PROF2_PONAB
ID PROF2_PONAB Reviewed; 140 AA.
AC Q5R4E2; Q5R4Z2; Q5R6D9; Q5R7C6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Profilin-2;
DE AltName: Full=Profilin II;
GN Name=PFN2;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, Heart, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC At high concentrations, profilin prevents the polymerization of actin,
CC whereas it enhances it at low concentrations. By binding to PIP2, it
CC inhibits the formation of IP3 and DG (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio (By similarity). Interacts with PFN2 (By
CC similarity). {ECO:0000250|UniProtKB:P35080,
CC ECO:0000250|UniProtKB:Q9JJV2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R4E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R4E2-2; Sequence=VSP_017822;
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; CR858725; CAH90934.1; -; mRNA.
DR EMBL; CR859236; CAH91416.1; -; mRNA.
DR EMBL; CR860192; CAH92334.1; -; mRNA.
DR EMBL; CR860552; CAH92677.1; -; mRNA.
DR EMBL; CR861095; CAH93174.1; -; mRNA.
DR EMBL; CR861308; CAH93374.1; -; mRNA.
DR RefSeq; NP_001126567.1; NM_001133095.1.
DR RefSeq; NP_001128792.1; NM_001135320.1. [Q5R4E2-2]
DR AlphaFoldDB; Q5R4E2; -.
DR BMRB; Q5R4E2; -.
DR SMR; Q5R4E2; -.
DR STRING; 9601.ENSPPYP00000015884; -.
DR GeneID; 100173558; -.
DR GeneID; 100189697; -.
DR KEGG; pon:100173558; -.
DR CTD; 5217; -.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_123405_1_0_1; -.
DR InParanoid; Q5R4E2; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR029891; PFN2.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR005454; Profilin1/2/3_vertebrate.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR13936:SF15; PTHR13936:SF15; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01639; PROFILINMAML.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35080"
FT CHAIN 2..140
FT /note="Profilin-2"
FT /id="PRO_0000199577"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35080"
FT VAR_SEQ 109..140
FT /note="VLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF -> ALVIVMGKEGVHGGTL
FT NKKAYELALYLRRSDV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017822"
FT CONFLICT 9
FT /note="D -> G (in Ref. 1; CAH92677)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="L -> S (in Ref. 1; CAH93174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 15046 MW; F43884E1427C9A99 CRC64;
MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF
TNGLTLGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH
GGGLNKKAYS MAKYLRDSGF