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
//