ADDA_RAT
ID ADDA_RAT Reviewed; 735 AA.
AC Q63028; Q3B7D4; Q64722;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 160.
DE RecName: Full=Alpha-adducin;
DE AltName: Full=Erythrocyte adducin subunit alpha;
GN Name=Add1;
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].
RC STRAIN=Milan; TISSUE=Bone marrow;
RX PubMed=8543181; DOI=10.1016/0378-1119(95)00590-0;
RA Tripodi G., Casari G., Tisminetzky S., Bianchi G., Devescovi G., Muro A.,
RA Tuteja R., Baralle F.E.;
RT "Characterisation and chromosomal localisation of the rat alpha- and beta-
RT adducin-encoding genes.";
RL Gene 166:307-311(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 426-735.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8624703; DOI=10.1016/0006-8993(95)00962-p;
RA Seidel B., Zuschratter W., Wex H., Garner C.C., Gundelfinger E.D.;
RT "Spatial and sub-cellular localization of the membrane cytoskeleton-
RT associated protein alpha-adducin in the rat brain.";
RL Brain Res. 700:13-24(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-355; THR-358;
RP SER-366; SER-465; SER-586; SER-600; THR-610 AND THR-614, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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. 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 {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q63028-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63028-2; Sequence=VSP_000179, VSP_000180;
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; Z49081; CAA88906.1; -; mRNA.
DR EMBL; Z49082; CAA88907.1; -; mRNA.
DR EMBL; BC107657; AAI07658.1; -; mRNA.
DR EMBL; X83715; CAA58690.1; -; mRNA.
DR PIR; S54147; S54147.
DR RefSeq; NP_058686.2; NM_016990.2. [Q63028-1]
DR AlphaFoldDB; Q63028; -.
DR SMR; Q63028; -.
DR BioGRID; 246360; 1.
DR IntAct; Q63028; 1.
DR MINT; Q63028; -.
DR STRING; 10116.ENSRNOP00000018072; -.
DR iPTMnet; Q63028; -.
DR PhosphoSitePlus; Q63028; -.
DR jPOST; Q63028; -.
DR PaxDb; Q63028; -.
DR PRIDE; Q63028; -.
DR GeneID; 24170; -.
DR KEGG; rno:24170; -.
DR CTD; 118; -.
DR RGD; 2041; Add1.
DR eggNOG; KOG3699; Eukaryota.
DR InParanoid; Q63028; -.
DR OrthoDB; 400524at2759; -.
DR PhylomeDB; Q63028; -.
DR TreeFam; TF313003; -.
DR Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-RNO-5223345; Miscellaneous transport and binding events.
DR PRO; PR:Q63028; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0008290; C:F-actin capping protein complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR GO; GO:0042608; F:T cell receptor binding; IDA:RGD.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:RGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0006884; P:cell volume homeostasis; ISO:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0020027; P:hemoglobin metabolic process; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006811; P:ion transport; NAS:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:RGD.
DR GO; GO:1903393; P:positive regulation of adherens junction organization; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
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_0000218532"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..486
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..453
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:0007744|PubMed:22673903"
FT MOD_RES 59
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P35611"
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:22673903"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 408
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 429
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35611"
FT MOD_RES 436
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P35611"
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:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC0"
FT MOD_RES 614
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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="GLPQEPTSRDGS -> GDGCAKEYLLP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000179"
FT VAR_SEQ 633..735
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000180"
FT VARIANT 316
FT /note="Y -> F (in strain: Milan hypersensitive)"
FT CONFLICT 633..636
FT /note="DATT -> GCHA (in Ref. 1; CAA88907)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="A -> G (in Ref. 3; CAA58690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 80355 MW; 5DFC5DB452774222 CRC64;
MNGDTRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM
ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTA SVPNVYPAAP QGGMAALNMS
LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF
LIVPFGLLYS EVTASSLVKV NLQGDIVDRG STNLGVNQAG FTLHSAIYAA RPDAKCIVHI
HTPAGAAVSA MKCGLLPISP EALSLGEVAY HDYHGILVDE EEKILIQKNL GPKSKVLILR
NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLDPGKYK AKSRSPGTPA
GEGSGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL RERSKKYSDV EVPASVTGHS
FASDGDSGTC SPLRHSFQKQ QREKTRWLNS GRGDDASEEG QNGSSPKSKT KWTKEDGHRT
STSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLCGVMMD RSLVQGELVT
ASKAIIEKEY QPHVIVSTTG PNPFNTLTDR ELEEYRREVE RKQKGSEENL DETREQKEKS
PPDQSAVPNT PPSTPVKLEG GLPQEPTSRD GSDATTSKPT PPDLSPDEPS EALAFPTVAE
EAHASPDTTQ PLAEADPEPA SASAPGAEEV ASPATEEGSP MDPGSDGSPG KSPSKKKKKF
RTPSFLKKSK KKSDS
