ADDB_PONAB
ID ADDB_PONAB Reviewed; 726 AA.
AC Q5R5V7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Beta-adducin;
DE AltName: Full=Erythrocyte adducin subunit beta;
GN Name=ADD2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- 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. {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; CR860745; CAH92859.1; -; mRNA.
DR RefSeq; NP_001127598.1; NM_001134126.1.
DR AlphaFoldDB; Q5R5V7; -.
DR SMR; Q5R5V7; -.
DR STRING; 9601.ENSPPYP00000013740; -.
DR PRIDE; Q5R5V7; -.
DR Ensembl; ENSPPYT00000043359; ENSPPYP00000040260; ENSPPYG00000012321.
DR GeneID; 100174677; -.
DR KEGG; pon:100174677; -.
DR CTD; 119; -.
DR eggNOG; KOG3699; Eukaryota.
DR GeneTree; ENSGT00940000159299; -.
DR HOGENOM; CLU_006033_9_2_1; -.
DR InParanoid; Q5R5V7; -.
DR OMA; PFVQEKA; -.
DR OrthoDB; 400524at2759; -.
DR TreeFam; TF313003; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Actin-binding; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..726
FT /note="Beta-adducin"
FT /id="PRO_0000262583"
FT REGION 1..25
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 467..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..721
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000255"
FT COMPBIAS 563..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05764"
FT MOD_RES 55
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
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 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 611
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 675
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05764"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB8"
FT MOD_RES 703
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P35612"
FT MOD_RES 713
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P35612"
SQ SEQUENCE 726 AA; 80840 MW; 7B1E4D622C29B0D4 CRC64;
MSEETVPEAA SPPPPQGQPY FDRFSEDDPE YMRLRNRAAD LRQDFNLMEQ KKRVTMILQS
PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPTSSMNVS MMTPINDLHT
ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV
TASSLIKVNI LGEVVEKGSS CFPVDTTGFC LHSAIYAARP DVRCIIHLHT PATAAVSAMK
WGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GVVALGDTVE
EAFYKIFHLQ AACEIQVSAL SSAGGVENLI LLEQEKHRPH DVGSVQWAGS TFGPMQKSRL
GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI PATVTAFVFE EDGAPVPALR
QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ RSMGSPRPKT TWMKADEVEK SSSGMPIRIE
NPNQFVPLYT DPQEVLEMRN KIREQNRQDV KSAGPQSQLL ASVIAEKSRS PSTESQLMSK
GDEDTKDDSE ETVPNPFSQL TDQELEEYKK EVERKKLELD GEKETAPEEP GSPAKSAPAS
PVQSPAKEAE TKSPLVSPSK SLEEGTKKTE TSKAATTEPE TTQPEGVVVN GREEEQTAEE
ILSKGLSQMT TSADTDVDTS KDKTESVTSG PMSPEGSPSK SPSKKKKKFR TPSFLKKSKK
KEKVES
