ADDG_MOUSE
ID ADDG_MOUSE Reviewed; 706 AA.
AC Q9QYB5; Q8JZT6; Q9D2M5; Q9QYB6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Gamma-adducin;
DE AltName: Full=Adducin-like protein 70;
GN Name=Add3; Synonyms=Addl;
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 [MRNA].
RX PubMed=10602987; DOI=10.1007/s003350010004;
RA Suriyapperuma S.P., Lozovatsky L., Ciciotte S.L., Peters L.L.,
RA Gilligan D.M.;
RT "The mouse adducin gene family: alternative splicing and chromosomal
RT localization.";
RL Mamm. Genome 11:16-23(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BTBR T+ tf/J;
RX PubMed=16682971; DOI=10.1038/ng1796;
RA Clee S.M., Yandell B.S., Schueler K.M., Rabaglia M.E., Richards O.C.,
RA Raines S.M., Kabara E.A., Klass D.M., Mui E.T.-K., Stapleton D.S.,
RA Gray-Keller M.P., Young M.B., Stoehr J.P., Lan H., Boronenkov I.,
RA Raess P.W., Flowers M.T., Attie A.D.;
RT "Positional cloning of Sorcs1, a type 2 diabetes quantitative trait
RT locus.";
RL Nat. Genet. 38:688-693(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-681, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-42; SER-64; SER-402;
RP SER-414; SER-423; SER-583; SER-585; SER-590; SER-673; SER-677; SER-679;
RP SER-681 AND SER-683, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes the
CC assembly of the spectrin-actin network. Plays a role in actin filament
CC capping. Binds to calmodulin. {ECO:0000250|UniProtKB:Q9UEY8}.
CC -!- SUBUNIT: Heterodimer of an alpha and a gamma subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=2; Synonyms=Long;
CC IsoId=Q9QYB5-1; Sequence=Displayed;
CC Name=1; Synonyms=Short;
CC IsoId=Q9QYB5-2; Sequence=VSP_000189;
CC -!- DOMAIN: Comprised of three regions: a N-terminal protease-resistant
CC globular head region, a short connecting subdomain, and a protease-
CC sensitive tail region.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF100424; AAF24974.1; -; mRNA.
DR EMBL; AF100425; AAF24975.1; -; mRNA.
DR EMBL; DQ479918; ABF48499.1; -; Genomic_DNA.
DR EMBL; AK019491; BAB31757.1; -; mRNA.
DR EMBL; AK028481; BAC25974.1; -; mRNA.
DR EMBL; CH466585; EDL01690.1; -; Genomic_DNA.
DR EMBL; BC037116; AAH37116.1; -; mRNA.
DR CCDS; CCDS29900.1; -. [Q9QYB5-1]
DR CCDS; CCDS50467.1; -. [Q9QYB5-2]
DR RefSeq; NP_001157571.1; NM_001164099.2. [Q9QYB5-1]
DR RefSeq; NP_001157572.1; NM_001164100.2. [Q9QYB5-2]
DR RefSeq; NP_001264029.1; NM_001277100.1. [Q9QYB5-1]
DR RefSeq; NP_038786.2; NM_013758.4. [Q9QYB5-1]
DR AlphaFoldDB; Q9QYB5; -.
DR SMR; Q9QYB5; -.
DR BioGRID; 205169; 5.
DR IntAct; Q9QYB5; 3.
DR MINT; Q9QYB5; -.
DR STRING; 10090.ENSMUSP00000107370; -.
DR iPTMnet; Q9QYB5; -.
DR PhosphoSitePlus; Q9QYB5; -.
DR EPD; Q9QYB5; -.
DR jPOST; Q9QYB5; -.
DR MaxQB; Q9QYB5; -.
DR PaxDb; Q9QYB5; -.
DR PeptideAtlas; Q9QYB5; -.
DR PRIDE; Q9QYB5; -.
DR ProteomicsDB; 296108; -. [Q9QYB5-1]
DR ProteomicsDB; 296109; -. [Q9QYB5-2]
DR Antibodypedia; 4067; 205 antibodies from 31 providers.
DR DNASU; 27360; -.
