ADDB_RAT
ID ADDB_RAT Reviewed; 725 AA.
AC Q05764;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Beta-adducin;
DE AltName: Full=Adducin-63;
DE AltName: Full=Erythrocyte adducin subunit beta;
GN Name=Add2;
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 2).
RC STRAIN=Milan; TISSUE=Spleen;
RX PubMed=2059221; DOI=10.1016/0006-291x(91)90629-l;
RA Tripodi G., Piscone A., Borsani G., Tisminetzky S., Salardi S., Sidoli A.,
RA James P., Pongor S., Bianchi G., Baralle F.E.;
RT "Molecular cloning of an adducin-like protein: evidence of a polymorphism
RT in the normotensive and hypertensive rats of the Milan strain.";
RL Biochem. Biophys. Res. Commun. 177:939-947(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 532-725 (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-25; SER-60; SER-530;
RP SER-532; SER-594; SER-602; SER-614; SER-618; THR-674; SER-678; SER-685;
RP SER-688 AND SER-692, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-561
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 the erythrocyte
CC membrane receptor SLC2A1/GLUT1 and may therefore provide a link between
CC the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin.
CC Calmodulin binds preferentially to the beta subunit (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Found in a complex
CC with ADD2, DMTN and SLC2A1. Interacts with SLC2A1 (By similarity).
CC {ECO:0000250}.
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=Q05764-1; Sequence=Displayed;
CC Name=2; Synonyms=Adducin 63;
CC IsoId=Q05764-2; Sequence=VSP_000186, VSP_000187;
CC -!- TISSUE SPECIFICITY: Found in liver, kidney, spleen, heart and brain.
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; M63894; AAA40679.1; -; mRNA.
DR EMBL; AF130338; AAF31764.1; -; mRNA.
DR PIR; JQ1036; JQ1036.
DR RefSeq; NP_001103350.1; NM_001109880.1.
DR RefSeq; NP_036623.1; NM_012491.2. [Q05764-2]
DR AlphaFoldDB; Q05764; -.
DR SMR; Q05764; -.
DR BioGRID; 246361; 3.
DR IntAct; Q05764; 1.
DR MINT; Q05764; -.
DR STRING; 10116.ENSRNOP00000021491; -.
DR iPTMnet; Q05764; -.
DR PhosphoSitePlus; Q05764; -.
DR PaxDb; Q05764; -.
DR PRIDE; Q05764; -.
DR Ensembl; ENSRNOT00000081173; ENSRNOP00000073973; ENSRNOG00000015903. [Q05764-2]
DR GeneID; 24171; -.
DR KEGG; rno:24171; -.
DR UCSC; RGD:2042; rat. [Q05764-1]
DR CTD; 119; -.
DR RGD; 2042; Add2.
DR VEuPathDB; HostDB:ENSRNOG00000015903; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000159299; -.
DR InParanoid; Q05764; -.
DR PhylomeDB; Q05764; -.
DR Reactome; R-RNO-5223345; Miscellaneous transport and binding events.
DR PRO; PR:Q05764; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000015903; Expressed in frontal cortex and 13 other tissues.
DR ExpressionAtlas; Q05764; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0008290; C:F-actin capping protein complex; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO: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:0019901; F:protein kinase 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:0051017; P:actin filament bundle assembly; ISO:RGD.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0006811; P:ion transport; IMP:RGD.
DR GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR027773; ADD2.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR PANTHER; PTHR10672:SF6; PTHR10672:SF6; 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 Actin-binding; Alternative splicing; Calmodulin-binding; Cell membrane;
KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..725
FT /note="Beta-adducin"
FT /id="PRO_0000218535"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..444
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT REGION 525..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..720
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..716
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 533
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT VAR_SEQ 532..562
FT /note="STESQLASKGDADTKDELEETVPNPFSQLTD -> VQQRLPPTEGEAYQTPG
FT AGQGTPESSGPLTP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2059221"
FT /id="VSP_000186"
FT VAR_SEQ 563..725
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2059221"
FT /id="VSP_000187"
FT VARIANT 529
FT /note="R -> Q (in strain: Milan hypertensive)"
FT MOD_RES Q05764-2:561
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 725 AA; 80593 MW; 0715BD6A75B3D174 CRC64;
MSEDTVPEAA SPPPSQGQHY FDRFSEDDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS
PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPASSMNFS MMTPINDLHT
ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV
TASSLIKVNI LGEVVEKGSS CFPVDTTGFS LHSAIYAARP DVRCAIHLHT PATAAVSAMK
CGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GMVALGDTVE
EAFYKVFHLQ AACEVQVSAL SSAGGTENLI LLEQEKHRPH EVGSVQWAGS TFGPMQKSRL
GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI PATVTAFVFE EDGVPVPALR
QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ RNMGSPRPKT TWMKADEVEK SSSGMPIRIE
NPNQFVPLYT DPQEVLDMRN KIREQNRQDI KSAGPQSQLL ASVIAEKSRS PSTESQLASK
GDADTKDELE ETVPNPFSQL TDQELEEYKK EVERKKLEQE QEGEKDAATE EPGSPVKSTP
ASPVQSPTRA GTKSPAVSPS KASEDAKKTE VSEANTEPEP EKPEGVVVNG KEEEPCVEEV
LSKGPGQMTT NADTDGDSYK DKTESVTSGP LSPEGSPSKS PSKKKKKFRT PSFLKKSKKK
EKVES
