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Ankyrin repeat and SAM domain-containing protein 6 (Polycystic kidney disease protein 1) (SamCystin) (Sterile alpha motif domain-containing protein 6) (SAM domain-containing protein 6)

 ANKS6_RAT               Reviewed;         885 AA.
P0C0T2; Q2VWC0; Q5BJL2;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
14-NOV-2006, sequence version 2.
16-JAN-2019, entry version 93.
RecName: Full=Ankyrin repeat and SAM domain-containing protein 6;
AltName: Full=Polycystic kidney disease protein 1;
AltName: Full=SamCystin;
AltName: Full=Sterile alpha motif domain-containing protein 6;
Short=SAM domain-containing protein 6;
Name=Anks6; Synonyms=Pkdr1, Samd6;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT
IN CY, AND VARIANT CY TRP-823.
STRAIN=Brown Norway; TISSUE=Kidney;
PubMed=16207829; DOI=10.1681/ASN.2005060601;
Brown J.H., Bihoreau M.-T., Hoffmann S., Kranzlin B., Tychinskaya I.,
Obermuller N., Podlich D., Boehn S.N., Kaisaki P.J., Megel N.,
Danoy P., Copley R.R., Broxholme J., Witzgall R., Lathrop M.,
Gretz N., Gauguier D.;
"Missense mutation in sterile alpha motif of novel protein SamCystin
is associated with polycystic kidney disease in (cy/+) rat.";
J. Am. Soc. Nephrol. 16:3517-3526(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 864-885.
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH BICC1, DOMAIN, AND
CHARACTERIZATION OF VARIANT CY TRP-823.
PubMed=19324013; DOI=10.1016/j.bbrc.2009.03.113;
Stagner E.E., Bouvrette D.J., Cheng J., Bryda E.C.;
"The polycystic kidney disease-related proteins Bicc1 and SamCystin
interact.";
Biochem. Biophys. Res. Commun. 383:16-21(2009).
[5]
INTERACTION WITH INVS; NEK8 AND NPHP3, DOMAIN, HYDROXYLATION AT
ASN-129, AND MUTAGENESIS OF ASN-129; ASN-209 AND GLN-433.
PubMed=23793029; DOI=10.1038/ng.2681;
Hoff S., Halbritter J., Epting D., Frank V., Nguyen T.M.,
van Reeuwijk J., Boehlke C., Schell C., Yasunaga T., Helmstadter M.,
Mergen M., Filhol E., Boldt K., Horn N., Ueffing M., Otto E.A.,
Eisenberger T., Elting M.W., van Wijk J.A., Bockenhauer D.,
Sebire N.J., Rittig S., Vyberg M., Ring T., Pohl M., Pape L.,
Neuhaus T.J., Elshakhs N.A., Koon S.J., Harris P.C., Grahammer F.,
Huber T.B., Kuehn E.W., Kramer-Zucker A., Bolz H.J., Roepman R.,
Saunier S., Walz G., Hildebrandt F., Bergmann C., Lienkamp S.S.;
"ANKS6 is a central component of a nephronophthisis module linking
NEK8 to INVS and NPHP3.";
Nat. Genet. 45:951-956(2013).
[6]
INTERACTION WITH ANKS3.
PubMed=25671767; DOI=10.1038/ki.2015.17;
Yakulov T.A., Yasunaga T., Ramachandran H., Engel C., Mueller B.,
Hoff S., Dengjel J., Lienkamp S.S., Walz G.;
"Anks3 interacts with nephronophthisis proteins and is required for
normal renal development.";
Kidney Int. 87:1191-1200(2015).
-!- FUNCTION: Required for renal function.
{ECO:0000269|PubMed:16207829}.
-!- SUBUNIT: Homooligomer (PubMed:19324013). Central component of a
complex containing at least ANKS6, INVS, NEK8 and NPHP3. ANKS6 may
organize complex assembly by linking INVS and NPHP3 to NEK8 and
INVS may target the complex to the proximal ciliary axoneme
(PubMed:23793029). Interacts (via SAM domain) with BICC1 (via KH
domains) in an RNA-dependent manner (PubMed:19324013). Interacts
with ANKS3 (PubMed:25671767). {ECO:0000269|PubMed:19324013,
ECO:0000269|PubMed:23793029, ECO:0000269|PubMed:25671767}.
-!- SUBCELLULAR LOCATION: Cell projection, cilium
{ECO:0000250|UniProtKB:Q6GQX6}. Cytoplasm
{ECO:0000269|PubMed:19324013}. Note=Localizes to the proximal
region of the primary cilium in the presence of INVS.
{ECO:0000250|UniProtKB:Q6GQX6}.
-!- TISSUE SPECIFICITY: Widely expressed with moderate level in brain,
skeletal muscle and testis. Expressed in renal tubules.
{ECO:0000269|PubMed:16207829}.
-!- DOMAIN: The ankyrin repeats are necessary and sufficient for NEK8-
binding. {ECO:0000269|PubMed:23793029}.
-!- DOMAIN: The SAM domain mediates interaction with the SAM domain of
ANKS3. {ECO:0000269|PubMed:19324013}.
-!- PTM: Hydroxylated at Asn-129, most probably by HIF1AN. This
hydroxylation results in decreased NEK8-binding.
{ECO:0000269|PubMed:23793029}.
-!- DISEASE: Note=Defects in Anks6 are the cause of polycystic kidney
disease (cy). Heterozygous cy rats are characterized by
progressive formation and enlargement of cysts in kidneys.
{ECO:0000269|PubMed:16207829, ECO:0000269|PubMed:19324013}.
-!- SEQUENCE CAUTION:
Sequence=AAH91436.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY661303; AAT76432.1; -; mRNA.