DR Ensembl; ENSMUST00000025999; ENSMUSP00000025999; ENSMUSG00000025026. [Q9QYB5-1]
DR Ensembl; ENSMUST00000050096; ENSMUSP00000052245; ENSMUSG00000025026. [Q9QYB5-2]
DR Ensembl; ENSMUST00000111741; ENSMUSP00000107370; ENSMUSG00000025026. [Q9QYB5-2]
DR Ensembl; ENSMUST00000235846; ENSMUSP00000157970; ENSMUSG00000025026. [Q9QYB5-2]
DR Ensembl; ENSMUST00000236296; ENSMUSP00000157697; ENSMUSG00000025026. [Q9QYB5-1]
DR Ensembl; ENSMUST00000237224; ENSMUSP00000158368; ENSMUSG00000025026. [Q9QYB5-2]
DR Ensembl; ENSMUST00000237301; ENSMUSP00000158149; ENSMUSG00000025026. [Q9QYB5-1]
DR Ensembl; ENSMUST00000237430; ENSMUSP00000157955; ENSMUSG00000025026. [Q9QYB5-1]
DR Ensembl; ENSMUST00000237832; ENSMUSP00000157432; ENSMUSG00000025026. [Q9QYB5-2]
DR Ensembl; ENSMUST00000238130; ENSMUSP00000158154; ENSMUSG00000025026. [Q9QYB5-2]
DR GeneID; 27360; -.
DR KEGG; mmu:27360; -.
DR UCSC; uc008hwi.3; mouse. [Q9QYB5-1]
DR CTD; 120; -.
DR MGI; MGI:1351615; Add3.
DR VEuPathDB; HostDB:ENSMUSG00000025026; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000155257; -.
DR HOGENOM; CLU_006033_9_2_1; -.
DR InParanoid; Q9QYB5; -.
DR OMA; SFMSMEV; -.
DR OrthoDB; 400524at2759; -.
DR PhylomeDB; Q9QYB5; -.
DR TreeFam; TF313003; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 27360; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Add3; mouse.
DR PRO; PR:Q9QYB5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9QYB5; protein.
DR Bgee; ENSMUSG00000025026; Expressed in gastrula and 257 other tissues.
DR ExpressionAtlas; Q9QYB5; baseline and differential.
DR Genevisible; Q9QYB5; MM.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027772; ADD3.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR PANTHER; PTHR10672:SF5; PTHR10672:SF5; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Calmodulin-binding;
KW Cell membrane; Cytoplasm; Cytoskeleton; Isopeptide bond; Membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
FT CHAIN 2..706
FT /note="Gamma-adducin"
FT /id="PRO_0000218537"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..701
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT COMPBIAS 585..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 484
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
FT VAR_SEQ 578..609
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_000189"
FT CONFLICT 37
FT /note="R -> G (in Ref. 3; BAB31757)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="T -> S (in Ref. 1; AAF24974/AAF24975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 78777 MW; 3866D14F33D262E4 CRC64;
MSSDTSPAVV TTPPPPSMPH KERYFDRINE SDPEYLRERN MSPDLRQDFN MMEQRKRVTQ
ILQSPAFRED LECLIQEQMK KGHNPSGLLA LQQIADYIVT SSFSGFSSPS LSLGMVTPIN
DLPGADTSSY VKGEKLTRCK LASLYRLADL FGWAHLANTY ISVRISKEQD HIIIIPRGLS
FSEATASTLV KVNIIGEVVD QGSTDLKIDH TGFSPHAAIY STRPDVKCVI HIHTLATAAV
SSMKCGILPI SQESLILGDV AYYDYQGSLD EEEERIELQK VLGPSCKVLV LRNHGMVALG
ETLEEAFHYI FNVQMACEIQ VQAVAGAGGV DNLLVLDLQK YKAFTHGVAM SGGGGVNMAS
HQKWKVGEIE FEGLMRTLDN LGYRTGYAYR HPLVREKPRH KSDVEIPATV TAFSFEDDSA
PLSPLKFMAQ RQQREKTRWL NSPNTYMKVN VPEESRNGET SPRTKITWMK AEDSSKVSSG
TPIKIEDPNQ FVPLNTNPTE VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMQF
DDDDQGPPAP PNPFSHLLEG ELEEYTKTIE RKQQGLDDAE QGSLSDDAAS VSQIQSQTQS
PQSVPERLEE NHELFSKSFT SMDAPVMIMN GKDEMHDVED ELAQRVSRLT TSTTIENIEI
TIKSPERTEE VLSPDGSPSK SPSKKKKKFR TPSFLKKNKK KEKVEA
