ID A0A3B4WVI9_SERLL Unreviewed; 899 AA.
AC A0A3B4WVI9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:ENSSLDP00000008186.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000008186.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000008186.1}
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; A0A3B4WVI9; -.
DR STRING; 1841481.ENSSLDP00000008186; -.
DR Ensembl; ENSSLDT00000008452.1; ENSSLDP00000008186.1; ENSSLDG00000006447.1.
DR GeneTree; ENSGT00940000159343; -.
DR Proteomes; UP000261360; 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; 2.
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; 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 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 794..829
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 437..471
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 899 AA; 102737 MW; C17B99C9AC52D1AF CRC64;
MVDYHAANNQ SSAGGVQTYM EQENDWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE
NIEEDFRDGL KLMLLLEVIS GERLPKPERG KMRVHKINNV NKALDFIASK GVKLVSIGAE
EIVDGNAKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYKN VNVQNFHISW
KDGLAFNALI HRHRPDLIDY DSLRKDDPVT NLNNAFEVAE KHLDIPKMLD AEDIVNTARP
DEKAIMTYVS SFYHAFSGAQ KAETAANRIC KVLAVNQENE QMMEDYEKLA SDLLEWIRRT
IPWLENRTQE KTVNDMQAKQ EDFRDYRCVH KPPKVQEKCQ LEISFNTLQT KLRLSNRPAF
MPSEGRMVSD INGAWHTLEG AEKGYEEWIL SEIRRLERLE HLAEKFHQKA AIHESWTDGK
EAMLTQKDYE TSTLSEVKAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYYDSASVN
ARCQKICDQW DVLGALTQSR KESLERTEKQ LESIDELYLE YAKRAAPFNN WMEGAMEDLQ
DMFIVHNIEE IQGLITAHEQ FKSTLSEANK EREAIQSIQA EVQKIAQSNG IKLSGANPYT
TITPESIDSK WEKAMAMVPL RDNALQEELN KQNSNDTLRA KFATQANAVG AYIQDKMEEI
GRISIEMNGT LEDQLTNLKE YQTNIMSYMP EINKLEGFHQ LIQEALIFDN QYTSYTMEHL
RVGWEQLLTT IARTINEVEN QILTRDAKGI SQEQLYEYRA SFNHFDKDHS GALMAEEFKA
CLISLGYDVE NDKQGDSEFA RIMGIVDPNG SGAVTFQAFI DFMSTETTDT DTADQVIASF
KILAADKNYI TAEELRRELP PDQAEYCIAR MAPYAGPDAV PGALDYMSFS TALYGESDL
//
