PANKY_MOUSE
ID PANKY_MOUSE Reviewed; 385 AA.
AC Q8BXP5; D5G1T0; Q8BXP4; Q8R1Z1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Photoreceptor ankyrin repeat protein {ECO:0000303|PubMed:20026326};
DE AltName: Full=Ankyrin repeat domain-containing protein 33 {ECO:0000312|MGI:MGI:2443398};
GN Name=Ankrd33 {ECO:0000312|MGI:MGI:2443398};
GN Synonyms=Panky {ECO:0000303|PubMed:20026326};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2),
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), TISSUE SPECIFICITY
RP (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE (ISOFORM 1), AND INDUCTION (ISOFORM
RP 1).
RC TISSUE=Retina;
RX PubMed=20026326; DOI=10.1016/j.febslet.2009.12.030;
RA Sanuki R., Omori Y., Koike C., Sato S., Furukawa T.;
RT "Panky, a novel photoreceptor-specific ankyrin repeat protein, is a
RT transcriptional cofactor that suppresses CRX-regulated photoreceptor
RT genes.";
RL FEBS Lett. 584:753-758(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 59-252 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: [Isoform 1]: Acts as a transcriptional repressor for CRX-
CC activated photoreceptor gene regulation. {ECO:0000269|PubMed:20026326}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:20026326}. Nucleus {ECO:0000269|PubMed:20026326}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Panky-A {ECO:0000303|PubMed:20026326};
CC IsoId=Q8BXP5-1; Sequence=Displayed;
CC Name=2; Synonyms=Panky-B {ECO:0000303|PubMed:20026326};
CC IsoId=Q8BXP5-2; Sequence=VSP_059268;
CC -!- TISSUE SPECIFICITY: Isoform 1: Expressed predominantly in the retina.
CC Isoform 2: Expressed in the pineal gland.
CC {ECO:0000269|PubMed:20026326}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Predominantly expressed in developing
CC and mature photoreceptors (at protein level).
CC {ECO:0000269|PubMed:20026326}.
CC -!- INDUCTION: [Isoform 1]: Expression is up-regulated by the CRX
CC transcription factor. {ECO:0000269|PubMed:20026326}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31971.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; FJ895380; ADA60445.1; -; mRNA.
DR EMBL; AK044543; BAC31971.1; ALT_SEQ; mRNA.
DR EMBL; AK044546; BAC31973.1; -; mRNA.
DR EMBL; CH466550; EDL04067.1; -; Genomic_DNA.
DR EMBL; BC022726; AAH22726.1; -; mRNA.
DR CCDS; CCDS27845.1; -. [Q8BXP5-2]
DR RefSeq; NP_659039.1; NM_144790.1. [Q8BXP5-2]
DR RefSeq; XP_006520750.1; XM_006520687.1.
DR AlphaFoldDB; Q8BXP5; -.
DR SMR; Q8BXP5; -.
DR BioGRID; 228969; 1.
DR IntAct; Q8BXP5; 1.
DR STRING; 10090.ENSMUSP00000067028; -.
DR iPTMnet; Q8BXP5; -.
DR PhosphoSitePlus; Q8BXP5; -.
DR PaxDb; Q8BXP5; -.
DR PRIDE; Q8BXP5; -.
DR ProteomicsDB; 294245; -. [Q8BXP5-1]
DR Antibodypedia; 50682; 69 antibodies from 20 providers.
DR DNASU; 208258; -.
DR Ensembl; ENSMUST00000070875; ENSMUSP00000067028; ENSMUSG00000047034. [Q8BXP5-2]
DR Ensembl; ENSMUST00000229954; ENSMUSP00000155584; ENSMUSG00000047034. [Q8BXP5-1]
DR GeneID; 208258; -.
DR KEGG; mmu:208258; -.
DR UCSC; uc007xsk.1; mouse. [Q8BXP5-2]
DR UCSC; uc011zzq.1; mouse.
DR CTD; 341405; -.
DR MGI; MGI:2443398; Ankrd33.
DR VEuPathDB; HostDB:ENSMUSG00000047034; -.
DR eggNOG; ENOG502QRWZ; Eukaryota.
DR GeneTree; ENSGT00500000044852; -.
DR HOGENOM; CLU_049994_1_0_1; -.
DR InParanoid; Q8BXP5; -.
DR OMA; KKRQKGY; -.
DR OrthoDB; 1045586at2759; -.
DR TreeFam; TF332022; -.
DR BioGRID-ORCS; 208258; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ankrd33; mouse.
DR PRO; PR:Q8BXP5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BXP5; protein.
DR Bgee; ENSMUSG00000047034; Expressed in retinal neural layer and 12 other tissues.
DR ExpressionAtlas; Q8BXP5; baseline and differential.
DR Genevisible; Q8BXP5; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..385
FT /note="Photoreceptor ankyrin repeat protein"
FT /id="PRO_0000243909"
FT REPEAT 17..46
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 53..83
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 87..116
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 122..151
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 156..190
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REGION 270..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..55
FT /note="MSEALPFPSNKTSTPECNLKTLYWACVHNDLAELQARLDAGVSPEEASQVDS
FT NGR -> METLESQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_059268"
FT CONFLICT 71
FT /note="A -> V (in Ref. 2; BAC31973)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="L -> Q (in Ref. 2; BAC31973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41599 MW; 379F81E94697BE1A CRC64;
MSEALPFPSN KTSTPECNLK TLYWACVHND LAELQARLDA GVSPEEASQV DSNGRTGLMV
ACYHGFGSIV ALLSCCPFLD VNQQDKDGNT ALMLAAQAGH MSLVTLLLNY FAGLDLERRD
QRGLTALMKA AIQDRSECVV ALLMAGADLS SVDPVRGKTA LEWAVLTDSF DTAQKIRQLL
RRPQAEQLSL HYQPEWPALA QLVAQAQAQA QAPAAPSLLE RLQATLSLSF AQSPQEGGVL
DHLVTVTTSL ASPFLSTACH TLCPDHPPKL GTRGKSVPEL LGTAPPPPPE PHPPQQVPVP
QVFAPNQSPQ SMFSQWLQSR DSTRSQVPKI LLSKAPSPSA RYELTLRPQG QQSLAPPVWR
FQERKKKEEE TEPRGGGLGQ AGGSK
