ID A0A3Q4MAZ6_NEOBR Unreviewed; 375 AA.
AC A0A3Q4MAZ6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Actin, cytoplasmic 1-like {ECO:0000313|Ensembl:ENSNBRP00000005924.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005924.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000005924.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Actin is a highly conserved protein that polymerizes to
CC produce filaments that form cross-linked networks in the cytoplasm of
CC cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin)
CC forms, both forms playing key functions, such as cell motility and
CC contraction. In addition to their role in the cytoplasmic cytoskeleton,
CC G- and F-actin also localize in the nucleus, and regulate gene
CC transcription and motility and repair of damaged DNA.
CC {ECO:0000256|ARBA:ARBA00037523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix (By
CC similarity). Each actin can bind to 4 others.
CC {ECO:0000256|ARBA:ARBA00038685}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the actin family.
CC {ECO:0000256|RuleBase:RU000487}.
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DR RefSeq; XP_006798048.1; XM_006797985.1.
DR AlphaFoldDB; A0A3Q4MAZ6; -.
DR SMR; A0A3Q4MAZ6; -.
DR Ensembl; ENSNBRT00000006106.1; ENSNBRP00000005924.1; ENSNBRG00000004668.1.
DR GeneID; 102786573; -.
DR CTD; 57935; -.
DR GeneTree; ENSGT00950000182960; -.
DR OrthoDB; 5341931at2759; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000004668; Expressed in zone of skin and 9 other cell types or tissues.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF46; ACTIN-42A-RELATED; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 3: Inferred from homology;
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
SQ SEQUENCE 375 AA; 41767 MW; 9C505616D33E9495 CRC64;
MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKCF
//
