ID   A0A3B3DXF9_ORYME        Unreviewed;       909 AA.
AC   A0A3B3DXF9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Alpha-actinin-4 {ECO:0000256|ARBA:ARBA00040341};
DE   AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000256|ARBA:ARBA00042924};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000034611.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000034611.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC       Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family.
CC       {ECO:0000256|ARBA:ARBA00010255}.
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DR   AlphaFoldDB; A0A3B3DXF9; -.
DR   Ensembl; ENSOMET00000028791.1; ENSOMEP00000034611.1; ENSOMEG00000021538.1.
DR   GeneTree; ENSGT00940000159343; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd21214; CH_ACTN_rpt1; 1.
DR   CDD; cd21216; CH_ACTN_rpt2; 1.
DR   CDD; cd00176; SPEC; 1.
DR   Gene3D; 1.20.58.60; -; 4.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF425; ALPHA-ACTININ-4; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00150; SPEC; 2.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF46966; Spectrin repeat; 4.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          37..141
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          150..256
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          804..839
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          436..470
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   909 AA;  104070 MW;  8A79065912CAF684 CRC64;
     MVDYHAANNQ PSGGPQTYME QENDWDRDLL LDPAWEKQQR KTFTAWCNSH LRKAGTQIEN
     IEEDFRDGLK LMLLLEVISG ERLPKPERGK MRVHKINNVN KALDFIASKG VKLVSIGAEE
     IVDGNIKMTL GMIWTIILRF AIQDISVEET SAKEGLLLWC QRKTAPYKNV NVQNFHISWK
     DGLAFNALIH RHRPDLIDYD NLRKDDPVTN LNNAFEVAEK HLDIPKMLDA EDIVNTARPD
     EKAIMTYVSS FYHAFSGAQK AETAANRICK VLAVNQENEQ MMEDYEKLAS NLLEWIRRTI
     PWLEDRTQQK TVNDMQAKQE DFRDYRTVHK PPKVQEKCQL EISFNTLQTK LRLSNRPAFM
     PSEGRMVSDI NAAWHTLEGA EKGYEEWILS EIRRLERLEH LAEKFHQKAA IHESWTSGKE
     AMLTQKDYET STLSEVKALL RKHEAFESDL AAHQDRVEQI AAIAQELNEL DYYDSASVND
     RCQKICDQWD TLGALTHRRK DSLERTEKQL ESIDELYLEY AKRAAPFNNW MEGAMEDLQD
     MFIVHNIEEI QGLIAAHEQF KSTLPEANKE REAIQAIQAE VQKIAQSNGI KLSGANPYTT
     ITPGSIDDKW EQAMAMVPQR DKALQEELNK QNSNDTLRAT FATQANAVGA YIQAKMEEIG
     RISIEMNGTL EDQLTHLREY QQSILSYMPE INKLEGDHQH IQEALIFDNQ YTSYTMEHLR
     VGWEQLLTTI ARTINEVENQ ILTRDAKGIS QEQLYEYRAS FNHFDKSISG AEKRSRCDHT
     GSLIAEEFKA CLISLGYDVE NDKQGDTEFA RIMSIVDPNN SGAVTFQAFI DFMSSETTDK
     DSADQVIASF KILAGDKNYI MPDELRRELP PDQAEYCIAR MAPYTGPDGV PGALDYMSFS
     TALYGESDL
//