ID DZAN1_MOUSE Reviewed; 778 AA.
AC Q8C008; A2AN93; Q8C060;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 24-JAN-2024, entry version 143.
DE RecName: Full=Double zinc ribbon and ankyrin repeat-containing protein 1;
GN Name=Dzank1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEIN SEQUENCE OF 212-223, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-768, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in vesicle transport in photoreceptor cells.
CC {ECO:0000250|UniProtKB:Q1LXR6}.
CC -!- SUBUNIT: Interacts with NINL. Associates with DYNC1H1 and multiple
CC dynein intermediate and light chains as well as actin-binding proteins.
CC {ECO:0000250|UniProtKB:Q9NVP4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q9NVP4}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9NVP4}.
CC Note=Colocalizes with NINL at the base of cilia.
CC {ECO:0000250|UniProtKB:Q9NVP4}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27747.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27960.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AK032182; BAC27747.1; ALT_FRAME; mRNA.
DR EMBL; AK032632; BAC27960.1; ALT_SEQ; mRNA.
DR EMBL; AL808119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38254.1; -.
DR RefSeq; NP_766447.2; NM_172859.2.
DR AlphaFoldDB; Q8C008; -.
DR SMR; Q8C008; -.
DR BioGRID; 232341; 6.
DR IntAct; Q8C008; 6.
DR MINT; Q8C008; -.
DR STRING; 10090.ENSMUSP00000080643; -.
DR iPTMnet; Q8C008; -.
DR PhosphoSitePlus; Q8C008; -.
DR MaxQB; Q8C008; -.
DR PaxDb; 10090-ENSMUSP00000080643; -.
DR ProteomicsDB; 277429; -.
DR Antibodypedia; 54096; 36 antibodies from 10 providers.
DR DNASU; 241688; -.
DR Ensembl; ENSMUST00000081982.12; ENSMUSP00000080643.6; ENSMUSG00000037259.16.
DR GeneID; 241688; -.
DR KEGG; mmu:241688; -.
DR UCSC; uc008mrd.1; mouse.
DR AGR; MGI:2139080; -.
DR CTD; 55184; -.
DR MGI; MGI:2139080; Dzank1.
DR VEuPathDB; HostDB:ENSMUSG00000037259; -.
DR eggNOG; ENOG502QTJR; Eukaryota.
DR GeneTree; ENSGT00390000000549; -.
DR InParanoid; Q8C008; -.
DR OMA; QTNICIK; -.
DR OrthoDB; 2940197at2759; -.
DR TreeFam; TF351270; -.
DR BioGRID-ORCS; 241688; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Dzank1; mouse.
DR PRO; PR:Q8C008; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C008; Protein.
DR Bgee; ENSMUSG00000037259; Expressed in lateral hypothalamic area and 176 other cell types or tissues.
DR ExpressionAtlas; Q8C008; baseline and differential.
DR Genevisible; Q8C008; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042462; P:eye photoreceptor cell development; IBA:GO_Central.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR025874; DZR.
DR InterPro; IPR026876; Fn3_assoc_repeat.
DR PANTHER; PTHR16058; DOUBLE ZINC RIBBON AND ANKYRIN REPEAT-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR16058:SF4; DOUBLE ZINC RIBBON AND ANKYRIN REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF12773; DZR; 2.
DR Pfam; PF13287; Fn3_assoc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..778
FT /note="Double zinc ribbon and ankyrin repeat-containing
FT protein 1"
FT /id="PRO_0000235912"
FT REPEAT 631..662
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 666..695
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT ZN_FING 230..289
FT /note="DZANK-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 359..407
FT /note="DZANK-type 2"
FT /evidence="ECO:0000255"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVP4"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT CONFLICT 202
FT /note="P -> H (in Ref. 1; BAC27960)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="I -> N (in Ref. 1; BAC27747)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="L -> Q (in Ref. 1; BAC27747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 85025 MW; 1A3EDB966EC74AED CRC64;
MTAGSVCAPQ IIPLRVPQPG KANHEIDTNT LLEMKSDTPD VNIYYTLDGS KPDFLKKVGS
GENNTFKYVK PITLPDGKIQ VKAVAVSKDC RQSGIVTKVF QVDYEPPKMV SSEDNVEDAL
KGFSKQELKN GFVGPKLRKK YKNAENKSTW NVNLRRLADL KVGERADPKT LKDLRFAESP
LEIPAYHEGA SARLPTHQAQ SPGFAHITGQ KSLTSTEIMR IQRETDFLKC AHCLASRPSD
PFARFCHECG APVPPIFGYR LPPPEGAQMG LCAECGSMVP MNTPICVVCE APLAPQLRPQ
ASLYLKERVI CRTCGTGNPA HLRYCVTCEG PLPPTQEQWL CNGDEVPHPP ARNGETISCS
RCGCQNLWEA SFCDWCGAML GISASHSVCP KCGASNHLTA RFCGSCGIYV KSITRFRMHN
SLAIVAGAPR PFPEPRSAWQ SLNVPLPTSA SGSKKDTGTQ TSGLFYPSGK LLAKKELEAA
SHRQRQEKMS DHRPVLTAVS PGRGYWRKQL DHISAHLRSY AQNNPEFRAL IAEPRMGKLI
SATVHEDGYE VSIRLNYIQV SNKSLYFNKS VNLSDHFLSS VTEGGNGLYD SRSSLVSAYS
QSVSDTPESI KKMKNLKAKS FLVNPEPLTP ENKLLLEEVG SSGKGRLSVL EQLLDEGADP
NCCDSQGRPA VIVAVVNKHY EAIPVLAQRG ADIDQQWGPF RNTALHEATL LGLEGRESIA
TLLGCNANAQ KKNTRGQTAY DIALEMGDDL TSSLFAAKFT QGLEDQLSPP GNRILGDS
//
