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Database: UniProt
Entry: A0A7K9MH34_OCETE
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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
//
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