ID A0A3B3R9Q5_9TELE Unreviewed; 886 AA.
AC A0A3B3R9Q5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSPKIP00000014635.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000014635.1}
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; A0A3B3R9Q5; -.
DR Ensembl; ENSPKIT00000039084.1; ENSPKIP00000014635.1; 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; 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; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
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 781..816
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 886 AA; 102211 MW; C8AF092079C1D8FD 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 RASFNHFDRK RTGMMDAEDF GVYLISLGYN
LGEAEFARIM SIVDPNRQGV VTFQAFIDFM SRETADTDTA DQVMTSFKVL AGDKNYILAD
ELRRELPPDQ AEYCIARMAP YSGPDGVPGA LDYMSFSTAL YGESDL
//
