ANKY2_MOUSE
ID ANKY2_MOUSE Reviewed; 440 AA.
AC Q3TPE9; Q8BK14; Q8BYW5; Q8R3N4; Q921J1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ankyrin repeat and MYND domain-containing protein 2;
GN Name=Ankmy2;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
RN [4]
RP INTERACTION WITH GC1.
RX PubMed=21124868; DOI=10.1371/journal.pgen.1001199;
RA Jensen V.L., Bialas N.J., Bishop-Hurley S.L., Molday L.L., Kida K.,
RA Nguyen P.A., Blacque O.E., Molday R.S., Leroux M.R., Riddle D.L.;
RT "Localization of a guanylyl cyclase to chemosensory cilia requires the
RT novel ciliary MYND domain protein DAF-25.";
RL PLoS Genet. 6:E1001199-E1001199(2010).
CC -!- FUNCTION: May be involved in the trafficking of signaling proteins to
CC the cilia. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the retinal-specific guanylyl cyclase GC1.
CC {ECO:0000269|PubMed:21124868}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TPE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TPE9-2; Sequence=VSP_019937, VSP_019938;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29839.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK037644; BAC29839.1; ALT_FRAME; mRNA.
DR EMBL; AK077556; BAC36860.1; -; mRNA.
DR EMBL; AK164434; BAE37787.1; -; mRNA.
DR EMBL; BC012275; AAH12275.1; -; mRNA.
DR EMBL; BC024959; AAH24959.1; -; mRNA.
DR CCDS; CCDS25885.1; -. [Q3TPE9-1]
DR RefSeq; NP_666145.3; NM_146033.3. [Q3TPE9-1]
DR AlphaFoldDB; Q3TPE9; -.
DR SMR; Q3TPE9; -.
DR BioGRID; 229918; 5.
DR IntAct; Q3TPE9; 1.
DR STRING; 10090.ENSMUSP00000039484; -.
DR iPTMnet; Q3TPE9; -.
DR PhosphoSitePlus; Q3TPE9; -.
DR EPD; Q3TPE9; -.
DR MaxQB; Q3TPE9; -.
DR PaxDb; Q3TPE9; -.
DR PeptideAtlas; Q3TPE9; -.
DR PRIDE; Q3TPE9; -.
DR ProteomicsDB; 296247; -. [Q3TPE9-1]
DR ProteomicsDB; 296248; -. [Q3TPE9-2]
DR Antibodypedia; 43960; 193 antibodies from 19 providers.
DR DNASU; 217473; -.
DR Ensembl; ENSMUST00000041640; ENSMUSP00000039484; ENSMUSG00000036188. [Q3TPE9-1]
DR GeneID; 217473; -.
DR KEGG; mmu:217473; -.
DR UCSC; uc007njs.2; mouse. [Q3TPE9-2]
DR UCSC; uc007njt.2; mouse. [Q3TPE9-1]
DR CTD; 57037; -.
DR MGI; MGI:2144755; Ankmy2.
DR VEuPathDB; HostDB:ENSMUSG00000036188; -.
DR eggNOG; KOG1710; Eukaryota.
DR GeneTree; ENSGT00390000016820; -.
DR HOGENOM; CLU_048951_0_0_1; -.
DR InParanoid; Q3TPE9; -.
DR OMA; AFKYHYL; -.
DR OrthoDB; 1413951at2759; -.
DR PhylomeDB; Q3TPE9; -.
DR TreeFam; TF351374; -.
DR BioGRID-ORCS; 217473; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Ankmy2; mouse.
DR PRO; PR:Q3TPE9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q3TPE9; protein.
DR Bgee; ENSMUSG00000036188; Expressed in ascending aorta and 246 other tissues.
DR Genevisible; Q3TPE9; MM.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell projection; Cilium; Metal-binding;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Ankyrin repeat and MYND domain-containing protein 2"
FT /id="PRO_0000247167"
FT REPEAT 45..74
FT /note="ANK 1"
FT REPEAT 79..108
FT /note="ANK 2"
FT REPEAT 159..188
FT /note="ANK 3"
FT ZN_FING 320..357
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 371..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT VAR_SEQ 295..300
FT /note="GSDPTA -> VRLLFC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019937"
FT VAR_SEQ 301..440
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019938"
FT CONFLICT 156
FT /note="L -> Q (in Ref. 1; BAC36860)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="C -> G (in Ref. 2; AAH24959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 48774 MW; 8E9B74469A54EB7A CRC64;
MGHIKKGELT QEEKELLEVI GKGTVQEAGR LLSSKNVHVN CLDENGMTPL MHAAYKGKLE
MCKLLLRHGA DASCHQHEHG YTALMFAALS GNKDITWVML EAGAETDVVN SVGRTAAQMA
AFVGQHDCVA IINNFFPRER LDYYTKPQGL DKEPKLPPKL AGPLHKIITT TNLHPVKIVM
LVSENPLLAD AAALGKCYRV MDLICEKCMK QRDMNEVLAM KMHYISCIFQ KCITFLKEGE
NKLDTLIRSL LKGRASDGFP VYQEKIIRES IRKFPYCEAT LLQQLVRSIA PVEIGSDPTA
FSVLTQAITG QVGFVDVEFC TTCGEKGASK RCSVCKMVIY CDQTCQKTHW FAHKKMCKSL
KDVYEKQQIE AAKHKRQEEK NGNPNVSSNH VNEDQPEAEE GITQENSIPS DSVEGEKEAA
NDTGLASAQD APTGPQLSEE
