ANKS3_MOUSE
ID ANKS3_MOUSE Reviewed; 655 AA.
AC Q9CZK6; Q6ZPF6; Q80X46;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 3;
GN Name=Anks3; Synonyms=Kiaa1977;
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;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-630.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [6]
RP INTERACTION WITH ANKS6; NEK7 AND NEK8, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION AT SER-5; SER-201; SER-225; SER-243; SER-244; SER-245;
RP THR-318; SER-319; SER-366; SER-369 AND SER-540, AND MUTAGENESIS OF SER-5;
RP SER-243; 318-THR-SER-319; SER-366 AND SER-369.
RX PubMed=26188091; DOI=10.1016/j.bbrc.2015.07.063;
RA Ramachandran H., Engel C., Mueller B., Dengjel J., Walz G., Yakulov T.A.;
RT "Anks3 alters the sub-cellular localization of the Nek7 kinase.";
RL Biochem. Biophys. Res. Commun. 464:901-907(2015).
RN [7]
RP INTERACTION WITH ANKS6; BICC1; NPHP1; NEK8 AND HIF1AN, HYDROXYLATION AT
RP ASN-96, AND MASS SPECTROMETRY.
RX PubMed=25671767; DOI=10.1038/ki.2015.17;
RA Yakulov T.A., Yasunaga T., Ramachandran H., Engel C., Mueller B., Hoff S.,
RA Dengjel J., Lienkamp S.S., Walz G.;
RT "Anks3 interacts with nephronophthisis proteins and is required for normal
RT renal development.";
RL Kidney Int. 87:1191-1200(2015).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ANKS6, AND TISSUE
RP SPECIFICITY.
RX PubMed=26327442; DOI=10.1371/journal.pone.0136781;
RA Delestre L., Bakey Z., Prado C., Hoffmann S., Bihoreau M.T., Lelongt B.,
RA Gauguier D.;
RT "ANKS3 Co-Localises with ANKS6 in Mouse Renal Cilia and Is Associated with
RT Vasopressin Signaling and Apoptosis In Vivo in Mice.";
RL PLoS ONE 10:E0136781-E0136781(2015).
CC -!- FUNCTION: May be involved in vasopressin signaling in the kidney.
CC {ECO:0000269|PubMed:26327442}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts (via SAM domain) with
CC ANKS6 (via SAM domain) (PubMed:25671767, PubMed:26327442,
CC PubMed:26188091). Interacts with BICC1 (PubMed:25671767). Interacts
CC with NPHP1 (PubMed:25671767). Interacts with NEK8 (PubMed:25671767,
CC PubMed:26188091). Interacts with HIF1AN (PubMed:25671767). Interacts
CC with NEK7; this interaction alters the subcellular distribution of NEK7
CC by preventing its nuclear translocation (PubMed:26188091).
CC {ECO:0000250|UniProtKB:Q6ZW76, ECO:0000269|PubMed:25671767,
CC ECO:0000269|PubMed:26188091, ECO:0000269|PubMed:26327442}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:26327442}. Cytoplasm {ECO:0000269|PubMed:26188091}.
CC -!- TISSUE SPECIFICITY: Kidney (at protein level).
CC {ECO:0000269|PubMed:26327442}.
CC -!- DOMAIN: The SAM domain mediates homooligomerization.
CC {ECO:0000250|UniProtKB:Q6ZW76}.
CC -!- PTM: Hydroxylated at Asn-96, most probably by HIF1AN.
CC {ECO:0000269|PubMed:25671767}.
CC -!- PTM: Phosphorylations at Ser-5, Ser-225, Thr-318, Ser-319, Ser-366 and
CC Ser-369 occur in a NEK7-dependent manner.
CC {ECO:0000269|PubMed:26327442}.
CC -!- PTM: Polyubiquitinated. {ECO:0000269|PubMed:26188091}.
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DR EMBL; AK012494; BAB28279.1; -; mRNA.
DR EMBL; BC050929; AAH50929.1; -; mRNA.
DR EMBL; AK129471; BAC98281.2; -; mRNA.
DR CCDS; CCDS27928.1; -.
DR RefSeq; NP_082577.2; NM_028301.4.
DR AlphaFoldDB; Q9CZK6; -.
DR SMR; Q9CZK6; -.
DR BioGRID; 215473; 3.
DR CORUM; Q9CZK6; -.
DR IntAct; Q9CZK6; 2.
DR STRING; 10090.ENSMUSP00000023157; -.
DR iPTMnet; Q9CZK6; -.
DR PhosphoSitePlus; Q9CZK6; -.
DR MaxQB; Q9CZK6; -.
DR PaxDb; Q9CZK6; -.
