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   04-NOV-2026, entry version 168.
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 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 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.
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). May act as a host antiviral
CC       restriction factor against Kaposi sarcoma-associated herpesvirus
CC       through SQSTM1/p62-mediated selective autophagy.
CC       {ECO:0000250|UniProtKB:P07737}.
CC   -!- SUBUNIT: Found in a complex with XPO6, Ran, ACTB and PFN1 (By
CC       similarity). Interacts with ACTB (By similarity). Interacts with VASP
CC       (By similarity). Interacts with HTT (By similarity). Interacts with
CC       SH3BGRL (By similarity). Occurs in many kinds of cells as a complex
CC       with monomeric actin in a 1:1 ratio (By similarity). Interacts with
CC       ACTMAP (By similarity). Interacts with SQSTM1 (By similarity).
CC       {ECO:0000250|UniProtKB:P07737}.
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   -!- PTM: Polyubiquitinated on Lys-116 by TRIM37; ubiquitination serves as a
CC       signal for the recognition of SQSTM1. {ECO:0000250|UniProtKB:P07737}.
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   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; 9913-ENSBTAP00000006465; -.
DR   PeptideAtlas; P02584; -.
DR   Ensembl; ENSBTAT00000006465.6; ENSBTAP00000006465.4; ENSBTAG00000004915.6.
DR   Ensembl; ENSBTAT00085047189; ENSBTAP00085029584; ENSBTAG00085030518.
DR   Ensembl; ENSBTAT00090082287; ENSBTAP00090046595; ENSBTAG00090038632.
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; AAAPGXG; -.
DR   OrthoDB; 421374at2759; -.
DR   Reactome; R-BTA-4086400; PCP/CE pathway.
DR   Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
DR   EvolutionaryTrace; P02584; -.
DR   PRO; PR:P02584; -.
DR   Bgee; ENSBTAG00000004915; Expressed in monocyte and 106 other cell types or tissues.
DR   CDD; cd00148; PROF; 1.
DR   FunFam; 3.30.450.30:FF:000008; Profilin; 1.
DR   Gene3D; 3.30.450.30; Dynein light chain 2a, cytoplasmic; 1.
DR   InterPro; IPR048278; PFN.
DR   InterPro; IPR005455; PFN_euk.
DR   InterPro; IPR036140; PFN_sf.
DR   InterPro; IPR005454; Profilin1/2/3_vertebrate.
DR   InterPro; IPR027310; Profilin_CS.
DR   PANTHER; PTHR13936; PROFILIN; 1.
DR   PANTHER; PTHR13936:SF14; PROFILIN-1; 1.
DR   Pfam; PF00235; Profilin; 1.
DR   PRINTS; PR00392; PROFILIN.
DR   PRINTS; PR01639; PROFILINMAML.
DR   SMART; SM00392; PROF; 1.
DR   SUPFAM; SSF55770; Profilin (actin-binding protein); 1.
DR   PROSITE; PS00414; PROFILIN; 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IBA:GO_Central.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR   Proteomes; UP000009136; Chromosome 19.
DR   AlphaFoldDB; P02584; -.
DR   MDposit; P02584; -.
DR   FunCoup; P02584; 1346.
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   CROSSLNK        116
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
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
//