ADDA_MOUSE
ID ADDA_MOUSE Reviewed; 735 AA.
AC Q9QYC0; Q9JLE3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Alpha-adducin;
DE AltName: Full=Erythrocyte adducin subunit alpha;
GN Name=Add1;
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], AND ALTERNATIVE SPLICING.
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=10845937;
RA Muro A.F., Marro M.L., Gajovic S., Porro F., Luzzatto L., Baralle F.E.;
RT "Mild spherocytic hereditary elliptocytosis and altered levels of
RT alpha- and gamma-adducins in beta-adducin-deficient mice.";
RL Blood 95:3978-3985(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-610, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-355; THR-358;
RP SER-364; SER-366; SER-408; SER-427; THR-429; SER-431; SER-436; SER-464;
RP SER-465; SER-586; SER-600; SER-605; THR-610; SER-613 AND THR-614,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-605; THR-610;
RP SER-613 AND THR-614 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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. Binds to calmodulin.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit or an alpha and a
CC 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=1;
CC IsoId=Q9QYC0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYC0-2; Sequence=VSP_000177, VSP_000178;
CC -!- DOMAIN: Each subunit is comprised of three regions: a NH2-terminal
CC protease-resistant globular head region, a short connecting subdomain,
CC and a protease-sensitive tail region.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF096839; AAF24971.1; -; mRNA.
DR EMBL; AF189771; AAF29504.1; -; mRNA.
DR CCDS; CCDS19216.1; -. [Q9QYC0-1]
DR CCDS; CCDS39069.1; -. [Q9QYC0-2]
DR RefSeq; NP_001019629.2; NM_001024458.4. [Q9QYC0-1]
DR RefSeq; NP_001095914.1; NM_001102444.2.
DR RefSeq; NP_001318009.1; NM_001331080.1. [Q9QYC0-1]
DR RefSeq; NP_001318016.1; NM_001331087.1. [Q9QYC0-2]
DR RefSeq; NP_038485.1; NM_013457.4. [Q9QYC0-2]
DR RefSeq; XP_017176104.1; XM_017320615.1. [Q9QYC0-2]
DR AlphaFoldDB; Q9QYC0; -.
DR SMR; Q9QYC0; -.
DR BioGRID; 197981; 17.
DR IntAct; Q9QYC0; 7.
DR MINT; Q9QYC0; -.
DR STRING; 10090.ENSMUSP00000109979; -.
DR iPTMnet; Q9QYC0; -.
DR PhosphoSitePlus; Q9QYC0; -.
DR SwissPalm; Q9QYC0; -.
DR EPD; Q9QYC0; -.
DR jPOST; Q9QYC0; -.
DR MaxQB; Q9QYC0; -.
DR PaxDb; Q9QYC0; -.
DR PeptideAtlas; Q9QYC0; -.
DR PRIDE; Q9QYC0; -.
DR ProteomicsDB; 282027; -. [Q9QYC0-1]
DR ProteomicsDB; 282028; -. [Q9QYC0-2]
DR Antibodypedia; 4065; 776 antibodies from 41 providers.
DR DNASU; 11518; -.
DR Ensembl; ENSMUST00000114338; ENSMUSP00000109977; ENSMUSG00000029106. [Q9QYC0-2]
DR Ensembl; ENSMUST00000114340; ENSMUSP00000109979; ENSMUSG00000029106. [Q9QYC0-1]
DR GeneID; 11518; -.
DR KEGG; mmu:11518; -.
DR UCSC; uc008xcp.1; mouse. [Q9QYC0-2]
DR UCSC; uc008xcr.1; mouse. [Q9QYC0-1]
DR CTD; 118; -.
DR MGI; MGI:87918; Add1.
DR VEuPathDB; HostDB:ENSMUSG00000029106; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000158581; -.
DR InParanoid; Q9QYC0; -.
DR OMA; KITKWVQ; -.
DR PhylomeDB; Q9QYC0; -.
DR TreeFam; TF313003; -.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR BioGRID-ORCS; 11518; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Add1; mouse.
DR PRO; PR:Q9QYC0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9QYC0; protein.
DR Bgee; ENSMUSG00000029106; Expressed in retinal neural layer and 262 other tissues.
DR ExpressionAtlas; Q9QYC0; baseline and differential.
DR Genevisible; Q9QYC0; MM.
DR GO; GO:0005912; C:adherens junction; IMP:CAFA.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0008290; C:F-actin capping protein complex; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:MGI.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:CAFA.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:1903393; P:positive regulation of adherens junction organization; IMP:CAFA.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IMP:CAFA.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027766; ADD1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR PANTHER; PTHR10672:SF4; PTHR10672:SF4; 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; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..735
FT /note="Alpha-adducin"
FT /id="PRO_0000218531"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..732
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT COMPBIAS 420..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 429
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 445
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 480
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 481
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 614
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 714
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 724
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT VAR_SEQ 621..632
FT /note="DLPQEPTSRDDS -> AGDGCAKEYLLP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000177"
FT VAR_SEQ 633..735
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000178"
FT CONFLICT 234
FT /note="A -> T (in Ref. 2; AAF29504)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9QYC0-2:600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QYC0-2:605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QYC0-2:610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QYC0-2:613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QYC0-2:614
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 735 AA; 80647 MW; E6AAA7F6273A33DD CRC64;
MNGDTRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM
ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTA SVPNVYPAAP QGGMAALNMS
LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF
LIVPFGLLYS EVTASSLVKV NLQGDIVDRG STNLGVNQAG FTLHSAVYAA RPDAKCIVHI
HTPAGAAVSA MKCGLLPISP EALSLGDVAY HDYHGILVDE EEKILIQKNL GPKSKVLILR
NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLDPGKYK AKSRSPGTPA
GEGSGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL RERSKKYSDV EVPASVTGHS
FASDGDSGTC SPLRHSFQKQ QREKTRWLHS GRGDDASEEG QNGSSPKSKT KWTKEDGHRT
STSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLCGVMMD RSLVQGELVT
ASKAIIEKEY QPHVIVSTTG PNPFNTLTDR ELEEYRREVE RKQKGSEENL DETREQKEKS
PPDQSAVPNT PPSTPVKLEE DLPQEPTSRD DSDATTFKPT PPDLSPDEPS EALAFPAVEE
EAHASPDPTQ PPAEADPEPA SAPTPGAEEV ASPATEEGSP MDPGSDGSPG KSPSKKKKKF
RTPSFLKKSK KKSDS
