ID A0A3Q1HVA4_9TELE Unreviewed; 921 AA.
AC A0A3Q1HVA4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Alpha-actinin-4 {ECO:0000256|ARBA:ARBA00040341};
DE AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000256|ARBA:ARBA00042924};
GN Name=ACTN4 {ECO:0000313|Ensembl:ENSAPOP00000031590.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000031590.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000031590.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1HVA4; -.
DR Ensembl; ENSAPOT00000033425.1; ENSAPOP00000031590.1; ENSAPOG00000019039.1.
DR GeneTree; ENSGT00940000159343; -.
DR Proteomes; UP000257200; 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; cd00051; EFh; 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; 3.
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; PF13833; EF-hand_8; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
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; 1.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 38..142
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 151..257
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 753..788
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 816..851
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 272..299
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 437..471
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 921 AA; 104962 MW; 645502FB08FB0FFA CRC64;
MVDYHAANNQ PSAGGVQTYM EQENDWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE
NIEEDFRDGL KLMLLLEVIS GERLAKPERG KMRVHKINNV NKALDFIASK GVKLVSIGAE
EIVDGNAKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYKN VNVQNFHISW
KDGLAFNALI HRHRPDLIDY DSLRKDDPVH NLNNAFEVAE KHLDIPKMLD AEDIVNTARP
DEKAIMTYVS SFYHAFSGAQ KAETAANRIC KVLAVNQENE QMMEDYEKLA SELLEWIRRT
IPWLENRTQE KTVNEMQAKQ EDFRDYRCVH KPPKVQEKCQ LEISFNTLQT KLRLSNRPAF
MPSEGRMVSD INGAWHTLEG AEKGYEEWIL SEIRRLERLE HLAEKFHQKA AIHQSWTDGK
EAMLTQKDYE TSTLSEVKAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYYDSASVN
ACCQKICDQW DVLGALTQSR KESLERTEKQ LESIDELYLE YAKRAAPFNN WMEGAMEDLQ
DMFIVHNIEE IQGLITAHEQ FKSTLSEANK EREAIQAIQA EVQKIAQSNG IKLSGANPYT
TITPESIDSK WEKAMAMVPQ RDAALQEELN KQNSNDSLRA TFAAQANTVG AYIQAKMEEI
GRISIEMNGT LEDQLTSLKE YQKNIMSYMP EINKLEGYHQ LIQEALIFDN QYTAYTMEHL
RVGWEQLLTT IARTINEVEN QILTRDAKGI SQEQLYEYRA SFNHFDKDHS GALMAEEFKA
CLISLGYDVE NDKQKRSGQM VSDDFRALLI STGNSLGDGE FARIMGIVDP NGSGAVTFQA
FIDFMSRETT DTDTADQVIA SFKILAGDKN FITAEELRRE LPPDQAEYCI ARMAPYTGPD
GAPGALDYMS FSTALYGESD L
//
