ADDG_HUMAN
ID ADDG_HUMAN Reviewed; 706 AA.
AC Q9UEY8; D3DRA8; O43243; Q5VU09; Q92773; Q9UEY7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Gamma-adducin;
DE AltName: Full=Adducin-like protein 70;
GN Name=ADD3; Synonyms=ADDL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8893809; DOI=10.1159/000134389;
RA Katagiri T., Ozaki K., Fujiwara T., Shimizu F., Kawai A., Okuno S.,
RA Suzuki M., Nakamura Y., Takahashi E., Hirai Y.;
RT "Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a
RT human cDNA highly homologous to human erythrocyte adducin.";
RL Cytogenet. Cell Genet. 74:90-95(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Moorthy S., Bennett V.;
RT "Cloning in the gamma quadrant.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=10581174; DOI=10.1006/bbrc.1999.1769;
RA Citterio L., Azzani T., Duga S., Bianchi G.;
RT "Genomic organization of the human gamma adducin gene.";
RL Biochem. Biophys. Res. Commun. 266:110-114(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
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 [8]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-423; SER-442;
RP SER-673; SER-677 AND SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-423 AND SER-681, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-42; SER-673 AND SER-677, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-681, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP INVOLVEMENT IN CPSQ3, VARIANT CPSQ3 ASP-367, CHARACTERIZATION OF VARIANT
RP CPSQ3 ASP-367, AND FUNCTION.
RX PubMed=23836506; DOI=10.1002/ana.23971;
RA Kruer M.C., Jepperson T., Dutta S., Steiner R.D., Cottenie E., Sanford L.,
RA Merkens M., Russman B.S., Blasco P.A., Fan G., Pollock J., Green S.,
RA Woltjer R.L., Mooney C., Kretzschmar D., Paisan-Ruiz C., Houlden H.;
RT "Mutations in gamma adducin are associated with inherited cerebral palsy.";
RL Ann. Neurol. 74:805-814(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-64; SER-442; SER-461;
RP SER-673; SER-677; SER-681 AND SER-683, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-484, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes the
CC assembly of the spectrin-actin network. Plays a role in actin filament
CC capping (PubMed:23836506). Binds to calmodulin.
CC {ECO:0000269|PubMed:23836506}.
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=Q9UEY8-1; Sequence=Displayed;
CC Name=1; Synonyms=Short;
CC IsoId=Q9UEY8-2; Sequence=VSP_000188;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed.
CC {ECO:0000269|PubMed:8893809}.
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:0000269|PubMed:15561718}.
CC -!- DISEASE: Cerebral palsy, spastic quadriplegic 3 (CPSQ3) [MIM:617008]: A
CC form of cerebral palsy, a group of non-progressive disorders of
CC movement and/or posture resulting from defects in the developing
CC central nervous system. CPSQ3 is an autosomal recessive
CC neurodevelopmental disorder characterized by variable spasticity and
CC cognitive impairment. {ECO:0000269|PubMed:23836506}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ADD3ID520ch10q25.html";
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; D67031; BAA23783.1; -; mRNA.
DR EMBL; U37122; AAB17126.1; -; mRNA.
DR EMBL; Y14372; CAB51805.1; -; Genomic_DNA.
DR EMBL; Y14373; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14374; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14375; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14376; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14377; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14378; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14379; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14380; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14381; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14382; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14383; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14384; CAB51805.1; JOINED; Genomic_DNA.
DR EMBL; Y14372; CAB51806.1; -; Genomic_DNA.
DR EMBL; Y14373; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14374; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14375; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14376; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14377; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14378; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14379; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14380; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14381; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14382; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; Y14384; CAB51806.1; JOINED; Genomic_DNA.
DR EMBL; BX647403; CAI46048.1; -; mRNA.
DR EMBL; AL590628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49573.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49574.1; -; Genomic_DNA.
DR EMBL; BC062559; AAH62559.1; -; mRNA.
DR CCDS; CCDS7561.1; -. [Q9UEY8-1]
DR CCDS; CCDS7562.1; -. [Q9UEY8-2]
DR PIR; JC7164; JC7164.
DR RefSeq; NP_001112.2; NM_001121.3. [Q9UEY8-2]
DR RefSeq; NP_001307520.1; NM_001320591.1. [Q9UEY8-1]
DR RefSeq; NP_001307521.1; NM_001320592.1. [Q9UEY8-1]
DR RefSeq; NP_001307522.1; NM_001320593.1. [Q9UEY8-1]
DR RefSeq; NP_001307523.1; NM_001320594.1.
DR RefSeq; NP_058432.1; NM_016824.4. [Q9UEY8-1]
DR RefSeq; NP_063968.1; NM_019903.4. [Q9UEY8-2]
DR AlphaFoldDB; Q9UEY8; -.
DR SMR; Q9UEY8; -.
DR BioGRID; 106633; 129.
DR IntAct; Q9UEY8; 49.
DR MINT; Q9UEY8; -.
DR STRING; 9606.ENSP00000348381; -.
DR GlyGen; Q9UEY8; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9UEY8; -.
DR MetOSite; Q9UEY8; -.
DR PhosphoSitePlus; Q9UEY8; -.
DR BioMuta; ADD3; -.
DR DMDM; 12643881; -.
DR EPD; Q9UEY8; -.
DR jPOST; Q9UEY8; -.
DR MassIVE; Q9UEY8; -.
DR MaxQB; Q9UEY8; -.
