GenomeNet

Database: UniProt
Entry: F7DTH8_MONDO
LinkDB: F7DTH8_MONDO
Original site: F7DTH8_MONDO 
ID   F7DTH8_MONDO            Unreviewed;       912 AA.
AC   F7DTH8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 87.
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:ENSMODP00000016717.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000016717.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000016717.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000016717.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_001362530.1; XM_001362493.3.
DR   AlphaFoldDB; F7DTH8; -.
DR   Ensembl; ENSMODT00000017027.4; ENSMODP00000016717.3; ENSMODG00000013370.4.
DR   GeneID; 100010983; -.
DR   KEGG; mdo:100010983; -.
DR   CTD; 81; -.
DR   eggNOG; KOG0035; Eukaryota.
DR   GeneTree; ENSGT00940000159343; -.
DR   HOGENOM; CLU_005217_1_1_1; -.
DR   OrthoDB; 2872403at2759; -.
DR   TreeFam; TF352676; -.
DR   Proteomes; UP000002280; Chromosome 4.
DR   Bgee; ENSMODG00000013370; Expressed in adult mammalian kidney and 18 other cell types or tissues.
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; 3.
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   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:UP000002280};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          51..155
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          164..270
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          766..801
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          807..842
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          450..484
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   912 AA;  104474 MW;  885893DC8DEEE892 CRC64;
     MVDYHAANQP YQYGPSSGGG GGNGGGGGVG DYMAQEDDWD RDLLLDPAWE KQQRKTFTAW
     CNSHLRKAGT QIENIDEDFR DGLKLMLLLE VISGERLPKP ERGKMRVHKI NNVNKALDFI
     ASKGVKLVSI GAEEIVDGNA KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP
     YKNVNVQNFH ISWKDGLAFN ALIHRHRPEL IEYDKLRKDD PVTNLNNAFE VAEKYLDIPK
     MLDAEDIVNT ARPDEKAIMT YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEHLMEDYE
     KLASDLLEWI RRTIPWLEDR VPQKTIQEMQ QKLEDFRDYR RVHKPPKVQE KCQLEINFNT
     LQTKLRLSNR PAFMPSEGKM VSDINNCWQH LEQAEKGFEE WLLNVIRRLE RLDHLGEKFG
     QKASIHEAWT DGKEAMLKQK DYETATLSDI KALIRKHEAF ESDLAAHQDR VEQIAAIAQE
     LNELDYYDSP SVNTRCQKIC DQWDALGSLT HSRREALEKT EKQLETIDQL HLEYAKRAAP
     FNNWMESAME DLQDMFIVHT IEEIEGLIAA HDQFKSTLPD ADKEREAILA IHGEAQKIAE
     CNHIKLLGSN PYTTVTPQII NSKWEKVQQL VPKRDDALLE EQSKQQSNER LRRQFASQAN
     IVGPWIQTKM EEIGRISIEM NGTLEDQLNH LKQYEQSIVD YKPNLDLLEQ QHQLIQEALI
     FDNKHTNYTM EHIRVGWEQL LTTIARTINE VENQILTRDA KGISQEQMQE FRASFNHFDK
     DHGGALGPEE FKACLISLGY DVENDRQGDA EFNRIMSVVD PNNSGIVTFQ AFIDFMSRET
     TDTDTADQVI ASFKVLAGDK NFITAEELRR ELPPDQAEYC IARMAPYQGP DAAPGALDYK
     SFSTALYGES DL
//
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