ANKS6_MOUSE
ID ANKS6_MOUSE Reviewed; 883 AA.
AC Q6GQX6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 6;
DE AltName: Full=SamCystin;
DE AltName: Full=Sterile alpha motif domain-containing protein 6;
DE Short=SAM domain-containing protein 6;
GN Name=Anks6; Synonyms=Gm635, Samd6;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-815.
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 IDENTIFICATION BY 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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23793029; DOI=10.1038/ng.2681;
RA Hoff S., Halbritter J., Epting D., Frank V., Nguyen T.M., van Reeuwijk J.,
RA Boehlke C., Schell C., Yasunaga T., Helmstadter M., Mergen M., Filhol E.,
RA Boldt K., Horn N., Ueffing M., Otto E.A., Eisenberger T., Elting M.W.,
RA van Wijk J.A., Bockenhauer D., Sebire N.J., Rittig S., Vyberg M., Ring T.,
RA Pohl M., Pape L., Neuhaus T.J., Elshakhs N.A., Koon S.J., Harris P.C.,
RA Grahammer F., Huber T.B., Kuehn E.W., Kramer-Zucker A., Bolz H.J.,
RA Roepman R., Saunier S., Walz G., Hildebrandt F., Bergmann C.,
RA Lienkamp S.S.;
RT "ANKS6 is a central component of a nephronophthisis module linking NEK8 to
RT INVS and NPHP3.";
RL Nat. Genet. 45:951-956(2013).
RN [5]
RP INTERACTION WITH ANKS3.
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 [6]
RP INTERACTION WITH ANKS3, AND TISSUE 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: Required for renal function. {ECO:0000250|UniProtKB:Q68DC2}.
CC -!- SUBUNIT: Homooligomer (By similarity). Central component of a complex
CC containing at least ANKS6, INVS, NEK8 and NPHP3 (By similarity). ANKS6
CC may organize complex assembly by linking INVS and NPHP3 to NEK8 and
CC INVS may target the complex to the proximal ciliary axoneme (By
CC similarity). Interacts (via SAM domain) with BICC1 (via KH domains) in
CC an RNA-dependent manner (By similarity). Interacts (via SAM domain)
CC with ANKS3 (via SAM domain) (PubMed:25671767, PubMed:26327442).
CC {ECO:0000250|UniProtKB:P0C0T2, ECO:0000269|PubMed:25671767,
CC ECO:0000269|PubMed:26327442}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:23793029}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0T2}. Note=Localizes to the proximal region
CC of the primary cilium in the presence of INVS.
CC {ECO:0000269|PubMed:23793029}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney (at protein level).
CC {ECO:0000269|PubMed:23793029, ECO:0000269|PubMed:26327442}.
CC -!- DOMAIN: The ankyrin repeats are necessary and sufficient for NEK8-
CC binding. {ECO:0000250|UniProtKB:P0C0T2}.
CC -!- PTM: Hydroxylated at Asn-129, most probably by HIF1AN. This
CC hydroxylation results in decreased NEK8-binding.
CC {ECO:0000250|UniProtKB:P0C0T2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72562.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL831741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC072562; AAH72562.1; ALT_INIT; mRNA.
DR CCDS; CCDS89741.1; -.
DR RefSeq; XP_006538395.1; XM_006538332.2.
DR AlphaFoldDB; Q6GQX6; -.
DR SMR; Q6GQX6; -.
DR BioGRID; 217674; 1.
DR CORUM; Q6GQX6; -.
DR IntAct; Q6GQX6; 1.
DR STRING; 10090.ENSMUSP00000103376; -.
DR iPTMnet; Q6GQX6; -.
DR PhosphoSitePlus; Q6GQX6; -.
DR MaxQB; Q6GQX6; -.
DR PaxDb; Q6GQX6; -.
DR PRIDE; Q6GQX6; -.
DR ProteomicsDB; 281987; -.
