ACTN4_PONAB
ID ACTN4_PONAB Reviewed; 911 AA.
AC Q5RCS6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alpha-actinin-4 {ECO:0000305};
DE AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000305};
GN Name=ACTN4 {ECO:0000305};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858192; CAH90431.1; -; mRNA.
DR RefSeq; NP_001127286.1; NM_001133814.1.
DR AlphaFoldDB; Q5RCS6; -.
DR BMRB; Q5RCS6; -.
DR SMR; Q5RCS6; -.
DR STRING; 9601.ENSPPYP00000011127; -.
DR PRIDE; Q5RCS6; -.
DR GeneID; 100174343; -.
DR KEGG; pon:100174343; -.
DR CTD; 81; -.
DR eggNOG; KOG0035; Eukaryota.
DR InParanoid; Q5RCS6; -.
DR OrthoDB; 543832at2759; -.
DR Proteomes; UP000001595; Unplaced.
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_0000073442"
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 1..30
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 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; 104855 MW; F210BC2DC206FF0D CRC64;
MVDYHAASQS YQYGPSSAGN GAGGGGSMGD 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 ICRVLAVNQE NEHLMEDYEK
LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK CQLEINFNTL
QTKLRLSNRP AFMPSEGKMV SDINNGWQHL EQAEKGYEEW LLNEIRRLER LDHLAEKFRQ
KASIHEAWTD GKEAMLKHRD YETATLSDIK ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL
NELDYYDSHN VNTRCQKICD QWDALGSLTH SRREALEKTE KQLEAIDQLH LEYAKRAAPF
NNWMESAMED LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES
NHIKLSGSNP YTTVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL RRQFASQANV
VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY KPNLDLLEQQ HQLIQEALIF
DNKHTNYTME HIRVGWEQLL TTIARTINEV ENQILTRDAK GISQEQMQEF RASFNHFDKD
HGGALGPEEF KACLISLGYD VENDRQGEAE FNRIMSLVDP NHSGLVTFQA FIDFMSRETT
DTDTADQVIA SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AVPGALDYKS
FSTALYGESD L
