LASP1_RAT
ID LASP1_RAT Reviewed; 263 AA.
AC Q99MZ8; Q499R9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=LIM and SH3 domain protein 1;
DE Short=LASP-1;
GN Name=Lasp1 {ECO:0000312|RGD:68408};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAK28338.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chew C.S., Cameron P.A., Chen X., Cameron R.S.;
RT "Cloning of the lasp-1 ORF from primary cultures of rat type I
RT astrocytes.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000312|EMBL:AAK28338.1}
RP PROTEIN SEQUENCE OF 11-17; 97-109 AND 131-144, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=10806114; DOI=10.1242/jcs.113.11.2035;
RA Chew C.S., Parente J.A. Jr., Chen X., Chaponnier C., Cameron R.S.;
RT "The LIM and SH3 domain-containing protein, lasp-1, may link the cAMP
RT signaling pathway with dynamic membrane restructuring activities in ion
RT transporting epithelia.";
RL J. Cell Sci. 113:2035-2045(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000269|PubMed:10806114}.
CC -!- SUBUNIT: Interacts with F-actin. Interacts with ANKRD54. Interacts with
CC KBTBD10 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:10806114}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10806114}. Note=Associated with the F-actin rich
CC cortical cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues (but not the
CC heart or skeletal muscle), the expression is specific for certain
CC actin-rich cell types within these tissues. Expression is prominent in
CC the cortical regions of ion-transporting duct cells in the pancreas, in
CC the salivary parotid gland and in certain F-actin-rich cells in the
CC distal tubule/collecting duct. In primary cultures of gastric
CC fibroblasts, expression is mainly within the tips of lamellipodia and
CC at the leading edges of membrane ruffles.
CC {ECO:0000269|PubMed:10806114}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:10806114}.
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DR EMBL; AF242187; AAK28338.1; -; mRNA.
DR EMBL; BC099791; AAH99791.1; -; mRNA.
DR RefSeq; NP_116002.1; NM_032613.2.
DR AlphaFoldDB; Q99MZ8; -.
DR SMR; Q99MZ8; -.
DR BioGRID; 247949; 3.
DR IntAct; Q99MZ8; 8.
DR STRING; 10116.ENSRNOP00000005522; -.
DR iPTMnet; Q99MZ8; -.
DR PhosphoSitePlus; Q99MZ8; -.
DR jPOST; Q99MZ8; -.
DR PaxDb; Q99MZ8; -.
DR PRIDE; Q99MZ8; -.
DR Ensembl; ENSRNOT00000005522; ENSRNOP00000005522; ENSRNOG00000004132.
DR GeneID; 29278; -.
DR KEGG; rno:29278; -.
DR UCSC; RGD:68408; rat.
DR CTD; 3927; -.
DR RGD; 68408; Lasp1.
DR eggNOG; KOG1702; Eukaryota.
DR GeneTree; ENSGT00940000154775; -.
DR HOGENOM; CLU_026811_0_1_1; -.
DR InParanoid; Q99MZ8; -.
DR OMA; QIEYVEY; -.
DR OrthoDB; 1549538at2759; -.
DR PhylomeDB; Q99MZ8; -.
DR PRO; PR:Q99MZ8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004132; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q99MZ8; RN.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0015075; F:ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IDA:UniProtKB.
DR CDD; cd11934; SH3_Lasp1_C; 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 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; SSF50044; SSF50044; 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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Ion transport; LIM domain; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW Transport; Zinc.
FT CHAIN 1..263
FT /note="LIM and SH3 domain protein 1"
FT /id="PRO_0000075764"
FT DOMAIN 3..63
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REPEAT 64..95
FT /note="Nebulin 1"
FT REPEAT 97..131
FT /note="Nebulin 2"
FT DOMAIN 204..263
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 122..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 75
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 112
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61792"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
SQ SEQUENCE 263 AA; 29970 MW; 63D416C4FA8B0744 CRC64;
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI
KYHEEFEKSR MGPSGGEGIE PERREAQDSS SYRRPTEQQQ PQPHHIPTSA PVYQQPQQQQ
VTPSYGGYKE PAAPVSIQRS APGGGGKRYR AVYDYSAADE DEVSFQDGDT IVNVQQIDDG
WMYGTVERTG DTGMLPANYV EAI
