ID   B4DIC4_HUMAN            Unreviewed;       125 AA.
AC   B4DIC4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=LIM and SH3 domain protein 1 {ECO:0000256|ARBA:ARBA00020662};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG58436.1};
RN   [1] {ECO:0000313|EMBL:BAG58436.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hippocampus {ECO:0000313|EMBL:BAG58436.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00025477}.
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DR   EMBL; AK295522; BAG58436.1; -; mRNA.
DR   RefSeq; NP_001258537.1; NM_001271608.1.
DR   AlphaFoldDB; B4DIC4; -.
DR   MaxQB; B4DIC4; -.
DR   PeptideAtlas; B4DIC4; -.
DR   ProteomicsDB; 4294; -.
DR   DNASU; 3927; -.
DR   GeneID; 3927; -.
DR   CTD; 3927; -.
DR   OrthoDB; 4243at2759; -.
DR   BioGRID-ORCS; 3927; 16 hits in 1156 CRISPR screens.
DR   GenomeRNAi; 3927; -.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd09447; LIM_LASP; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   InterPro; IPR000900; Nebulin_repeat.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR46218; LASP; 1.
DR   PANTHER; PTHR46218:SF2; LIM AND SH3 DOMAIN PROTEIN 1; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00880; Nebulin; 1.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00227; NEBU; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS51216; NEBULIN; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          3..63
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
SQ   SEQUENCE   125 AA;  14598 MW;  900F5D3C3D145534 CRC64;
     MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
     SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRS SLGFLWNEIP
     PSPHL
//