ZN326_CHICK
ID ZN326_CHICK Reviewed; 566 AA.
AC Q5ZJ02; F1NCX4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 101.
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=RCJMB04_22c23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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=CAG32291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ720632; CAG32291.1; ALT_INIT; mRNA.
DR EMBL; AC140938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001006533.2; NM_001006533.2.
DR AlphaFoldDB; Q5ZJ02; -.
DR STRING; 9031.ENSGALP00000009853; -.
DR PaxDb; Q5ZJ02; -.
DR Ensembl; ENSGALT00000009867; ENSGALP00000009853; ENSGALG00000006113.
DR GeneID; 424512; -.
DR KEGG; gga:424512; -.
DR CTD; 284695; -.
DR VEuPathDB; HostDB:geneid_424512; -.
DR eggNOG; ENOG502QUAZ; Eukaryota.
DR GeneTree; ENSGT00530000063777; -.
DR HOGENOM; CLU_024193_2_0_1; -.
DR InParanoid; Q5ZJ02; -.
DR OMA; AYPENTF; -.
DR OrthoDB; 902224at2759; -.
DR PRO; PR:Q5ZJ02; -.
DR Proteomes; UP000000539; Chromosome 8.
DR Bgee; ENSGALG00000006113; Expressed in granulocyte and 13 other tissues.
DR GO; GO:0044609; C:DBIRD complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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..566
FT /note="DBIRD complex subunit ZNF326"
FT /id="PRO_0000075390"
FT ZN_FING 359..381
FT /note="C2H2 AKAP95-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT ZN_FING 452..475
FT /note="C2H2 AKAP95-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT REGION 19..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..263
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 318..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..566
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 541
FT /note="Missing (in Ref. 1; CAG32291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 63541 MW; D71081C208E62182 CRC64;
MDYGEAEDRD WRFPDTPMHC GVNMPSGSVS DMDRDYGHGG YGGPRSMDSY LNQSYGMESH
GGGGGGGGGG GNRFGPYESY DSGSSLGGRD LYRSGYGYNE PEQSRFGGSY GGRFDNSYRN
SLDSFGGRNQ GGSSWEAPYS RSKLRPGFME DRGRESYSSY SSFSSPHMKP APVGSRGRGT
PAYPESGFGS RNYDAFGGPS TGRGRGRGHM GDFGGMHRPG IVVDYHNKPS PAAVAARGIK
RKMMPQPYNK PGGTFIKKPK MTKPILKLTQ KKSSNMKSSF QDSTIEEIEV DTSGAVVIYE
DFTRDAYDVG YQTFGDSKGE GKSEEEEKRR IEARREKQRR RREKNSEKYG DGYRMAFTCS
FCKFRTFEEK EIESHLESAA HQETLDHIQK QTKFDKVVME FLHECMVNKF KKTAMRKQQT
SNQTENAQAV EKDIMEGVTA DDHMMKVETV HCSACSVYVP ALHSSVQQHL KSPDHTKGKQ
AYREQIKRES VLTATSILNN PIVKARYELY VKGENPFEIN DQAQEQQTEE EDKAEEPAEG
EEEEEEEEEE ETEEQTDFTL DHTEDN
