ID A0A3P9P445_POERE Unreviewed; 229 AA.
AC A0A3P9P445;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=LIM and SH3 domain protein 1 {ECO:0000256|ARBA:ARBA00020662};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000016574.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000016574.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000016574.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_008435546.1; XM_008437324.2.
DR AlphaFoldDB; A0A3P9P445; -.
DR Ensembl; ENSPRET00000016753.1; ENSPREP00000016574.1; ENSPREG00000011220.1.
DR GeneID; 103481683; -.
DR KEGG; pret:103481683; -.
DR GeneTree; ENSGT00940000154775; -.
DR OMA; MHMERSC; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000011220; Expressed in caudal fin and 1 other cell type or tissue.
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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000900; Nebulin_repeat.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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; 2.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00227; NEBU; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS51216; NEBULIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; 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"
FT DOMAIN 170..229
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 126..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 26179 MW; 3127FE37F4C618F1 CRC64;
MNPPCGRCNK PVYPTEKINC LDKYWHKGCF SCEVCKMALS MNNYKGFEKK PYCTMHYPKS
SFTIVTDTPE NLRLKQQSLL NSQALYKEDF EKNKGKGFSV VVDTPEMQRL KKTQDQISNI
KYHEEFEKSK IRSDAPPPEN RQEQELQESN PERFNQPAGQ MRPAVASPPS GGKRYQALYS
YVAAEADEVS LQEGDLVSDV EPIDEGWMFG CNQRTGKKGM LPANYVRPI
//
