ID A0A2K5YJC3_MANLE Unreviewed; 857 AA.
AC A0A2K5YJC3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSMLEP00000015647.1};
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:ENSMLEP00000015647.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000015647.1}
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; A0A2K5YJC3; -.
DR Ensembl; ENSMLET00000039108.1; ENSMLEP00000015647.1; ENSMLEG00000031659.1.
DR GeneTree; ENSGT00940000159343; -.
DR OMA; KTIMSYM; -.
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 1..100
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 109..215
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 711..746
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 752..787
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 395..429
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 857 AA; 98933 MW; E44F2DC4662D10FC CRC64;
TFTAWCNSHL RKAGTQIENI DEDFRDGLKL MLLLEVISGE RLPKPERGKM RVHKINNVNK
ALDFIASKGV KLVSIGAEEI VDGNAKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ
RKTAPYKNVN VQNFHISWKD GLAFNALIHR HRPELIEYDK LRKDDPVTNL NNAFEVAEKY
LDIPKMLDAE DIVNTARPDE KAIMTYVSSF YHAFSGAQKA ETAANRICKV LAVNQENEHL
MEDYEKLASD LLEWIRRTIP WLEDRVPQKT IQEMQQKLED FRDYRRVHKP PKVQEKCQLE
INFNTLQTKL RLSNRPAFMP SEGKMVSDIN NGWQHLEQAE KGYEEWLLNE IRRLERLDHL
AEKFRQKASI HEAWTDGKEA MLKHRDYETA TLSDIKALIR KHEAFESDLA AHQDRVEQIA
AIAQELNELD YYDSHNVNTR CQKICDQWDA LGSLTHSRRE ALEKTEKQLE AIDQLHLEYA
KRAAPFNNWM ESAMEDLQDM FIVHTIEEIE GLISAHDQFK STLPDADRER EAILAIHKEA
QRIAESNHIK LSGSNPYTTV TPQIINSKWE KVQQLVPKRD HALLEEQSKQ QSNEHLRRQF
ASQANVVGPW IQTKMEEIGR ISIEMNGTLE DQLSHLKQYE RSIVDYKPNL DLLEQQHQLI
QEALIFDNKH TNYTMEHIRV GWEQLLTTIA RTINEVENQI LTRDAKGISQ EQMQEFRASF
NHFDKDHGGA LGPEEFKACL ISLGYDVEND RQGEAEFNRI MSLVDPNHSG LVTFQAFIDF
MSRETTDTDT ADQVIASFKV LAGDKNFITA EELRRELPPD QAEYCIARMA PYQGPDAVPG
ALDYKSFSTA LYGESDL
//