LASP1_PIG
ID LASP1_PIG Reviewed; 30 AA.
AC P80171;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=LIM and SH3 domain protein 1;
DE Short=LASP-1;
DE AltName: Full=Cysteine-rich peptide ZF-1;
DE Flags: Fragment;
GN Name=LASP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Intestine;
RX PubMed=8425549; DOI=10.1111/j.1432-1033.1993.tb19908.x;
RA Sillard R., Joernvall H., Carlquist M., Mutt V.;
RT "Chemical assay for cyst(e)ine-rich peptides detects a novel intestinal
RT peptide ZF-1, homologous to a single zinc-finger motif.";
RL Eur. J. Biochem. 211:377-380(1993).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=8841116; DOI=10.1021/bi961149j;
RA Hammarstroem A., Berndt K.D., Sillard R., Adermann K., Otting G.;
RT "Solution structure of a naturally-occurring zinc-peptide complex
RT demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM
RT domain is an independent folding unit.";
RL Biochemistry 35:12723-12732(1996).
CC -!- FUNCTION: Plays an important role in the regulation of dynamic actin-
CC based, cytoskeletal activities. Agonist-dependent changes in LASP1
CC phosphorylation may also serve to regulate actin-associated ion
CC transport activities, not only in the parietal cell but also in certain
CC other F-actin-rich secretory epithelial cell types (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin (By similarity). Interacts with
CC ANKRD54. Interacts with KBTBD10 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Associated with the F-actin rich
CC cortical cytoskeleton. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR PIR; S28849; S28849.
DR PDB; 1ZFO; NMR; -; A=1-30.
DR PDBsum; 1ZFO; -.
DR AlphaFoldDB; P80171; -.
DR SMR; P80171; -.
DR iPTMnet; P80171; -.
DR PeptideAtlas; P80171; -.
DR PRIDE; P80171; -.
DR InParanoid; P80171; -.
DR EvolutionaryTrace; P80171; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0015075; F:ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Ion transport; LIM domain; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transport; Zinc.
FT CHAIN 1..>30
FT /note="LIM and SH3 domain protein 1"
FT /id="PRO_0000075763"
FT DOMAIN 5..>30
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:8425549"
FT NON_TER 30
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1ZFO"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1ZFO"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1ZFO"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1ZFO"
SQ SEQUENCE 30 AA; 3517 MW; 042AB8FBE2314986 CRC64;
MNPNCARCGK IVYPTEKVNC LDKFWHKACF
