ID A0A2U9CUR1_SCOMX Unreviewed; 873 AA.
AC A0A2U9CUR1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=26S protease regulatory subunit 4 {ECO:0000313|EMBL:AWP19720.1};
GN ORFNames=F2P81_023806 {ECO:0000313|EMBL:KAF0023176.1}, SMAX5B_008153
GN {ECO:0000313|EMBL:AWP19720.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP19720.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP19720.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0023176.1, ECO:0000313|Proteomes:UP000438429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ysfricsl-2016a {ECO:0000313|EMBL:KAF0023176.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAF0023176.1};
RA Xu H., Xu X.-W., Shao C., Chen S.;
RT "Draft genomes of female and male turbot (Scophthalmus maximus).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC ECO:0000256|RuleBase:RU003857}.
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DR EMBL; CP026262; AWP19720.1; -; Genomic_DNA.
DR EMBL; VEVO01000022; KAF0023176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CUR1; -.
DR STRING; 52904.ENSSMAP00000006921; -.
DR Proteomes; UP000246464; Chromosome 20.
DR Proteomes; UP000438429; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR005410; 2pore_dom_K_chnl_THIK.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01588; THIKCHANNEL.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AWP19720.1};
KW Ion channel {ECO:0000256|RuleBase:RU003857};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:AWP19720.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 22..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 651..790
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 336..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 97099 MW; E24B21579D4D7403 CRC64;
MMACRSGGCC GSGPINEDNA RFLLLALFIV IYLFCGAAVF SALEQPKERE AKERWAHRFE
LFSQKYNLSR KDLHNFLRSY EEANVAGIRV DTVRPRWDFT GAFYFVGTVV STIGFGMTTP
ATVGGKVFLM FYGLLGCAAT LLFFNLFLER VITVIAVVLK SCHELRHSKA VLPQNGRRVS
EENRPAVAAG GGRGRGEDLA GWKPSVYCVM VILGVAAILV SCCASFMYSA AEGWGYLDSL
YFCFVAFSTI GFGDMVSSQR VVYDGHASVA YQMGNFFFIL TGVCCIYSLF NVISIVIKQV
LNWLLRRLEA PCRCCHPRRG HHPHRHPRRN VVAPGHLRTR RDPSIETDAM NESETDAGRR
MSGEMISMRD FLAANKVNLA IMQKQLSEMA IGHPRQSSSS SRQNGFSGGV GALGIMNNRV
AVPSDVTPER QVTMGQSQSG GHGPGGGKKD DKDKKKKYEP PIPTRVGKRK KKSKGPDAAS
KLPLVTPHTQ CRLKLLKQER IKDYLLMEEE FIRNQEQMKP LEEKQEEERS KVDDLRGTPM
SVGTLEEIID DNHAIVSTSV GSEHYVSILS FVDKDLLEPG CSVLLNHKVH AVIGVLMDDT
DPLVTVMKVE KAPQETYADI GGLDNQIQEI KESVELPLTH PEYYEEMGIK PPKGVILYGA
PGTGKTLLAK AVANQTSATF LRVVGSELIQ KYLGDGPKLV RELFRVAEEH APSIVFIDEI
DAIGTKRYDS NSGGEREIQR TMLELLNQLD GFDSRGDVKV IMATNRIETL DPALIRPGRI
DRKIEFPLPD EKTKRRIFQI HTSRMTVADD VTLDDLILAK DDLSGADIKA ICTEAGLMAL
RERRMKVTNE DFKKSKENVL YKKQEGTPEG LYL
//
