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Database: UniProt
Entry: H9GX78_DANRE
LinkDB: H9GX78_DANRE
Original site: H9GX78_DANRE 
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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