EMBL; AABR03040311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC091436; AAH91436.1; ALT_SEQ; mRNA.
RefSeq; NP_001015028.2; NM_001015028.2.
UniGene; Rn.101322; -.
ProteinModelPortal; P0C0T2; -.
SMR; P0C0T2; -.
CORUM; P0C0T2; -.
STRING; 10116.ENSRNOP00000056754; -.
PaxDb; P0C0T2; -.
PRIDE; P0C0T2; -.
GeneID; 362515; -.
KEGG; rno:362515; -.
UCSC; RGD:3334; rat.
CTD; 203286; -.
RGD; 3334; Anks6.
eggNOG; KOG4369; Eukaryota.
eggNOG; KOG4374; Eukaryota.
eggNOG; COG0666; LUCA.
HOGENOM; HOG000231711; -.
HOVERGEN; HBG059049; -.
InParanoid; P0C0T2; -.
KO; K21415; -.
OrthoDB; 1137424at2759; -.
PhylomeDB; P0C0T2; -.
TreeFam; TF328552; -.
PRO; PR:P0C0T2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
CDD; cd00204; ANK; 3.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
Pfam; PF12796; Ank_2; 3.
Pfam; PF13606; Ank_3; 1.
Pfam; PF00536; SAM_1; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 10.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48403; SSF48403; 2.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 7.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
ANK repeat; Cell projection; Cilium; Complete proteome; Cytoplasm;
Disease mutation; Hydroxylation; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 885 Ankyrin repeat and SAM domain-containing
protein 6.
/FTId=PRO_0000067067.
REPEAT 8 37 ANK 1.
REPEAT 68 97 ANK 2.
REPEAT 101 130 ANK 3.
REPEAT 134 163 ANK 4.
REPEAT 181 210 ANK 5.
REPEAT 215 244 ANK 6.
REPEAT 282 312 ANK 7.
REPEAT 316 345 ANK 8.
REPEAT 350 379 ANK 9.
REPEAT 383 414 ANK 10.
DOMAIN 773 836 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
COMPBIAS 609 769 Ser-rich.
MOD_RES 129 129 3-hydroxyasparagine.
{ECO:0000269|PubMed:23793029}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000250|UniProtKB:Q68DC2}.
MOD_RES 734 734 Phosphoserine.
{ECO:0000250|UniProtKB:Q68DC2}.
MOD_RES 742 742 Phosphoserine.
{ECO:0000250|UniProtKB:Q68DC2}.
VARIANT 823 823 R -> W (in cy; loss of ability to self-
associate, does not affect interaction
with Bicc1).
{ECO:0000269|PubMed:16207829,
ECO:0000269|PubMed:19324013}.
MUTAGEN 129 129 N->A: Decreased NEK8-binding, but no
effect on INVS-binding; when associated
with A-209.
{ECO:0000269|PubMed:23793029}.
MUTAGEN 209 209 N->A: Decreased NEK8-binding, but no
effect on INVS-binding; when associated
with A-129.
{ECO:0000269|PubMed:23793029}.
MUTAGEN 433 433 Q->R: No effect on interaction with INVS,
NEK8 AND NPHP3, nor on ciliary
localization. Unable to rescue ANKS6
knockout in a heterologous system.
{ECO:0000269|PubMed:23793029}.
CONFLICT 870 870 C -> S (in Ref. 1; AAT76432 and 3;
AAH91436). {ECO:0000305}.
SEQUENCE 885 AA; 93809 MW; B4F91C5DFCD2D35E CRC64;
MGEGALAPGL QLLLRACEQG DTDTARRLLE PGGEPVAGSE AGAEPAGPEA ARAVEAGTPV
PVDCSDEAGN SALQLAAAGG HEPLVRFLLR RGASVNSRNH YGWSALMQAA RCGHASVAHL
LLDHGADVNA QNRLGASVLT VASRGGHLGV VKLLLEAGAT VDHRNPSGES TASGGSRDEL
LGITALMAAV QHGHEAVVRL LMEWGADPNH TARTVGWSPL MLAALLGKLS VVQQLVEKGA
NPDHLGVLEK TAFEVALDRK HRDLADYLDP LTTVRPKTDE EKRRPDIFHA LKMGNFQLVK
EIADEDPNHV NLVNGDGATP LMLAAVTGQL PLVQLLVEKH ADMNKQDSVH GWTALMQATY
HGNKEIVKYL LNQGADVTLR AKNGYTAFDL VMLLNDPDTE LVRLLASVCM QVNKDRGGRP
SHRPPLPHSK ARQPWSIPML PDDKGGLKSW WSRMSNRFRK LKLMQTLPRG LAANQPLPFS
DEPELALDST MRAPPQDRTN HLGPPEAAHA AKDSGPGNPR REKDDVLLTT MLRNGAPFPR
LPSDKLKAVI PPFLPPSSFE LWSSDRSRTC PNGKADPMKT VLPPRASRAH PVGCVGTDGA
AGRPVKFPSI SRSPTSPASS GNFNHSPHSS GGASGVGSMS RLGGELHNRS GGSVDSVLSQ
IAAQRKKAAG LCEQKPPCQQ SSPVGPATGS SPPELPASLL GSGSGSSNVT SSSKKLDPGK
RPPSGTSATS KSTSPTLTPS PSPKGHTAES SVSSSSSHRQ SKSSGGSSSG TITDEDELTG
ILKKLSLEKY QPIFEEQEVD MEAFLTLTDG DLQELGIKTD GSRQQILAAI SELNAGKGRE
RQILQETIHN FHSSFESSAS NTRAPGNSPC MAGWVRPEET VSSRR


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