ID H2XWD3_CIOIN Unreviewed; 239 AA.
AC H2XWD3; A0A1W3JJJ0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000256|PIRNR:PIRNR017888};
GN Name=LOC104266883 {ECO:0000313|Ensembl:ENSCINP00000033967.1};
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:ENSCINP00000033967.1, 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:ENSCINP00000033967.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that
CC functions as an activator of the pre-mRNA 3'-end cleavage and
CC polyadenylation processing required for the maturation of pre-mRNA into
CC functional mRNAs. CFIm contributes to the recruitment of multiprotein
CC complexes on specific sequences on the pre-mRNA 3'-end, so called
CC cleavage and polyadenylation signals (pA signals). Most pre-mRNAs
CC contain multiple pA signals, resulting in alternative cleavage and
CC polyadenylation (APA) producing mRNAs with variable 3'-end formation.
CC The CFIm complex acts as a key regulator of cleavage and
CC polyadenylation site choice during APA through its binding to 5'-UGUA-
CC 3' elements localized in the 3'-untranslated region (UTR) for a huge
CC number of pre-mRNAs. {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBUNIT: Homodimer (via N- and C-terminus); binds RNA as homodimer.
CC Component of the cleavage factor Im (CFIm) complex.
CC {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR017888}.
CC Cytoplasm {ECO:0000256|PIRNR:PIRNR017888}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC {ECO:0000256|PIRNR:PIRNR017888}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EAAA01000380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009862495.1; XM_009864193.1.
DR AlphaFoldDB; H2XWD3; -.
DR STRING; 7719.ENSCINP00000033967; -.
DR Ensembl; ENSCINT00000034903.1; ENSCINP00000033967.1; ENSCING00000018240.1.
DR GeneTree; ENSGT00390000015814; -.
DR HOGENOM; CLU_068704_2_1_1; -.
DR InParanoid; H2XWD3; -.
DR OMA; NDEWEIG; -.
DR OrthoDB; 142507at2759; -.
DR TreeFam; TF106356; -.
DR Proteomes; UP000008144; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR13047:SF0; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 5; 1.
DR PANTHER; PTHR13047; PRE-MRNA CLEAVAGE FACTOR IM, 25KD SUBUNIT; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR PIRSF; PIRSF017888; CPSF-25; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR017888};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR017888};
KW Nucleus {ECO:0000256|PIRNR:PIRNR017888};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW RNA-binding {ECO:0000256|PIRNR:PIRNR017888}.
FT DOMAIN 88..213
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 239 AA; 27461 MW; 587A986F7343AA75 CRC64;
MTARRQSSGS GWPRYQQQQQ QQQGYNDVNN AQGDTNSTTK ISQYINRGIN LYPLTNYTFG
TKEPLYERDS TVQARFQRMR EEFDKAGQRR SVEGVLIVHE HGLPHVLLLQ LGTTFFKLPG
GELHNGENEV DGLKRLMTET LGRQDGVAQD WVIEDCIGNW WRPNFEPPLY PYIPAHITKP
KEHKKLFLVQ LGEKALFAVP RNYKLVAAPL FELYDNSNGY GPVISSLPQL LSRFNFVYN
//
