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Database: UniProt
Entry: A0A6P7M8G5_BETSP
LinkDB: A0A6P7M8G5_BETSP
Original site: A0A6P7M8G5_BETSP 
ID   A0A6P7M8G5_BETSP        Unreviewed;       688 AA.
AC   A0A6P7M8G5;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   08-OCT-2025, entry version 22.
DE   SubName: Full=Adducin 3 (Gamma) a isoform X3 {ECO:0000313|RefSeq:XP_029003288.1, ECO:0000313|RefSeq:XP_029003297.1};
GN   Name=add3a {ECO:0000313|RefSeq:XP_029003288.1,
GN   ECO:0000313|RefSeq:XP_029003297.1, ECO:0000313|RefSeq:XP_029003306.1,
GN   ECO:0000313|RefSeq:XP_029003317.1, ECO:0000313|RefSeq:XP_029003327.1};
OS   Betta splendens (Siamese fighting fish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Osphronemidae; Betta.
OX   NCBI_TaxID=158456 {ECO:0000313|Proteomes:UP000515150, ECO:0000313|RefSeq:XP_029003306.1};
RN   [1] {ECO:0000313|RefSeq:XP_029003288.1, ECO:0000313|RefSeq:XP_029003297.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (APR-2025) to UniProtKB.
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   RefSeq; XP_029003288.1; XM_029147455.3.
DR   RefSeq; XP_029003297.1; XM_029147464.3.
DR   RefSeq; XP_029003306.1; XM_029147473.3.
DR   RefSeq; XP_029003317.1; XM_029147484.3.
DR   RefSeq; XP_029003327.1; XM_029147494.3.
DR   GeneID; 114853726; -.
DR   CTD; 556762; -.
DR   GeneTree; ENSGT00940000155257; -.
DR   Proteomes; UP000515150; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0061008; P:hepaticobiliary system development; IEA:Ensembl.
DR   FunFam; 3.40.225.10:FF:000004; gamma-adducin isoform X1; 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   PANTHER; PTHR10672; ADDUCIN; 1.
DR   PANTHER; PTHR10672:SF5; GAMMA-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   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:UP000515150}.
FT   DOMAIN          139..321
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..604
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..663
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..688
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  77147 MW;  E9591AC1875A28DB CRC64;
     MSADGRQEVV TTPPPPSGGT KERYFDRVDT SDPDYIRSRN MSPDLRQDFN VLEQKKRVTQ
     ILQSPAFKEE LESLIKEQQR KGNNPTGLLA LRQIADFFMA SSVAGFNTSP LSLGMVTPIN
     DMYSVEPATM VKGEKLTRCK LASLYRLVDL FSWAYFANSY ITARVSKEQD HILIIPRGLS
     FAEASASNLV KVNIIGDVIE QGSTNLRIDA SGFSPHAAIY SMRPDIRCVV HVHTPATAAV
     SSMKCGILPI SQEALLLGDV AYYSYQGSLD DQGERRELQK ALGPTTKVLV LRNHGVVALG
     ETIEEAFHYI YNAHYACEIQ VNAISCAGGV DNLIVLDQEK YKSRVHDVAT AGDVNMCGQY
     KWKIGELEFE SLMRMLDNLG YRTGHAYRHP VVRDKPRHKS DVEIPATVTA FMFEEDADGA
     ATRLPFKFLQ QRQQREKTRW LNSPNSYTKV SVEGGAERYS SRTTTWMKAE ETGTPIRIED
     PNQFVPLNTD PTEVLQRRNK IREQNRFDVM TSGPRSQHLA GIPVDEPRRV QIKVMPYVPT
     EEEQMAPLPP NPFNELSEKE LEEYRKNVER RQLGLSDGEH ELTSDDGSTL SQSLSLTQSP
     QSTPAKEENH TGLMNGKGAH EDEELSRRVS QLTTSAESVE ISVRAGEKIE EALSPESSPS
     KSPNTKKKKK FRTPSFLKKN KKKEKTEA
//
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