ID A0A3P9DEZ9_9CICH Unreviewed; 910 AA.
AC A0A3P9DEZ9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:ENSMZEP00005033058.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005033058.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005033058.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005033058.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
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 RefSeq; XP_012771131.1; XM_012915677.1.
DR AlphaFoldDB; A0A3P9DEZ9; -.
DR STRING; 106582.ENSMZEP00005033058; -.
DR Ensembl; ENSMZET00005034153.1; ENSMZEP00005033058.1; ENSMZEG00005024648.1.
DR GeneID; 101467576; -.
DR GeneTree; ENSGT00940000159343; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000265160; LG14.
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: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; 2.
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: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; 2.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 38..142
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 151..257
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 805..840
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 437..471
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 910 AA; 104169 MW; F0FD4977313141EA CRC64;
MVDYHAANNQ STVGGAQTYM EQENDWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE
NIEEDFRDGL KLMLLLEVIS GERLPKPERG KMRVHKINNV NKALDFIASK GVKLVSIGAE
EIVDGNAKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYKN VNVQNFHISW
KDGLAFNALI HRHRPDLIDY DSLRKDDPVT NLNNAFEVAE KHLDIPKMLD AEDIVGTLRP
DEKAIMTYVS CFYHAFSGAQ KAETAANRIC KVLAVNQENE QMMEDYEKLA SDLLEWIRRT
IPWLENRTQE KTVNDMQVKQ EDFRDYRCVH KPPKVQEKCQ LEISFNTLQT KLRLSNRPAF
MPSEGRMVSD INKAWHNLEG AEKGYEEWIL SEIRRLERLE HLAVKFHQKC AIHESWTDGK
EAMLTQKDYE TCTLSEVKAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYYDAASVN
ARCQKICDQW DVLGALTHKR KESLERTEKQ LESIDELYLE YAKRAAPFNN WMEGAMEDLQ
DMFIVHNIEE IQGLITAHEQ FKSTLPEANK EREAIQSIQS EVQKIAQSNG IKLSSGNPYT
SITPESINSK WEQAMAMVPL RDNALQEELN KQNSNDTLRA TFATQANTVG AYIQAKMEEI
GRISIEMNGT LEDQLTNLKE YQKSIISYTP EINKLEGYHQ HIQEALIFDN QYTSYTMEHL
RVGWEQLLTT IARTINEVEN QILTRDAKGI SQEQLYEYRA SFNHFDKTLN GGERGARHDH
SGALMAEEFK ACLISLGYDV EKDKQGEAEF NRIMGIVDPN GSGAVTFQAF IDFMSTETTD
RDTADQVIAS FKILAADKNY ITADELRREL PPDQAEYCIA RMAPYTGPDA VPGALDYMSF
STALYGESDL
//
