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ACTN4_BOVIN
ID   ACTN4_BOVIN             Reviewed;         911 AA.
AC   A5D7D1;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Alpha-actinin-4 {ECO:0000305};
DE   AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000305};
GN   Name=ACTN4 {ECO:0000305};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC       actin to a variety of intracellular structures. This is a bundling
CC       protein. Probably involved in vesicular trafficking via its association
CC       with the CART complex. The CART complex is necessary for efficient
CC       transferrin receptor recycling but not for EGFR degradation. Involved
CC       in tight junction assembly in epithelial cells probably through
CC       interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and
CC       recruits it to the tight junctions. May also function as a
CC       transcriptional coactivator, stimulating transcription mediated by the
CC       nuclear hormone receptors PPARG and RARA.
CC       {ECO:0000250|UniProtKB:O43707}.
CC   -!- SUBUNIT: Homodimer; antiparallel. Identified in a IGF2BP1-dependent
CC       mRNP granule complex containing untranslated mRNAs (By similarity).
CC       Component of the CART complex, at least composed of ACTN4, HGS/HRS,
CC       MYO5B and TRIM3 (By similarity). Binds TRIM3 at the N-terminus (By
CC       similarity). Interacts with MAGI1 (By similarity). Interacts with
CC       PDLIM2 (By similarity). Identified in a complex with CASK, IQGAP1,
CC       MAGI2, NPHS1, SPTAN1 and SPTBN1 (By similarity). Interacts with MICALL2
CC       (preferentially in opened conformation); stimulated by RAB13
CC       activation. Interacts with PPARG and RARA (By similarity). Binds to
CC       VCL; this interaction triggers VCL conformational changes (By
CC       similarity). Interacts with SEPTIN14 (By similarity).
CC       {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:P57780,
CC       ECO:0000250|UniProtKB:Q9QXQ0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O43707}. Cell junction
CC       {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber
CC       {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs. Expressed in the perinuclear
CC       rim and manchette structure in early elongating spermatids during
CC       spermiogenesis (By similarity). {ECO:0000250|UniProtKB:O43707,
CC       ECO:0000250|UniProtKB:P57780}.
CC   -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif that mediates
CC       interaction with nuclear receptors. {ECO:0000250|UniProtKB:O43707}.
CC   -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR   EMBL; BC140512; AAI40513.1; -; mRNA.
DR   RefSeq; NP_001091521.1; NM_001098052.1.
DR   AlphaFoldDB; A5D7D1; -.
DR   BMRB; A5D7D1; -.
DR   SMR; A5D7D1; -.
DR   IntAct; A5D7D1; 2.
DR   STRING; 9913.ENSBTAP00000014894; -.
DR   PaxDb; A5D7D1; -.
DR   PeptideAtlas; A5D7D1; -.
DR   PRIDE; A5D7D1; -.
DR   Ensembl; ENSBTAT00000086063; ENSBTAP00000060553; ENSBTAG00000011215.
DR   GeneID; 522269; -.
DR   KEGG; bta:522269; -.
DR   CTD; 81; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011215; -.
DR   VGNC; VGNC:25583; ACTN4.
DR   eggNOG; KOG0035; Eukaryota.
DR   GeneTree; ENSGT00940000159343; -.
DR   HOGENOM; CLU_005217_1_1_1; -.
DR   InParanoid; A5D7D1; -.
DR   OMA; INTAWHT; -.
DR   OrthoDB; 543832at2759; -.
DR   TreeFam; TF352676; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000011215; Expressed in placenta and 106 other tissues.
DR   ExpressionAtlas; A5D7D1; baseline and differential.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR   GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd00014; CH; 2.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd00176; SPEC; 3.
DR   Gene3D; 1.10.418.10; -; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
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   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; SM00150; SPEC; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Calcium; Cell junction; Cytoplasm;
KW   Cytoskeleton; Metal-binding; Nucleus; Phosphoprotein; Protein transport;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..911
FT                   /note="Alpha-actinin-4"
FT                   /id="PRO_0000312775"
FT   DOMAIN          50..154
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          163..269
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          293..403
FT                   /note="Spectrin 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          413..518
FT                   /note="Spectrin 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          528..639
FT                   /note="Spectrin 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          649..752
FT                   /note="Spectrin 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          765..800
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          806..841
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..269
FT                   /note="Actin-binding"
FT   REGION          8..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          12..26
FT                   /note="Interaction with VCL"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   REGION          40..61
FT                   /note="Interaction with VCL"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   REGION          108..126
FT                   /note="Interaction with VCL"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   REGION          177..192
FT                   /note="Polyphosphoinositide (PIP2)-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          736..911
FT                   /note="Mediates interaction with MICALL2"
FT                   /evidence="ECO:0000250|UniProtKB:P57780"
FT   MOTIF           84..88
FT                   /note="LXXLL motif"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         778
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         780
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         789
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         31
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P12814"
FT   MOD_RES         114
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   MOD_RES         214
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P12814"
FT   MOD_RES         249
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   MOD_RES         592
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   MOD_RES         625
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43707"
FT   MOD_RES         696
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12814"
FT   MOD_RES         779
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P57780"
FT   MOD_RES         859
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P57780"
FT   MOD_RES         909
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1P2"
SQ   SEQUENCE   911 AA;  104928 MW;  78BBD1E1F8F935D6 CRC64;
     MVDYHAANQS YQYGPSSGSN GAGGGGTMGD YMAQEDDWDR DLLLDPAWEK QQRKTFTAWC
     NSHLRKAGTQ IENIDEDFRD GLKLMLLLEV ISGERLPKPE RGKMRVHKIN NVNKALDFIA
     SKGVKLVSIG AEEIVDGNAK MTLGMIWTII LRFAIQDISV EETSAKEGLL LWCQRKTAPY
     KNVNVQNFHI SWKDGLAFNA LIHRHRPELI EYDKLRKDDP VTNLNNAFEV AEKYLDIPKM
     LDAEDIVNTA RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYER
     LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK CQLEINFNTL
     QTKLRLSNRP AFMPSEGKMV SDINNGWQHL EQAEKGYEEW LLNEIRRLER LDHLAEKFRQ
     KASIHEAWTD GKEAMLKHRD YETATLSDIK ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL
     NELDYYDSHN VNTRCQKICD QWDALGSLTH SRREALEKTE KQLETIDQLH LEYAKRAAPF
     NNWMESAMED LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES
     NHIKLSGSNP YTTVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL RRQFASQANI
     VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY KPNLDLLEQQ HQLIQEALIF
     DNKHTNYTME HIRVGWEQLL TTIARTINEV ENQILTRDAK GISQEQMQEF RASFNHFDKD
     HGGALGPEEF KACLISLGYD VENDRQGDAE FNRIMSVVDP NHSGLVTFQA FIDFMSRETT
     DTDTADQVIA SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AVPGALDYKS
     FSTALYGESD L
 
 
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