CAPZA_CHATD
ID CAPZA_CHATD Reviewed; 274 AA.
AC P9WF01; G0SA92;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 25-MAY-2022, entry version 7.
DE RecName: Full=F-actin-capping protein subunit alpha {ECO:0000250|UniProtKB:Q10434};
GN ORFNames=CTHT_0041430, CTHT_0041430-2;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC to the fast growing ends of actin filaments (barbed end) thereby
CC blocking the exchange of subunits at these ends. Unlike other capping
CC proteins (such as gelsolin and severin), these proteins do not sever
CC actin filaments. {ECO:0000250|UniProtKB:Q10434}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000250|UniProtKB:Q10434}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10434}.
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS19664.1; Type=Erroneous gene model prediction; Note=The predicted gene CTHT_0041430 has been split into 2 genes: CTHT_0041430-1 and CTHT_0041430-2.; Evidence={ECO:0000305};
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DR EMBL; GL988043; EGS19664.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P9WF01; -.
DR SMR; P9WF01; -.
DR EnsemblFungi; EGS19664; EGS19664; CTHT_0041430.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051016; P:barbed-end actin filament capping; IEA:InterPro.
DR Gene3D; 3.30.1140.60; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR042489; CapZ_alpha_1.
DR InterPro; IPR017865; F-actin_cap_asu_CS.
DR PANTHER; PTHR10653; PTHR10653; 1.
DR Pfam; PF01267; F-actin_cap_A; 1.
DR PRINTS; PR00191; FACTINCAPA.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE 3: Inferred from homology;
KW Actin capping; Actin-binding; Cytoplasm; Reference proteome.
FT CHAIN 1..274
FT /note="F-actin-capping protein subunit alpha"
FT /id="PRO_0000450357"
SQ SEQUENCE 274 AA; 29939 MW; 66FF7DE23ED66DFF CRC64;
MTLQSQKAIL SSFIEGAPPG ELADVVADIK NLTSSTPNLI NELGPAFQKY NEEQFTTVKL
PGSSQHVIIS SHNSLGGSRY YDVETSTSFA FDHTTQKASA VETYVVEGAQ GDLTKSVIKA
LAPYVKEHYS NAAYGAWPIE NDSKVAIIIV ANKYSPNNYW NGRWRSLYIL DPAAGTVEGS
IKVDVHYYED GNVRLLTDKP VTASVSATGA AIVKEISAVE KKYQEELNRS FASLSEGAFK
ALRRQLPVTR QKIEWEKIAG YRLGQDIGGG GARR