ID A0A091IEK6_CALAN Unreviewed; 741 AA.
AC A0A091IEK6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-OCT-2025, entry version 31.
DE RecName: Full=Alpha-adducin {ECO:0000256|ARBA:ARBA00072931};
DE AltName: Full=Erythrocyte adducin subunit alpha {ECO:0000256|ARBA:ARBA00076470};
GN ORFNames=N300_01805 {ECO:0000313|EMBL:KFP07039.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Strisores; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP07039.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP07039.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP07039.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes the
CC assembly of the spectrin-actin network. Binds to calmodulin.
CC {ECO:0000256|ARBA:ARBA00055853}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit or an alpha and a
CC gamma subunit. {ECO:0000256|ARBA:ARBA00065959}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000256|ARBA:ARBA00006274}.
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DR EMBL; KL218617; KFP07039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IEK6; -.
DR STRING; 9244.A0A091IEK6; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:TreeGrafter.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter.
DR GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:TreeGrafter.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProtKB-ARBA.
DR GO; GO:1903393; P:positive regulation of adherens junction organization; IEA:TreeGrafter.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IEA:TreeGrafter.
DR FunFam; 3.40.225.10:FF:000002; alpha-adducin isoform X2; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR InterPro; IPR051017; Aldolase-II_Adducin_sf.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR NCBIfam; NF005451; PRK07044.1; 1.
DR PANTHER; PTHR10672; ADDUCIN; 1.
DR PANTHER; PTHR10672:SF4; ALPHA-ADDUCIN; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT DOMAIN 147..329
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..741
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 81917 MW; BA0C385B577684B9 CRC64;
MNGDSGVGVV TSPPPTTAPH KERYFDRVDE NNPDYLRERN MAPDLRQDFN MMEQKKRVSM
ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTT NVPNVYPAAP QGGMAALNMS
LGMVTPVNDL RGSDSIAYEK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT ARVNSEQEHF
LIVPFGLLYS EVTASSLVKI NIQGDVVDRG STNLGVNQAG FTLHSAIYAA RPDVKCIVHI
HTPAGAAVSA MKCGLLPISP EALSLGEVAY HDYHGILVDD EEKVVIQKNL GPKSKVLILR
NHGLVSVGET VEEAFYYIHN LVLACEIQVR ILVCYILIYA GGPDNLVLLD PGKYKAKSRS
PESPSGEGTV SHPKWQIGEQ EFEALMRMLD NLGYRTGYPY RCPALREKSK KYSDVEIPAS
VTGYSFASDG ESGTCSPLRH SFQKQQREKT RWLNSGRGDD ASEEGQNGSS PKSKTKWTKE
DGHRTATSAV PNLFVPLNTN PKEVQEMRNK IREQNLQDIK TAGPQSQVLS GVVVDRSLVQ
GELVTASKAI IEKEYQPKVI VSTTGPNPFN KLTDRELEEY RKEVERKQKG PEEPSEHGRQ
QKERSPPDHT SARTPPSTPI KIEEETQQDQ TYKDDSDAAT FKQTLPDLTP DEPSEALGFP
PLGKEEGRCD EVVPKSQTQL PAVENKEPQS QAAEEAVTPT AEEGTAADAG SDESPGKSPS
KKKKKFRTPS FLKKSKKKSD S
//
