ID H9GX78_DANRE Unreviewed; 901 AA.
AC H9GX78; A0A8M9Q056;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Alpha-actinin-4 {ECO:0000256|ARBA:ARBA00040341};
DE AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000256|ARBA:ARBA00042924};
GN Name=wu:fb53f05 {ECO:0000313|RefSeq:XP_021337012.1};
GN Synonyms=zgc:63508 {ECO:0000313|RefSeq:XP_021337012.1};
GN OrderedLocusNames=actn4 {ECO:0000313|Ensembl:ENSDARP00000132801,
GN ECO:0000313|RefSeq:XP_021337012.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-940};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000132801};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000132801, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000132801};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000132801}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000132801};
RG Ensembl;
RL Submitted (JUN-2015) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_021337012.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021337012.1};
RG RefSeq;
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 EMBL; CABZ01100159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01100160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01100466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01100467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01100468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01100469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01102128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01102129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01115154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO018570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_021337012.1; XM_021481337.1.
DR Ensembl; ENSDART00000172154; ENSDARP00000132801; ENSDARG00000099786.
DR Ensembl; ENSDART00000172154.2; ENSDARP00000132801.2; ENSDARG00000099786.2.
DR ZFIN; ZDB-GENE-030131-940; actn4.
DR eggNOG; KOG0035; Eukaryota.
DR HOGENOM; CLU_038415_1_1_1; -.
DR Proteomes; UP000000437; Chromosome 15.
DR Bgee; ENSDARG00000099786; Expressed in paraxial mesoderm and 38 other cell types or tissues.
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; -; 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; PF13499; EF-hand_7; 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; 2.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:H9GX78};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 40..144
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 153..259
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 755..790
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 796..831
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 439..473
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 901 AA; 103785 MW; 12A4E71AC3391CCC CRC64;
MVDYHAVNNQ GQYSAGGPPT YMEQENDWDR DLLLDPAWEK QQRKTFTAWC NSHLRKAGTQ
IENIEEDFRD GLKLMLLLEV ISGERLPKPE RGKMRVHKIN NVNKALDFIA SKGVKLVSIG
AEEIVDGNAK MTLGMIWTII LRFAIQDISV EETSAKEGLL LWCQRKTAPY KNVNVQNFHI
SWKDGLAFNA LIHRHRPELI DYDKLRKDDP VTNLNNAFEV AERYLDIPKM LDAEDIVNTA
RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYEK LASDLLEWIR
RTIPWLENRA PEKTMAEMQQ KLEDFRDYRR VHKPPKVQEK CQLEINFNTL QTKLRLSNRP
AFMPSEGRMV SDINGAWHKL EGAEKGYEEW LLNEIRRLER LDHLAEKFRQ KAAIHEGWTD
GKEAMLTQKD YETASLSEIK ALLKKHEAFE SDLAAHQDRV EQIAAIAQEL NELDYYDSPS
VNARCQKICE QWDALGSLTQ NRRESLERTE KQLESIDELY LEYAKRAAPF NNWMEGAMED
LQDMFIVHNI DEIQGLITAH EQFKSTLPEA NKEREAIQAI QAEVQKIANY NGIKLAGNNP
YTTITPQSID KKWEKVQQLV PQRDQALQEE LTRQQSNDHL RRQFANQANM IGPWIQNKME
EIGRISIEMN GTLEDQLTHL SQYEQSIIEY KPNIDQLEGD HQLIQEALIF DNKYTAYTME
HLRVGWEQLL TTIARTINEI ENQVLTRDAK GISQEQLHEY RTSFNHFDKD HSGLLQSEEF
KACLISLGYD VENDKQGDAE FARIMGIVDP NNSGAVTFQA FIDFMSRETT DTDTADQVIA
SFKILAGDKN YITAEELRRE LPPDQAEYCI ARMAPYSGPD AVAGALDYMS FSTALYGESD
L
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