ID   A0A3B3VXC9_9TELE        Unreviewed;       878 AA.
AC   A0A3B3VXC9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 1 {ECO:0000256|ARBA:ARBA00014929, ECO:0000256|PIRNR:PIRNR015947};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000029527.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000029527.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       This complex plays a key role in the maintenance of protein homeostasis
CC       by removing misfolded or damaged proteins, which could impair cellular
CC       functions, and by removing proteins whose functions are no longer
CC       required. Therefore, the proteasome participates in numerous cellular
CC       processes, including cell cycle progression, apoptosis, or DNA damage
CC       repair. {ECO:0000256|ARBA:ARBA00002362, ECO:0000256|PIRNR:PIRNR015947}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). {ECO:0000256|PIRNR:PIRNR015947}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S1 family.
CC       {ECO:0000256|ARBA:ARBA00006308, ECO:0000256|PIRNR:PIRNR015947}.
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DR   AlphaFoldDB; A0A3B3VXC9; -.
DR   Ensembl; ENSPLAT00000024583.1; ENSPLAP00000029527.1; ENSPLAG00000019925.1.
DR   GeneTree; ENSGT00940000153386; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR016642; 26S_Psome_Rpn2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR   InterPro; IPR048570; PSMD1_RPN2_N.
DR   InterPro; IPR040623; RPN2_C.
DR   PANTHER; PTHR10943; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10943:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 1; 1.
DR   Pfam; PF13646; HEAT_2; 1.
DR   Pfam; PF01851; PC_rep; 4.
DR   Pfam; PF18004; RPN2_C; 1.
DR   Pfam; PF21505; RPN2_N; 1.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PIRNR:PIRNR015947};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        770..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..347
FT                   /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21505"
FT   DOMAIN          787..857
FT                   /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18004"
FT   REGION          277..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  96798 MW;  F299D70EF1B18D7C CRC64;
     MITSAAGIIS LLDEEEPKLK EFALHKLDSI VNDFWAEISG SVDKIEVLYE DESFQSREFA
     ALVASKVFYH LGAFEESLNY ALGAGDLFSV TDDSEYVETI IAKCIDHYTK LRVENAELSE
     DEEKKKIDPR LEGIVNKMFL RCLDDHKYKQ AIGIALETRR LDIFEKTILE SNDVSGLLAY
     SLKVCMSLMQ NKKFRNDVLR VLVKLYMNLE KPDFINVCQC LIFLDDPQAV SDILEKLVKE
     DNLLMAYQIC FDLYESASQQ FLSSVIQNLH TVGTPIPAVP GSTNTGTVPT ADKESEAMET
     DEKAGSSPAG KAAETKEEPK DQNAKMITIL SGEMTIELHL QFLIRNNNTD LMILKNTKDA
     VRNSVCHTAT VIANSFMHTG TTSDQFLREN LEWLARATNW AKFTATASLG VIHKGHEKEA
     LQLMATYLPK DTSPGSAYQE GGGLYALGLI HANHGGDIID YLLGQLKNAS NDIVRHGGAL
     GLGLAALGTA RQDVYDLLKS NLYQDDAVTG EAAGLALGLV MLGSKSAQAI EDMVGYAQET
     QHEKILRGLA VGIALVMYGR MEEADALIES LCRDKDPILR RSGMYTVGMA YCGSGNNKAI
     RRLLHVAVSD VNDDVRRAAV ESIGFILFRT PEQCPSVVSL LSESYNPHVR CGAAMALGIC
     CAGTGNKEAI NLLEPMTNDP VNYVRQGALI ASALIMIQQT EVTCPKVNQF RQLYAKVIND
     KHDDVMAKFG AILAQGILDA GGRNVSISLQ SRTGHTHMPS VVGLLVFTQF WFWFPLSHFL
     SLAFTPTAII GLNKDLKMPK VQYRSNCKPS TFAYPPALEV PKEKEKEKVS TAVLSITAKA
     KKKEKEKKEK EEEKMEVVSG SLHKAPSFSL LLRLYRCG
//