ID A0A3Q4M516_NEOBR Unreviewed; 856 AA.
AC A0A3Q4M516;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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 Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000002469.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000002469.1}
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; A0A3Q4M516; -.
DR Ensembl; ENSNBRT00000002561.1; ENSNBRP00000002469.1; ENSNBRG00000001031.1.
DR GeneTree; ENSGT00940000155548; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000001031; Expressed in mesonephros and 6 other cell types or tissues.
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; 1.
DR Gene3D; 1.20.58.60; -; 3.
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; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 3.
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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 43..147
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 156..262
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 715..750
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 751..786
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 277..304
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 442..476
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 856 AA; 97758 MW; F0C45D84B32BB2EF CRC64;
MPDNPRLATP TVCIQWSSVW KLSEENPEVK FVGTTGKGES VGAGIASTFT AWCNSHLRKA
GTQIENIEED FRDGLKLMLL LEVISGERLA KPERGKMRVH KISNVNKALD FIASKGVKLV
SIGAEEIVDG NAKMTLGMIW TIILRFAIQD ISVEETSAKE GLLLWCQRKT APYKNVNIQN
FHISWKDGLG FCALIHRHRP ELIDYGKLRK DDPMTNLNTA FDVAEKYLDI PKMLDAEDIV
GTARPDEKAI MTYVSSFYHA FSGAQKAETA ANRICKVLAV NQENEQLMED YEKLASDLLE
WIRRTIPWLE NRMPENTMQA MQQKLEDFRD YRRLHKPPKV QEKCQLEINF NTLQTKLRLS
NRPAFMPSEG KMVSDINNAW GNLEGAEKGY EEWLLNEIRR LERLDHLAEK FRQKAAIHEA
WTEGKEDMLQ KRDYETASLS EIKALLKKHE AFESDLAAHQ DRVEQIAAIA QELNELDYYD
SPSVNARCQR ICDQWDALGA LTQKRSEALQ RTEKLLETID QLYLEFAKRA APFNNWMEGA
MEDLQDTFIV HTIEEIQGLS AAHEQFKATL PEADKERLAI LGIHNEIAKI VQTYHVNIAG
TNPYTTINPQ EINAKWDKVR QLVPQRDQAL IEEHARQQNN ERLRRQFANQ ANVIGPWIQT
KMEVSSTLTL PLPSSFSPLQ HIRVGWEQLL TTIARTINEI ENQILTRDAK GISQEQLNEF
RASFNHFDRK RTGIMDPEDF KTCLISMGYN LGENEFSRIM SIVDPNRMGL VTFQAFIDFM
SRETADTDTA DQVMASFKVL AGDKNYILAD ELRRELPPDQ AEYCIARMAP YTGPDGVPGA
LDYMSFSTAL YGESDL
//