DR Antibodypedia; 1903; 121 antibodies from 17 providers.
DR Ensembl; ENSMUST00000229609; ENSMUSP00000155271; ENSMUSG00000066191.
DR MGI; MGI:1922941; Anks6.
DR VEuPathDB; HostDB:ENSMUSG00000066191; -.
DR eggNOG; KOG4369; Eukaryota.
DR GeneTree; ENSGT00940000157664; -.
DR InParanoid; Q6GQX6; -.
DR OrthoDB; 1137424at2759; -.
DR PhylomeDB; Q6GQX6; -.
DR BioGRID-ORCS; 75691; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q6GQX6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6GQX6; protein.
DR Bgee; ENSMUSG00000066191; Expressed in proximal tubule and 57 other tissues.
DR ExpressionAtlas; Q6GQX6; baseline and differential.
DR GO; GO:0097543; C:ciliary inversin compartment; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 7.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cell projection; Cilium; Cytoplasm; Hydroxylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..883
FT /note="Ankyrin repeat and SAM domain-containing protein 6"
FT /id="PRO_0000067066"
FT REPEAT 8..37
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 181..210
FT /note="ANK 5"
FT REPEAT 215..244
FT /note="ANK 6"
FT REPEAT 282..312
FT /note="ANK 7"
FT REPEAT 316..345
FT /note="ANK 8"
FT REPEAT 350..379
FT /note="ANK 9"
FT REPEAT 383..414
FT /note="ANK 10"
FT DOMAIN 771..834
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 821
FT /note="Essential for ANKS3 interaction"
FT /evidence="ECO:0000250|UniProtKB:P0C0T2"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DC2"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DC2"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DC2"
SQ SEQUENCE 883 AA; 93474 MW; 424B3DBC30966A91 CRC64;
MGEGALAPGL QLLLRACEQG DTDTARRLLE PGADPVAGPE AGAEPAGPEA VRAAEAGAPV
PVDCSDEAGN SALQLAAAGG HEPLVRFLLR RGASVNSRNH YGWSALMQAA RCGHVSVAHL
LLDHGADVNA QNRLGASVLT VASRGGHLGV VKLLLEAGAI VDHHTPSGES PATGGSGDEL
LGITALMAAV QHGHEAVVRL LMEWGADPNH TARTVGWSPL MLAALLGKLN VAQQLVEKGA
NPDHLSVLEK TAFEVALDRK YRDLAEYLDP LTTVRPKTDE EKRRPDIFYA LKMGNFQLVK
EIADEDPNHV NLVNGDGATP LMLAAVTGHL PLVQLLVEKH ADMDKQDSVH GWTALMQATY
HGNKEIVKYL LNQGADVALR AKNGYTAFDL VMLLNDPDTE LVRLLASVCM QVNKDRGRPS
HRPPLPHSKA RQPWSIPVLP DDKGGLKSWW SRMSNRFRKL KLMQTLPRGL AANQPLPFSD
EPELALDSTM RAPPQDRTSH LGPPEAAHAT KDSGPGNPRR EKGDVLLTTM LRNGAPFPRL
PSDKLKAVIP PFLPPSSFEL WSSDRSHTCH NGKADPTKTA LPPRASRAHP VGCVGTDGAT
SRPVKFPSIS RSPASPASSG SFNHSPHSSG GASGIGGMSR LGGELHSRSG GSVDSVLSQI
AAQRKKAAGL CEQKPRQQSS PVGPATSSSP PELPASLPSS GSGSSSGPSS SKKLDPSKRP
PSGTSATSKS TSPTLTPSPS PKGHTAESSV SSSSSHRQSK SSGGSSSGTI TDEDELTGIL
KKLSLEKYQP IFEEQEVDME AFLTLTDGDL QELGIKTDGS RQQILAAISE LNAGKGRERQ
ILQETIHNFH SSFESSASNT RAPGNGPSMA GWTRPEETVS SRR
