ID A0A3B3R8K3_9TELE Unreviewed; 891 AA.
AC A0A3B3R8K3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Alpha-actinin-1 {ECO:0000256|ARBA:ARBA00018384};
DE AltName: Full=Alpha-actinin cytoskeletal isoform {ECO:0000256|ARBA:ARBA00041477};
DE AltName: Full=F-actin cross-linking protein {ECO:0000256|ARBA:ARBA00043249};
DE AltName: Full=Non-muscle alpha-actinin-1 {ECO:0000256|ARBA:ARBA00042871};
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:ENSPKIP00000014574.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000014574.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, ruffle
CC {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000256|ARBA:ARBA00004216}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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DR AlphaFoldDB; A0A3B3R8K3; -.
DR STRING; 1676925.ENSPKIP00000014574; -.
DR Ensembl; ENSPKIT00000039023.1; ENSPKIP00000014574.1; ENSPKIG00000001541.1.
DR GeneTree; ENSGT00940000155548; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; 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; 3.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF434; ALPHA-ACTININ-1; 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; 3.
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; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 30..134
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 143..249
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 745..780
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 786..821
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 264..291
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 429..463
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 670..697
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 891 AA; 102556 MW; 6D48DAC832EE3D95 CRC64;
MDHYEADENE YMHQEDDWDR DLLLDPAWEK QQRKTFTAWC NSHLRKAGTQ IENIEEDFRD
GLKLMLLLEV ISGERLAKPE RGKMRVHKIS NVNKALDFIA SKGVKLVFIG AEEIVDGNAK
MTLGMIWTII LRFAIQDISV EETSAKEGLL LWCQRKTAPY KNVNIQNFHI SWKDGLGFCA
LIHRHRPELI DYGKLRKDDP MTNLNTAFDV AEKYLDIPKM LDAEDIVGTA RPDEKAIMTY
VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEQLMEDYEK LASDLLEWIR RTIPWLENKT
PENTMQAMQQ KLEDFRDYRR LHKPPKVQEK CQLEINFNTL QTKLRLSNRP AFMPSEGKMV
SDISNAWVGL EGAEKGYEEW LLNEIRRLER LDHLAEKFRQ KAAIHEAWTE GKEEMLQKSD
YETASLSDIK ALLKKHEAFE SDLAAHQDRV EQIAAIAQEL NELDYYDSPS VNTRCQHICD
QWDALGVLSQ KRSEALQRTE KLLETIDQLY LEFAKRAAPF NNWMEGAMED LQDTFIVHTI
EEILGLSTAH EQFKATLPDA DKERQAILGI HNEIAKIVQT YHVNMAGSNP YTTINPQEIN
TKWDKVRQLV PQRDQALSGE HARQQNNERL RKQFASQANV IGPWMQTKME EIGRISIEMH
GTLEDQLTHL RQYEKSIVNY KSKIDQLEGD HQLIQEALIF DNKHTNYTME HVRVGWEQLL
TTIARTINEI ENQILTRDAK GISQEQMNEF RASFNHFDRD HSGTLGAEEF KACLISLGYD
IANDAQGEAE FARIMSIVDP NRQGVVTFQA FIDFMSRETA DTDTADQVMT SFKVLAGDKN
YILADELRRE LPPDQAEYCI ARMAPYSGPD GVPGALDYMS FSTALYGESD L
//