PROF1_BOVIN
ID PROF1_BOVIN Reviewed; 140 AA.
AC P02584; Q3ZCH4; Q5E942;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Profilin-1;
DE AltName: Full=Profilin I;
GN Name=PFN1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-140, AND ACETYLATION AT ALA-2.
RC TISSUE=Spleen;
RX PubMed=446730; DOI=10.1016/0014-5793(79)81317-4;
RA Nystroem L.-E., Lindberg U., Kendrick-Jones J., Jakes R.;
RT "The amino acid sequence of profilin from calf spleen.";
RL FEBS Lett. 101:161-165(1979).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=3342873; DOI=10.1016/0014-5793(88)80575-1;
RA Ampe C., Markey F., Lindberg U., Vandekerckhove J.;
RT "The primary structure of human platelet profilin: reinvestigation of the
RT calf spleen profilin sequence.";
RL FEBS Lett. 228:17-21(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF COMPLEX WITH BETA-ACTIN.
RX PubMed=8413665; DOI=10.1038/365810a0;
RA Schutt C.E., Myslik J.C., Rozycki M.D., Goonesekere N.C.W., Lindberg U.;
RT "The structure of crystalline profilin-beta-actin.";
RL Nature 365:810-816(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF COMPLEX WITH BETA-ACTIN.
RX PubMed=8918942; DOI=10.1006/jmbi.1996.0602;
RA Chik J.K., Lindberg U., Schutt C.E.;
RT "The structure of an open state of beta-actin at 2.65-A resolution.";
RL J. Mol. Biol. 263:607-623(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8046751; DOI=10.1006/jmbi.1994.1461;
RA Cedergren-Zeppezauer E.S., Goonesekere N.C., Rozycki M.D., Myslik J.C.,
RA Dauter Z., Lindberg U., Schutt C.E.;
RT "Crystallization and structure determination of bovine profilin at 2.0-A
RT resolution.";
RL J. Mol. Biol. 240:459-475(1994).
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. Inhibits androgen receptor (AR)
CC and HTT aggregation and binding of G-actin is essential for its
CC inhibition of AR (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VASP. Occurs in many kinds of cells as a
CC complex with monomeric actin in a 1:1 ratio. Found in a complex with
CC XPO6, Ran, ACTB and PFN1 (By similarity). Interacts with HTT (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Phosphorylation at Ser-138 reduces its affinity for G-actin and
CC blocks its interaction with HTT, reducing its ability to inhibit
CC androgen receptor (AR) and HTT aggregation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; BT021078; AAX09095.1; -; mRNA.
DR EMBL; BC102240; AAI02241.1; -; mRNA.
DR PIR; S00308; FABO.
DR RefSeq; NP_001015592.1; NM_001015592.1.
DR PDB; 1HLU; X-ray; 2.65 A; P=2-140.
DR PDB; 1PNE; X-ray; 2.00 A; A=2-140.
DR PDB; 2BTF; X-ray; 2.55 A; P=2-140.
DR PDB; 3U4L; X-ray; 2.40 A; P=2-140.
DR PDB; 3UB5; X-ray; 2.20 A; P=2-140.
DR PDBsum; 1HLU; -.
DR PDBsum; 1PNE; -.
DR PDBsum; 2BTF; -.
DR PDBsum; 3U4L; -.
DR PDBsum; 3UB5; -.
DR AlphaFoldDB; P02584; -.
DR SMR; P02584; -.
DR BioGRID; 170522; 2.
DR DIP; DIP-17037N; -.
DR IntAct; P02584; 2.
DR STRING; 9913.ENSBTAP00000006465; -.
DR iPTMnet; P02584; -.
DR SwissPalm; P02584; -.
DR PaxDb; P02584; -.
DR PeptideAtlas; P02584; -.
DR PRIDE; P02584; -.
DR Ensembl; ENSBTAT00000006465; ENSBTAP00000006465; ENSBTAG00000004915.
DR GeneID; 513895; -.
DR KEGG; bta:513895; -.
DR CTD; 5216; -.
DR VEuPathDB; HostDB:ENSBTAG00000004915; -.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00940000153664; -.
DR HOGENOM; CLU_123405_1_0_1; -.
DR InParanoid; P02584; -.
DR OMA; NKKCFEM; -.
DR OrthoDB; 1428600at2759; -.
DR TreeFam; TF331744; -.
DR Reactome; R-BTA-376176; Signaling by ROBO receptors.
DR Reactome; R-BTA-4086400; PCP/CE pathway.
DR Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
DR EvolutionaryTrace; P02584; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000004915; Expressed in monocyte and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR029892; PFN1.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR005454; Profilin1/2/3_vertebrate.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR13936:SF14; PTHR13936:SF14; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:446730"
FT CHAIN 2..140
FT /note="Profilin-1"
FT /id="PRO_0000199570"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:3342873,
FT ECO:0000269|PubMed:446730"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62963"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT MOD_RES 138
FT /note="Phosphoserine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1PNE"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1PNE"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:1PNE"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1PNE"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1PNE"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:1PNE"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:1PNE"
SQ SEQUENCE 140 AA; 15057 MW; E56BFBB5BBB016E3 CRC64;
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGI LVGKDRSSFF
VNGLTLGGQK CSVIRDSLLQ DGEFTMDLRT KSTGGAPTFN ITVTMTAKTL VLLMGKEGVH
GGMINKKCYE MASHLRRSQY
