ID ANR26_MOUSE Reviewed; 1581 AA.
AC Q811D2; Q69ZS2; Q9CS61;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Ankyrin repeat domain-containing protein 26;
GN Name=Ankrd26; Synonyms=Kiaa1074;
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] OF 1-729, AND VARIANTS ASN-114;
RP ALA-142 AND ILE-218.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-528, AND VARIANTS HIS-399 AND
RP SER-450.
RC STRAIN=C57BL/6J; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1581.
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [4]
RP IDENTIFICATION.
RX PubMed=16364570; DOI=10.1016/j.gene.2005.07.045;
RA Hahn Y., Bera T.K., Pastan I.H., Lee B.;
RT "Duplication and extensive remodeling shaped POTE family genes encoding
RT proteins containing ankyrin repeat and coiled coil domains.";
RL Gene 366:238-245(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18162531; DOI=10.1073/pnas.0710978105;
RA Bera T.K., Liu X.F., Yamada M., Gavrilova O., Mezey E., Tessarollo L.,
RA Anver M., Hahn Y., Lee B., Pastan I.;
RT "A model for obesity and gigantism due to disruption of the Ankrd26 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:270-275(2008).
RN [7]
RP FUNCTION.
RX PubMed=22666460; DOI=10.1371/journal.pone.0038130;
RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.;
RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate
RT adipogenesis in 3T3-L1 cells.";
RL PLoS ONE 7:E38130-E38130(2012).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24633808; DOI=10.1007/s00429-014-0741-9;
RA Acs P., Bauer P.O., Mayer B., Bera T., Macallister R., Mezey E., Pastan I.;
RT "A novel form of ciliopathy underlies hyperphagia and obesity in Ankrd26
RT knockout mice.";
RL Brain Struct. Funct. 220:1511-1528(2015).
CC -!- FUNCTION: Acts as a regulator of adipogenesis. Involved in the
CC regulation of the feeding behavior. {ECO:0000269|PubMed:22666460,
CC ECO:0000269|PubMed:24633808}.
CC -!- SUBUNIT: Interacts with TRIO. Interacts with GPS2. Interacts with
CC CCDC85B. Interacts with HMMR. {ECO:0000250|UniProtKB:Q9UPS8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18162531}.
CC Note=Located just near the plasma membrane in close association with
CC filamentous actin. {ECO:0000269|PubMed:18162531}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:18162531). Expressed in
CC the arcuate and ventromedial nuclei within the hypothalamus and in the
CC ependyma and the circumventricular organs (at protein level)
CC (PubMed:18162531). {ECO:0000269|PubMed:18162531,
CC ECO:0000269|PubMed:24633808}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display hyperphagia, severe
CC obesity, gigantism, insulin resistance and elevated serum leptin levels
CC potentially linked to defects in primary cilia (PubMed:18162531,
CC PubMed:24633808). {ECO:0000269|PubMed:18162531,
CC ECO:0000269|PubMed:24633808}.
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DR EMBL; BC047067; AAH47067.1; ALT_SEQ; mRNA.
DR EMBL; AK017783; BAB30930.1; -; mRNA.
DR EMBL; AK173096; BAD32374.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q811D2; -.
DR SMR; Q811D2; -.
DR STRING; 10090.ENSMUSP00000108449; -.
DR iPTMnet; Q811D2; -.
DR PhosphoSitePlus; Q811D2; -.
DR MaxQB; Q811D2; -.
DR PaxDb; 10090-ENSMUSP00000108449; -.
DR ProteomicsDB; 282119; -.
DR AGR; MGI:1917887; -.
DR MGI; MGI:1917887; Ankrd26.
DR eggNOG; ENOG502QR0R; Eukaryota.
DR InParanoid; Q811D2; -.
DR PhylomeDB; Q811D2; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR ChiTaRS; Ankrd26; mouse.
DR PRO; PR:Q811D2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q811D2; Protein.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:MGI.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:MGI.
DR GO; GO:0035265; P:organ growth; IMP:MGI.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI.
DR GO; GO:0060259; P:regulation of feeding behavior; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR039497; CC144C-like_CC_dom.
DR InterPro; IPR021885; DUF3496.
DR PANTHER; PTHR24147; ANKYRIN REPEAT DOMAIN 36-RELATED; 1.
DR PANTHER; PTHR24147:SF60; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 26-RELATED; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF14915; CCDC144C; 2.