DR PaxDb; Q9UEY8; -.
DR PeptideAtlas; Q9UEY8; -.
DR PRIDE; Q9UEY8; -.
DR ProteomicsDB; 84160; -. [Q9UEY8-1]
DR ProteomicsDB; 84161; -. [Q9UEY8-2]
DR Antibodypedia; 4067; 205 antibodies from 31 providers.
DR DNASU; 120; -.
DR Ensembl; ENST00000277900.12; ENSP00000277900.8; ENSG00000148700.15. [Q9UEY8-2]
DR Ensembl; ENST00000356080.9; ENSP00000348381.4; ENSG00000148700.15. [Q9UEY8-1]
DR Ensembl; ENST00000360162.7; ENSP00000353286.3; ENSG00000148700.15. [Q9UEY8-2]
DR GeneID; 120; -.
DR KEGG; hsa:120; -.
DR MANE-Select; ENST00000356080.9; ENSP00000348381.4; NM_016824.5; NP_058432.1.
DR UCSC; uc001kys.5; human. [Q9UEY8-1]
DR CTD; 120; -.
DR DisGeNET; 120; -.
DR GeneCards; ADD3; -.
DR HGNC; HGNC:245; ADD3.
DR HPA; ENSG00000148700; Low tissue specificity.
DR MalaCards; ADD3; -.
DR MIM; 601568; gene.
DR MIM; 617008; phenotype.
DR neXtProt; NX_Q9UEY8; -.
DR OpenTargets; ENSG00000148700; -.
DR Orphanet; 210141; Inherited congenital spastic tetraplegia.
DR PharmGKB; PA24567; -.
DR VEuPathDB; HostDB:ENSG00000148700; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000155257; -.
DR HOGENOM; CLU_006033_9_2_1; -.
DR InParanoid; Q9UEY8; -.
DR OMA; SFMSMEV; -.
DR PhylomeDB; Q9UEY8; -.
DR TreeFam; TF313003; -.
DR PathwayCommons; Q9UEY8; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9UEY8; -.
DR SIGNOR; Q9UEY8; -.
DR BioGRID-ORCS; 120; 12 hits in 1085 CRISPR screens.
DR ChiTaRS; ADD3; human.
DR GeneWiki; ADD3; -.
DR GenomeRNAi; 120; -.
DR Pharos; Q9UEY8; Tbio.
DR PRO; PR:Q9UEY8; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UEY8; protein.
DR Bgee; ENSG00000148700; Expressed in secondary oocyte and 211 other tissues.
DR ExpressionAtlas; Q9UEY8; baseline and differential.
DR Genevisible; Q9UEY8; HS.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
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; Disease variant; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT CHAIN 2..706
FT /note="Gamma-adducin"
FT /id="PRO_0000218536"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB5"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB5"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB5"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB5"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 484
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 576..607
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:8893809, ECO:0000303|Ref.2"
FT /id="VSP_000188"
FT VARIANT 367
FT /note="G -> D (in CPSQ3; decreased actin capping activity;
FT increased fibroblast proliferation and migration; decreased
FT colocalization with alpha subunit ADD1; dbSNP:rs564185858)"
FT /evidence="ECO:0000269|PubMed:23836506"
FT /id="VAR_076996"
FT CONFLICT 49..50
FT /note="FN -> SS (in Ref. 1; BAA23783)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="Q -> R (in Ref. 1; BAA23783)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="Q -> P (in Ref. 2; AAB17126)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="V -> M (in Ref. 2; AAB17126)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="P -> L (in Ref. 1; BAA23783)"
FT /evidence="ECO:0000305"
FT CONFLICT 426..433
FT /note="KYMAQRQQ -> QIHGTRGNK (in Ref. 2; AAB17126)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="K -> Q (in Ref. 2; AAB17126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 79155 MW; EB8EAF602A4D7B41 CRC64;
MSSDASQGVI TTPPPPSMPH KERYFDRINE NDPEYIRERN MSPDLRQDFN MMEQRKRVTQ
ILQSPAFRED LECLIQEQMK KGHNPTGLLA LQQIADYIMA NSFSGFSSPP LSLGMVTPIN
DLPGADTSSY VKGEKLTRCK LASLYRLVDL FGWAHLANTY ISVRISKEQD HIIIIPRGLS
FSEATASNLV KVNIIGEVVD QGSTNLKIDH TGFSPHAAIY STRPDVKCVI HIHTLATAAV
SSMKCGILPI SQESLLLGDV AYYDYQGSLE EQEERIQLQK VLGPSCKVLV LRNHGVVALG
ETLEEAFHYI FNVQLACEIQ VQALAGAGGV DNLHVLDFQK YKAFTYTVAA SGGGGVNMGS
HQKWKVGEIE FEGLMRTLDN LGYRTGYAYR HPLIREKPRH KSDVEIPATV TAFSFEDDTV
PLSPLKYMAQ RQQREKTRWL NSPNTYMKVN VPEESRNGET SPRTKITWMK AEDSSKVSGG
TPIKIEDPNQ FVPLNTNPNE VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMQF
EDDDHGPPAP PNPFSHLTEG ELEEYKRTIE RKQQGLEDAE QELLSDDASS VSQIQSQTQS
PQNVPEKLEE NHELFSKSFI SMEVPVMVVN GKDDMHDVED ELAKRVSRLS TSTTIENIEI
TIKSPEKIEE VLSPEGSPSK SPSKKKKKFR TPSFLKKNKK KEKVEA
