ID H2V5T2_TAKRU Unreviewed; 958 AA.
AC H2V5T2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 1 {ECO:0000256|ARBA:ARBA00014929, ECO:0000256|PIRNR:PIRNR015947};
GN Name=psmd1 {ECO:0000313|Ensembl:ENSTRUP00000044566.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000044566.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000044566.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000044566.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; H2V5T2; -.
DR STRING; 31033.ENSTRUP00000044566; -.
DR Ensembl; ENSTRUT00000044716.3; ENSTRUP00000044566.3; ENSTRUG00000017396.3.
DR eggNOG; KOG2062; Eukaryota.
DR GeneTree; ENSGT00940000153386; -.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; H2V5T2; -.
DR OMA; IMFGRQE; -.
DR OrthoDB; 151732at2759; -.
DR TreeFam; TF105742; -.
DR Proteomes; UP000005226; Chromosome 20.
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 Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 769..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..346
FT /note="26S proteasome non-ATPase regulatory subunit 1/RPN2
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21505"
FT DOMAIN 786..928
FT /note="26S proteasome regulatory subunit RPN2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18004"
FT REGION 276..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..958
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 106422 MW; 49FC47F740F149ED CRC64;
MITSAAGIIS LLDEEEPQLK EFALHKLNSI VNDFWAEISG SVDKIEVLYE DETFRSRAFA
ALVASKVFYH LGAFEESLNY ALGAGELFNV TDESEYVETI IAKCIDHYTK LRVENAELPE
DQEKKSVDPR LEGIVNKMFQ RCLDDRMYKQ AIGIALETRR LDMFEKTILE SNDVSGLLAY
SLKLCMSLMQ NKKFRNEVLR VLVKLYMNLE KPDFINVCQC LIFLDDPQAV SDILEKLVKE
DNLLMAYQIC FDLYESASQQ FLSSVIQNLR TVGTPIPSVP GSTNTGTVST SDKDSDAMET
DEKPGSSPAG KPEAKDEPKD QNAKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV
RNSVCHTATV IANSFMHTGT TSDQFLRENL EWLARATNWA KFTATASLGV IHKGHEKEAL
QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLGQLKNASN DIVRHGGALG
LGLAALGTAR QDVYDLLKSN LYQDDAVTGE AAGLALGLVM LGSKSAQAIE DMVGYAQETQ
HEKILRGLAV GIAMVMYGRM EEADALIESL CRDKDAILRR SGMYTVGMAY CGSGNNKAIR
RLLHVAVSDV NDDVRRAAVE SIGFILFRTP EQCPSVVSLL SESYNPHVRC GAAMALGICC
AGTGHKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQSE VTCPKVNQFR QLYSKVINDK
HDDVMAKFGA ILAQGILDAG GRNVTISLQS RTGHTHMPSV VGLLVFTQFW FWFPLSHFLS
LAFTPTAIIG LNKDLKMPKV QYRSNCKPST FAYPPALEIP KEKEKEKVST AVLSITAKAK
KKEKEKKEKE EEKMEVEVQE GEKKEEEKEK EKKKEVEPNF QLLENPARAM PAQLKVLTMP
ETCRYQPFKP LHTGGIIIMK DTSEEEEELV EPVSAHGPKI EEEEQEPEPP EPFEYIDE
//
