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Database: UniProt
Entry: F6YTK9_CIOIN
LinkDB: F6YTK9_CIOIN
Original site: F6YTK9_CIOIN 
ID   F6YTK9_CIOIN            Unreviewed;       445 AA.
AC   F6YTK9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=26S proteasome regulatory subunit 4 {ECO:0000313|Ensembl:ENSCINP00000007310.3};
GN   Name=LOC100182082 {ECO:0000313|Ensembl:ENSCINP00000007310.3};
OS   Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000007310.3, ECO:0000313|Proteomes:UP000008144};
RN   [1] {ECO:0000313|Proteomes:UP000008144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12481130; DOI=10.1126/science.1080049;
RA   Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA   Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA   Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA   Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA   Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA   Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA   Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA   Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA   Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA   Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA   Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA   Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA   Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA   Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA   Satoh N., Rokhsar D.S.;
RT   "The draft genome of Ciona intestinalis: insights into chordate and
RT   vertebrate origins.";
RL   Science 298:2157-2167(2002).
RN   [2] {ECO:0000313|Ensembl:ENSCINP00000007310.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR   AlphaFoldDB; F6YTK9; -.
DR   Ensembl; ENSCINT00000007310.3; ENSCINP00000007310.3; ENSCING00000003550.3.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_3_1; -.
DR   Proteomes; UP000008144; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd19502; RecA-like_PAN_like; 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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
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; PF16450; Prot_ATP_ID_OB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003651};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT   DOMAIN          223..362
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  49846 MW;  4E764AD6CCEAF54E CRC64;
     MGQNQSGGGR NGAGDNKKGD KGKEKKKYER PLPTRVGKRR KKAKGPDAAN KLPSDTVTPH
     TRCRLRLLKQ ERIKDYLLME EEYIRNQERL KPQEEKQEEE RTKVDDLRGS PMSVGTLEEI
     IDENHAIVST SVGSEHYVSI LSFVDKDLLE PGCTVLMNHK VHAVVGFLGD DVDPLVTVMK
     LEKAPKESYA DIGGLDTQIT EIKESVELPL THPEYYEEMG IKPPKGVILY GPPGTGKTLL
     AKAVANQTSA TFLRVVGSEL IQKYLGDGPK LVRELFRVAE EHAPSIVFID EIDAIGTKRY
     ESNSGGEREI QRTMLELLNQ LDGFDSRGDV KVIMATNRID SLDPALIRAG RIDRKIEFPM
     PDEKTKRRIF NIHTARMTLS DDVNVDEHVQ AKDDLSGADI KAICTEAGLL ALRERRMKVT
     SEDFKKSKEN VLYRKNEGAP QGLYL
//
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