DR Pfam; PF12001; DUF3496; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW ANK repeat; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1581
FT /note="Ankyrin repeat domain-containing protein 26"
FT /id="PRO_0000240844"
FT REPEAT 46..76
FT /note="ANK 1"
FT REPEAT 80..109
FT /note="ANK 2"
FT REPEAT 113..142
FT /note="ANK 3"
FT REPEAT 146..175
FT /note="ANK 4"
FT REPEAT 179..208
FT /note="ANK 5"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 715..845
FT /evidence="ECO:0000255"
FT COILED 876..1345
FT /evidence="ECO:0000255"
FT COILED 1396..1470
FT /evidence="ECO:0000255"
FT COILED 1521..1550
FT /evidence="ECO:0000255"
FT COMPBIAS 230..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS8"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS8"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS8"
FT VARIANT 114
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 142
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 218
FT /note="M -> I"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 399
FT /note="D -> H"
FT /evidence="ECO:0000269|PubMed:16141072"
FT VARIANT 450
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:16141072"
FT CONFLICT 469
FT /note="M -> MGMEKN (in Ref. 2; BAB30930)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="V -> A (in Ref. 2; BAB30930)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="K -> R (in Ref. 2; BAB30930)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="A -> V (in Ref. 1; AAH47067)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="A -> T (in Ref. 1; AAH47067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1581 AA; 180647 MW; 6C298F79B3731DC9 CRC64;
MKKIFGFRSK GPSPLGPSAR PRSNCVGFGR ESASGSHVPR YHIHDKDMGK IHKAASVGDV
AKVQHILILG KSGVNDRDKK DRTALHLACA YGHPEVVTLL VERKCEIDAR DSESSTALIK
AVQCQEEECA AILLDHGADP NVMDSSGNTA LHYAVYSENT SMAAKLLAHN ANIEAKNKDD
LTPMLLAVKE NKQHIVEFLV KKKASIHAVD QLGSNRQMFE YDGKRLQRSE NSNPVDNGSE
DGSLTRSYNT PGPADSWPTS DEEDYNFDNK NVPKINLTEL WTAAQQSRKN QTKCGFEELD
NGARFDDSDS PSESEDAIEV EPAPSVRVQT LSPSRQSPDP VEGATELAIE GEENGTDVIE
SASQEQPNHD NLTRADGWHK SNKSEMMSAL GLGEDEDEDS PWDSESISES VSLKDVGHFS
GTADQTGKRR AHGQIEDVTY IPSCMSGSRN FKMAKLEESR NVGLPVAHME APRKYVIMEP
TIERRAPVLN KTETVGMTDA QTFKSEPESV SREEQTRLSG SEDSQQKVEE KRKYKNNEAE
PSGNLYSGAA DGGADVKPQS GDTENQQSPR EGSEGRGSGP ALLMKEAKKM ENEKWVSREP
ARTAMSERTG LPTGGWPQMQ DGSCWSDTDQ SEARPTKKTS SKHNKDSGQT AAVDNLDDFT
ESSETASEDH ELQGPDSESI LCAIEHLRLE CKDTASLLKI RDAVYSYKRL IELKRSHCEL
LTGKLKRMEN KYKGLQKEMS ETEEVKSRLE HEKVGWEQEL CRLRFALKQE EEKRRSADQL
SEKTMEQLRR KGEQCQSEVE ARQQLEASLR TLEMELKTVK SHLNQVLEER NETQRQLSRE
QNARMLQDGI LASHLCKQKE IEMTQKKMTS EVSVSHEKEK DLLHKNQRLQ DEVAVLRLEM
DTIKSHNQEK EKRYLEDIKI ANEKNDNLQR MVKLNMLSSK LDNEKQNKER LETDVESFRS
RLASALHDHA EIQTAKRDLE IAFQRARDEW FRVKDKMNFD MSNLRDNNEV LSQQLSKTER
KLNSLEIEFH HTKDELREKT LALKHAQRDL SQTQCQMKEV EHMFQDEQGK VSKFMGKQES
IEERLAQLQS ENTLLRQQLD DAANKAESKD KTIVNIQDQF QDVLTRFQAE SQRHSLRLED
RNQELVSECS HLRERLCQYE NEKAEREVVV RQLQQELADT LKKQSMSEAS LEVSSRYRSN
LEEEARDLKK KLGQLRSQLQ EARDQHREAV HHAEKMEDHL QKLELEKSKF EITIKKQSEE
IDQLQENLSR VNLSEEDKEK LQKLTELKES LECTVDQEQK RSSALEKELM RTIQKKCGKL
EKNKKQLEQE VVNLRSHMEK NMVEHSQAQQ YAREVEERAR QDLVEKLKQV NLFLQAQAAS
QESLEQLREN SNASVRSQME LRIKDLESQL YRMKAQEDFD KIELEKYKQL YQEEFRARKS
LSSKLNKTSE KLEEASSKLL LEEQQNRSLL STLSTRPVVE CPCVGSLHNS LVFNRTLIPR
ENIVVPTSGL QPSNKRVEIY LTKMHQELEK SINRELKEAT AELESEFCRV SPLGSATKAS
QDQLSDASQE FIDILKKKYM I
//
