ID  Q5RCS6;
PN  Alpha-actinin-4;
GN  ACTN4;
OS  9601;
SL  Nucleus Position: SL-0198;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:P57780}.
DR  UNIPROT: Q5RCS6;
DR  Pfam: PF00307;
DR  Pfam: PF08726;
DR  Pfam: PF00435;
DR  PROSITE: PS00019;
DR  PROSITE: PS00020;
DR  PROSITE: PS50021;
DR  PROSITE: PS00018;
DR  PROSITE: PS50222;
DE  Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA. {ECO:0000250|UniProtKB:O43707}.
DE  Reference Proteome: Yes;
GO  GO:0070161;
GO  GO:0005737;
GO  GO:0005856;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:1990904;
GO  GO:0003779;
GO  GO:0005509;
GO  GO:0030374;
GO  GO:0035357;
GO  GO:0015031;
GO  GO:0048384;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MVDYHAASQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRD
SQ  GLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISV
SQ  EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKM
SQ  LDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICRVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRV
SQ  PQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEW
SQ  LLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQEL
SQ  NELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTI
SQ  EEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEE
SQ  QSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIF
SQ  DNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYD
SQ  VENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCI
SQ  ARMAPYQGPDAVPGALDYKSFSTALYGESDL
//