ZN326_XENTR
ID ZN326_XENTR Reviewed; 489 AA.
AC Q28F29; B7ZT04; F6SBU2;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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; ORFNames=TGas098h07.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI70704.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI70732.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR762202; CAJ82513.1; -; mRNA.
DR EMBL; AAMC01118988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC170704; AAI70704.1; ALT_INIT; mRNA.
DR EMBL; BC170732; AAI70732.1; ALT_INIT; mRNA.
DR RefSeq; NP_001016086.2; NM_001016086.3.
DR AlphaFoldDB; Q28F29; -.
DR PaxDb; Q28F29; -.
DR GeneID; 548840; -.
DR KEGG; xtr:548840; -.
DR CTD; 284695; -.
DR Xenbase; XB-GENE-483978; znf326.
DR eggNOG; ENOG502QUAZ; Eukaryota.
DR InParanoid; Q28F29; -.
DR OMA; GEDFTCD; -.
DR OrthoDB; 902224at2759; -.
DR TreeFam; TF105407; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0044609; C:DBIRD complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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..489
FT /note="DBIRD complex subunit ZNF326"
FT /id="PRO_0000417537"
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..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..489
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 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..263
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"
SQ SEQUENCE 489 AA; 55078 MW; 69D56C38D9147DCC CRC64;
MDREYGSYNQ RSMDSYGNQS YSVDEMGDSN FSRFGPYESY DSRSSVGGRD LYRSGYGYND
HEQGHFGDSY DGRYENPYRN SVDSFEGRSQ GGSSWDPSFT RSKVRTGFME DRGRDSYSSY
GSFSSPYMKP ATVGSRGRGM PAYPENAFGG RSNDAFGGPS KGRGRGRGQM PEYGGIRRPG
LVGDYKQLGG AARGVARGVK RKMAPPFKPV GVFGKKQKLS KPGANQNKTV PPPAEKLSEE
EEEKRRTEAR REKQRRRREK NSEKYGDGMA FTCSFCKFRS FDEKGIEEHL SSTTHQEMLD
HIQKQTKFDK PVMEFLHECI VNKFKKTAAR RAQSLANEAA KALEKDVMEG VTPDDHMMKV
ETVHCSACSV YVPALHSSVQ LHLKSADHSK SKLAYKEQIK RESILTATSI LNNPLVKARY
ELYLKGENPF ETQPEEQQQE QEEEEEEEEQ QEQAAVPEQD LSEEQPAAIA AEPEGEDFTC
DPLTTTDEV
