQ LAQYLPEGSW SPADLMELLQ
     SPQFRQQVDT FTHVLRTGQI DLSQFGINPN KFTVLSFLEA LEDSVAKSSE AAGSNSAQDE
     SKDSQSQRCG RDSTI
//