ID A0A3B4G541_9CICH Unreviewed; 235 AA.
AC A0A3B4G541;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=LIM and SH3 domain protein 1 {ECO:0000256|ARBA:ARBA00020662};
GN Name=lasp1 {ECO:0000313|RefSeq:XP_005726214.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000016858.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000016858.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005726214.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005726214.1; XM_005726157.1.
DR AlphaFoldDB; A0A3B4G541; -.
DR STRING; 303518.ENSPNYP00000016858; -.
DR Ensembl; ENSPNYT00000017279.1; ENSPNYP00000016858.1; ENSPNYG00000012785.1.
DR GeneID; 102203403; -.
DR CTD; 3927; -.
DR GeneTree; ENSGT00940000154775; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
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 GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd09447; LIM_LASP; 1.
DR CDD; cd11934; SH3_Lasp1_C; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035630; Lasp1_SH3.
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; PF00018; SH3_1; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
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:UP000695023};
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 176..235
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 131..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 235 AA; 26729 MW; 04078938E686DCE2 CRC64;
MNPLCSRCNL VVYPTEKVNC LDKYWHKGCF SCEVCKMTLN MKNYKGFEKR PYCNAHYPKS
SFTCVTDTPE NLRLKQQSKI QSQVLYREDF EKNKGKGFSV VADTPEMQRI KKTQDQISNI
KYHEEFEKKK IGGEGPQHLP SNPSAGGYQQ PAATQNYHYD PAPEPVRQAA AAPPPSAGKR
YRAVYDYSAA DEDEVSFMDG DVIVDVQQID EGWMYGRVER TGQQGMLPAN YVEAI
//
