ID   ZN326_XENLA             Reviewed;         494 AA.
AC   A2RV70;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=DBIRD complex subunit ZNF326;
DE   AltName: Full=Zinc finger protein 326;
DE   AltName: Full=Zinc finger protein interacting with mRNPs;
GN   Name=znf326; Synonyms=zird;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Core component of the DBIRD complex, a multiprotein complex
CC       that acts at the interface between core mRNP particles and RNA
CC       polymerase II (RNAPII) and integrates transcript elongation with the
CC       regulation of alternative splicing. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the DBIRD complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01140}.
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DR   EMBL; BC133202; AAI33203.1; -; mRNA.
DR   RefSeq; NP_001091313.1; NM_001097844.1.
DR   AlphaFoldDB; A2RV70; -.
DR   BioGRID; 674417; 1.
DR   IntAct; A2RV70; 1.
DR   DNASU; 100037139; -.
DR   GeneID; 100037139; -.
DR   KEGG; xla:100037139; -.
DR   CTD; 100037139; -.
DR   Xenbase; XB-GENE-865034; znf326.S.
DR   OMA; GEDFTCD; -.
DR   OrthoDB; 902224at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 100037139; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0044609; C:DBIRD complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR007071; AKAP95.
DR   InterPro; IPR034736; ZF_C2H2_AKAP95.
DR   PANTHER; PTHR12190; PTHR12190; 1.
DR   Pfam; PF04988; AKAP95; 1.
DR   PROSITE; PS51799; ZF_C2H2_AKAP95; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..494
FT                   /note="DBIRD complex subunit ZNF326"
FT                   /id="PRO_0000417536"
FT   ZN_FING         273..295
FT                   /note="C2H2 AKAP95-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT   ZN_FING         365..388
FT                   /note="C2H2 AKAP95-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           200..221
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        7..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..454
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  55935 MW;  4E94CDDB79CED204 CRC64;
     MDREYGSYNQ RSVNSYGNQS FSMDEMGDSN FSRFGPYESY DSRSSVGGRD LYRSGYGYND
     HEQGHFGDSY DGRYENPYRN SVDSFEGRSQ GGSSWDPSFT RSKVRTGFME DRGRDSYSSY
     GSFSSPYMKP AAVGSRGRGM PAYPENAFGG RSNDAFGGPS KGRGRGRGQM PEYGVMRRHR
     VVVEYKHLGV AARGAARGVK RKMAPPFKPV GFFGKKQKLS KPGANQNKSV PPPAEKLSEE
     EEEKRRTEAR REKQRRRREK NSEKYGDGTA FTCSFCKFRS FDEKGIEEHL TSATHQEMLD
     HIQKQTKFDK PVMEFLHECI VNKFKKTVAR RVQSVANEAA KTLEKDVMEG VNPDDHMMKV
     ETVHCSACSV YVPALHSSVQ LHLKSADHSK SKLTYKEQIK RESILTATSI LNNPLVKARY
     ELYLKGENPF ETQPDEQQQE QEEEEEEEEQ QEQVAVSEQE PSEQETSDEQ AAAIAAEPEG
     EDFTCDPLTT TDEV