ID A0A3B3S2W0_9TELE Unreviewed; 895 AA.
AC A0A3B3S2W0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Alpha-actinin-4 {ECO:0000256|ARBA:ARBA00040341};
DE AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000256|ARBA:ARBA00042924};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000024873.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000024873.1}
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; A0A3B3S2W0; -.
DR Ensembl; ENSPKIT00000005594.1; ENSPKIP00000024873.1; ENSPKIG00000007802.1.
DR GeneTree; ENSGT00940000155548; -.
DR Proteomes; UP000261540; 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; 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; PF13499; EF-hand_7; 1.
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 39..143
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 152..258
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 754..789
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 790..825
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 438..472
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 895 AA; 103545 MW; FD063F64811E8073 CRC64;
MVDYHAANNQ NQQYPSGGTY MEQENDWDRD LLLDPAWEKQ QRKTFTAWCN SHLRKAGTQI
ENIEEDFRDG LKLMLLLEVI SGERLPKPER GKMRVHKINN VNKALDFIAS KGVKLVSIGA
EEIVDGNIKM TLGMIWTIIL RFAIQDISVE ETSAKEGLLL WCQRKTAPYK NVNVQNFHIS
WKDGLAFNAL IHRHRPDLID YEKLRKDDPV TNLNNAFEVA EKYLDIPKML DAEDIVGTLR
PDEKAIMTYV SCFYHAFSGA QKAETAANRI CKVLAVNQEN EHLMEDYEKL ASDLLEWIRR
TVPWLENRTP EKTMHEMQQK LEDFRDYRRV HKPPKVQEKC QLEINFNTLQ TKLRLNNRPA
FMPSEGRMVS DINSAWQHLE GAEKGYEEWL LNEIRRLERL DHLAEKFRQK ATIHEGWTAG
KESMLTQKDY ETASLSEVKA LLKKHEAFES DLAAHQDRVE QIAAIAQELN ELDYYDSPNV
NARCQKICEQ WDSLGSLTQS RRESLERTEK QLESIDELYL EYAKRAAPFN NWMEGAMEDL
QDMFIVHNIE EIQGLITAHE QFKSTLPEAN KEREAIQAIQ KEVQNIAQYN GIKLSGSNPY
TSITPESIDS KWDKVRQLVP QRDQALQEEL ERQQSNDHLR RQFANQANIV GPWIQNKMEE
IGRISIEMNG TLEDQLTHLR QYEQSIIEYK PNIDQLESNH ELIQEALIFD NKYTTYTMEH
LRVGWEQLLT TIARTINEIE NQILTRDAKG ISQEQLHEYR ASFNHFDKKR TGMMDSDDFR
ALLISTGNSL GDAEFARIMG IVDPNNSGAV TFQAFIDFMS RETTDTDTAD QVIASFKILA
GDKNYITAEE LRRELPHDQA DYCIARMVPY SGPDAIPGAL DYMSFSTALY GESDL
//