DR PRIDE; Q9CZK6; -.
DR ProteomicsDB; 281986; -.
DR Antibodypedia; 24396; 93 antibodies from 21 providers.
DR DNASU; 72615; -.
DR Ensembl; ENSMUST00000023157; ENSMUSP00000023157; ENSMUSG00000022515.
DR GeneID; 72615; -.
DR KEGG; mmu:72615; -.
DR UCSC; uc007ybb.2; mouse.
DR CTD; 124401; -.
DR MGI; MGI:1919865; Anks3.
DR VEuPathDB; HostDB:ENSMUSG00000022515; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000156610; -.
DR HOGENOM; CLU_014543_0_0_1; -.
DR InParanoid; Q9CZK6; -.
DR OMA; NKGHHSK; -.
DR OrthoDB; 58543at2759; -.
DR PhylomeDB; Q9CZK6; -.
DR TreeFam; TF331487; -.
DR BioGRID-ORCS; 72615; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Anks3; mouse.
DR PRO; PR:Q9CZK6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CZK6; protein.
DR Bgee; ENSMUSG00000022515; Expressed in retinal neural layer and 207 other tissues.
DR ExpressionAtlas; Q9CZK6; baseline and differential.
DR Genevisible; Q9CZK6; MM.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cell projection; Coiled coil; Cytoplasm; Hydroxylation;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..655
FT /note="Ankyrin repeat and SAM domain-containing protein 3"
FT /id="PRO_0000230778"
FT REPEAT 34..64
FT /note="ANK 1"
FT REPEAT 68..97
FT /note="ANK 2"
FT REPEAT 101..130
FT /note="ANK 3"
FT REPEAT 134..163
FT /note="ANK 4"
FT REPEAT 168..197
FT /note="ANK 5"
FT REPEAT 201..220
FT /note="ANK 6"
FT DOMAIN 424..487
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..421
FT /note="Interaction with NEK7"
FT /evidence="ECO:0000269|PubMed:26188091"
FT REGION 314..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 500..575
FT /evidence="ECO:0000255"
FT COMPBIAS 321..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M9H0"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 96
FT /note="3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:25671767"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26188091"
FT MUTAGEN 5
FT /note="S->A: No effect on its interaction with NEK7."
FT /evidence="ECO:0000269|PubMed:26188091"
FT MUTAGEN 243
FT /note="S->A: No effect on its interaction with NEK7."
FT /evidence="ECO:0000269|PubMed:26188091"
FT MUTAGEN 318..319
FT /note="TS->AA: No effect on its interaction with NEK7."
FT /evidence="ECO:0000269|PubMed:26188091"
FT MUTAGEN 366
FT /note="S->A: No effect on its interaction with NEK7."
FT /evidence="ECO:0000269|PubMed:26188091"
FT MUTAGEN 369
FT /note="S->A: No effect on its interaction with NEK7."
FT /evidence="ECO:0000269|PubMed:26188091"
FT CONFLICT 259
FT /note="R -> Q (in Ref. 3; BAC98281)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="R -> G (in Ref. 1; BAB28279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 72082 MW; A6B3043D5527FFF1 CRC64;
MSELSDEASE PELLKRSLSM WHGLGAQGSP EELDVPLDLH TAASIGQHEV VKECVQRGEL
DLNKKNGGGW TALMYASYIG HDTIVHLLLE AGVSVNVPTP EGQTPLMLAS SCGNESIAYF
LLQQGAELEM KDIHGWTALF HCTSAGHQQM VKFLLESGAN ANVREPVYGY TPLMEAAASG
HEIIVQYFLN HGVKVDTRDH SGATACMLAR QFGHMKIVAL METHSPVLPK SLYRSPEKYE
DLSSSDESWP VPQRQRPCRK KGLSIHEGPR ALAKITAIGL GGKTQTTYEQ VPPRGYVTFT
SSDENTMESE GLCYRDVTSP INEQDVESSS SSSREEPTFC ASLGPVWRSS SSDGLARAQG
LSSEASIESN EDSDHARKSS VRKQTRSYLK NKSRHGNSDG HWPSSTGPAS IPGSEPQTEK
SPYSGPQDLA TLLEQIGCLK YLQVFEEQDI DLRIFLTLTE SDLKEIGITL FGPKRKMTSA
IARWHSSARP PSDALELAYA DRLETEMQEL AIQLHKCCEE AEALRGQVSQ EQELRAVVES
CLLEQDSARK DIHAQLQEAQ TLAQDAALVL DQLRACQAEL SARLRQHHSP REGTPNPHFL
SADSKGWPIP LQALSLPELS GALEDRVHEM GQALCSVTQS LEKLQMLNAK KWREP
