ID A0A2K5YJ46_MANLE Unreviewed; 878 AA.
AC A0A2K5YJ46;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Alpha-actinin-4 {ECO:0000256|ARBA:ARBA00040341};
DE AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000256|ARBA:ARBA00042924};
GN Name=ACTN4 {ECO:0000313|Ensembl:ENSMLEP00000015567.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000015567.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000015567.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000256|ARBA:ARBA00004529}.
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; A0A2K5YJ46; -.
DR Ensembl; ENSMLET00000039028.1; ENSMLEP00000015567.1; ENSMLEG00000031659.1.
DR GeneTree; ENSGT00940000159343; -.
DR Proteomes; UP000233140; 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:0001725; C:stress fiber; 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:SF425; ALPHA-ACTININ-4; 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; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00150; SPEC; 4.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..121
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 130..236
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 732..767
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 773..808
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 416..450
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 878 AA; 101273 MW; D47DE2F5B4EAF7BC CRC64;
MLRNENLLWG PSPQGAHSHG RTFTAWCNSH LRKAGTQIEN IDEDFRDGLK LMLLLEVISG
ERLPKPERGK MRVHKINNVN KALDFIASKG VKLVSIGAEE IVDGNAKMTL GMIWTIILRF
AIQDISVEET SAKEGLLLWC QRKTAPYKNV NVQNFHISWK DGLAFNALIH RHRPELIEYD
KLRKDDPVTN LNNAFEVAEK YLDIPKMLDA EDIVGTLRPD EKAIMTYVSC FYHAFSGAQK
AETAANRICK VLAVNQENEH LMEDYEKLAS DLLEWIRRTI PWLEDRVPQK TIQEMQQKLE
DFRDYRRVHK PPKVQEKCQL EINFNTLQTK LRLSNRPAFM PSEGKMVSDI NNGWQHLEQA
EKGYEEWLLN EIRRLERLDH LAEKFRQKAS IHEAWTDGKE AMLKHRDYET ATLSDIKALI
RKHEAFESDL AAHQDRVEQI AAIAQELNEL DYYDSHNVNT RCQKICDQWD ALGSLTHSRR
EALEKTEKQL EAIDQLHLEY AKRAAPFNNW MESAMEDLQD MFIVHTIEEI EGLISAHDQF
KSTLPDADRE REAILAIHKE AQRIAESNHI KLSGSNPYTT VTPQIINSKW EKVQQLVPKR
DHALLEEQSK QQSNEHLRRQ FASQANVVGP WIQTKMEEIG RISIEMNGTL EDQLSHLKQY
ERSIVDYKPN LDLLEQQHQL IQEALIFDNK HTNYTMEHIR VGWEQLLTTI ARTINEVENQ
ILTRDAKGIS QEQMQEFRAS FNHFDKDHGG ALGPEEFKAC LISLGYDVEN DRQGEAEFNR
IMSLVDPNHS GLVTFQAFID FMSRETTDTD TADQVIASFK VLAGDKNFIT AEELRRELPP
DQAEYCIARM APYQGPDAVP GALDYKSFST ALYGESDL
//
