ADDG_RAT
ID ADDG_RAT Reviewed; 705 AA.
AC Q62847;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Gamma-adducin;
DE AltName: Full=Adducin-like protein 70;
DE AltName: Full=Protein kinase C-binding protein 35H;
GN Name=Add3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, AND INTERACTION WITH ADD1.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=7592723; DOI=10.1074/jbc.270.43.25534;
RA Dong L., Chapline C., Mousseau B., Fowler L., Ramsay K., Stevens J.L.,
RA Jaken S.;
RT "35H, a sequence isolated as a protein kinase C binding protein, is a novel
RT member of the adducin family.";
RL J. Biol. Chem. 270:25534-25540(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Milan;
RX PubMed=9299427; DOI=10.1006/bbrc.1997.7173;
RA Tripodi G., Szpirer C., Reina C., Szpirer J., Bianchi G.;
RT "Polymorphism of gamma-adducin gene in genetic hypertension and mapping of
RT the gene to rat chromosome 1q55.";
RL Biochem. Biophys. Res. Commun. 237:685-689(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-583; SER-585;
RP SER-672; SER-676 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 {ECO:0000269|PubMed:7592723}.
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=Q62847-1; Sequence=Displayed;
CC Name=1; Synonyms=Short;
CC IsoId=Q62847-2; Sequence=VSP_000190;
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}.
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; U35775; AAC52277.1; -; mRNA.
DR RefSeq; NP_001157575.1; NM_001164103.1.
DR RefSeq; NP_113740.2; NM_031552.2.
DR AlphaFoldDB; Q62847; -.
DR SMR; Q62847; -.
DR BioGRID; 247271; 1.
DR STRING; 10116.ENSRNOP00000043399; -.
DR iPTMnet; Q62847; -.
DR PhosphoSitePlus; Q62847; -.
DR jPOST; Q62847; -.
DR PaxDb; Q62847; -.
DR PRIDE; Q62847; -.
DR GeneID; 25230; -.
DR KEGG; rno:25230; -.
DR CTD; 120; -.
DR RGD; 2043; Add3.
DR eggNOG; KOG3699; Eukaryota.
DR InParanoid; Q62847; -.
DR OrthoDB; 400524at2759; -.
DR PhylomeDB; Q62847; -.
DR Reactome; R-RNO-5223345; Miscellaneous transport and binding events.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q62847; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
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..705
FT /note="Gamma-adducin"
FT /id="PRO_0000218538"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..700
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 682..696
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:0000250|UniProtKB:Q9QYB5"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
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:22673903"
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:22673903"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB5"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB5"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 682
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q9UEY8"
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:0000303|PubMed:7592723"
FT /id="VSP_000190"
FT VARIANT 572
FT /note="Q -> K (in strain: Milan hypersensitive)"
FT CONFLICT 701..705
FT /note="EKVEA -> GES (in Ref. 1; AAC52277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 705 AA; 78804 MW; E8448431AD2E436B CRC64;
MSSDSSQAVI TTPPPPSMPH KERYFDRINE SDPEYLRERN MSPDLREDFN MMEQRKRVTQ
ILQSPAFRED LECLTQEQMK KGHDPTGLLA LQQIADYIMA NSFTGFSSPP LSLGMVTPIN
DLPGADTSSY VKGEKLTRCE LASLYRLADL FGWAHLANTY ISVRVSKEQD HIIIIPRGLP
FSEATASALV KVNIIGEVVD QGSTNLKIDH SGFSPHAAIY STRPDVKCVI HIHTLATAAV
SSMKCGILPI SQESLILGDV AYYDYQGSLD EEEERIELQK VLGPSCKVLV LRNHGVVALG
ETLEEAFHYI FNVQMACEIQ VQAVAGAGGV DNLLILDLQK YKAFTHGVAM TGGGGVNMGS
HQKWKVGEIE FEGLMRTLDN LGYRTGYAYR HPLVREKPRH KSDVEIPATV TAFSFEDDSV
PLSPLKYMAQ RQQREKTRWL NSPNTYMKVN VPEESRNGET SPRTKITWMK AEDPSKVSSG
TPIKIEDPNQ FVPLNTNPTE VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMRF
EDDDQGPPAP PNPFSHLMEG ELEEYTKTIE RQQQGLDDAE QESLSDDAAS VSQIQSQTQS
PQSVPERLEE NHELFSKSFT SVDVPVIVNG KDEMHDVEDE LAQRVSRLTT STTIENIEIT
IKSPDRTEEV LSPDGSPSKS PSKKKKKFRT PSFLKKNKKK EKVEA
