ID A0A7K9MH34_OCETE Unreviewed; 736 AA.
AC A0A7K9MH34;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE RecName: Full=Alpha-adducin {ECO:0000256|ARBA:ARBA00072931};
DE AltName: Full=Erythrocyte adducin subunit alpha {ECO:0000256|ARBA:ARBA00076470};
DE Flags: Fragment;
GN Name=Add1 {ECO:0000313|EMBL:NXH73971.1};
GN ORFNames=HYDTET_R06403 {ECO:0000313|EMBL:NXH73971.1};
OS Oceanodroma tethys (Wedge-rumped storm-petrel) (Hydrobates tethys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Procellariiformes;
OC Hydrobatidae; Oceanodroma.
OX NCBI_TaxID=79633 {ECO:0000313|EMBL:NXH73971.1, ECO:0000313|Proteomes:UP000527232};
RN [1] {ECO:0000313|EMBL:NXH73971.1, ECO:0000313|Proteomes:UP000527232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-32 {ECO:0000313|EMBL:NXH73971.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXH73971.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXH73971.1}.
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DR EMBL; VWZR01011911; NXH73971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K9MH34; -.
DR OrthoDB; 3238794at2759; -.
DR Proteomes; UP000527232; 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 CDD; cd00398; Aldolase_II; 1.
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:UP000527232}.
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 421..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..702
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..736
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXH73971.1"
FT NON_TER 736
FT /evidence="ECO:0000313|EMBL:NXH73971.1"
SQ SEQUENCE 736 AA; 81227 MW; 8C919412DF4898AA 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 TLASAGGPDN LVLLDPGKYK AKSRSPESPA
GEGTVSHPKW QIGEQEFEAL MRMLDNLGYR TGYPYRCPAL REKSKKYSDV EIPASVTGYS
FTSDGESGTC SPLRHSFQKQ QREKTRWLNS GRGDDASEEG QNGSSPKSKT KWTKEDGHRT
ATSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLSGVVVD RSLVQGELVT
ASKAIIEKEY QPKVIVSTTG PNPFNKLTDR ELEEYRKEVE RKQKGPEEPS EDGRQQKERS
PPDHTSAHTP PSTPIKVEEE TQQDQTYKDD SDAATFKQTL PDLTPDEPSE ALSFPPLGKE
EGRCDEDVPK SQTESPAVEN KEPQSQPAEE PVTPTAEEGT AADAGSDESP GKSPSKKKKK
FRTPSFLKKS KKKSDS
//