ID A0A3Q3KSH2_9TELE Unreviewed; 907 AA.
AC A0A3Q3KSH2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
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 Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000000264.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000000264.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3KSH2; -.
DR Ensembl; ENSMAMT00000000269.2; ENSMAMP00000000264.2; ENSMAMG00000000189.2.
DR GeneTree; ENSGT00940000155548; -.
DR Proteomes; UP000261640; 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; 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; 3.
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; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 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; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
DR PROSITE; PS00020; ACTININ_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 24..128
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 137..243
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 739..774
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 802..837
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 258..285
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 423..457
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 907 AA; 104341 MW; 4E37A08970F7F770 CRC64;
LSVISLRKFH ECSEPTHQWL LSGFCSPATF TAWCNSHLRK AGTQIENIEE DFRDGLKLML
LLEVISGERL AKPERGKMRV HKISNVNKAL DFIASKGVKL VSIGAEEIVD GNAKMTLGMI
WTIILRFAIQ DISVEETSAK EGLLLWCQRK TAPYKNVNIQ NFHISWKDGL GFCALIHRHR
PELIDYAKLR KDDPMTNLNT AFDVAEKYLD IPKMLDAEDI ISTLRPDEKA VMTYVSCYYH
AFSGKQKAET AANRICKVLA VNQENEQLME DYEKLASDLL EWIRRTIPWL ENRMPENTMQ
AMQQKLEDFR DYRRLHKPPK VQEKCQLEIN FNTLQTKLRL SNRPAFMPSE GKMVSDINNA
WGNLEGAEKG YEEWLLNEIR RLERLDHLAE KFRQKAAIHE AWTEGKEDML QKRDYETASL
SEIKALLKKH EAFESDLAAH QDRVEQIAAI AQELNELDYY DSPSVNARCQ RICDQWDALG
ALTQKRSEAL QRTEKLLETI DQLYLEFAKR AAPFNNWMEG AMEDLQDTFI VHTIEEIQGL
STAHEQFKAT LPEADKERQA ILGIHNEIAK IVQTYHVNMA GTNPYTTINP QEINTKWDKV
RQLVPQRDQA LIEEHARQQN NERLRRQFAN QANVIGPWIQ TKMEEIGRIS IEMHGTLEDQ
LTHLRQYEKS IVNYKPKIDQ LEGDHQLIQE ALIFDNKHTN YTMEHIRVGW EQLLTTIART
INEIENQILT RDAKGISQDQ LNEFRASFNH FDRDHSGTLG AEEFKACLIS LGFDIANDAQ
KRTGIMDAED FKTCLISMGY NLGENEFSRI MSIVDPNRMG IVTFQAFIDF MSRETADTDT
ADQVMASFKV LAGDKNYILA DELRRELPPD QADYCIARMA PYTGPDAVPG ALDYMSFSTA
LYGESDL
//
