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Protein

LIM and SH3 domain protein 1

Gene

Lasp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types.1 Publication

GO - Molecular functioni

  • ion transmembrane transporter activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • ion transmembrane transport Source: GOC
  • ion transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
LIM and SH3 domain protein 1
Short name:
LASP-1
Gene namesi
Name:Lasp1Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi68408. Lasp1.

Subcellular locationi

  • Cytoplasmcell cortex 1 Publication
  • Cytoplasmcytoskeleton 1 Publication

  • Note: Associated with the F-actin rich cortical cytoskeleton.

GO - Cellular componenti

  • cortical actin cytoskeleton Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263LIM and SH3 domain protein 1PRO_0000075764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei68 – 681PhosphothreonineBy similarity
Modified residuei104 – 1041PhosphothreonineCombined sources
Modified residuei112 – 1121N6-succinyllysineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ99MZ8.
PRIDEiQ99MZ8.

PTM databases

iPTMnetiQ99MZ8.
PhosphoSiteiQ99MZ8.

Expressioni

Tissue specificityi

Expressed in a wide range of tissues (but not the heart or skeletal muscle), the expression is specific for certain actin-rich cell types within these tissues. Expression is prominent in the cortical regions of ion-transporting duct cells in the pancreas, in the salivary parotid gland and in certain F-actin-rich cells in the distal tubule/collecting duct. In primary cultures of gastric fibroblasts, expression is mainly within the tips of lamellipodia and at the leading edges of membrane ruffles.1 Publication

Gene expression databases

GenevisibleiQ99MZ8. RN.

Interactioni

Subunit structurei

Interacts with F-actin. Interacts with ANKRD54. Interacts with KBTBD10 (By similarity).By similarity

Protein-protein interaction databases

BioGridi247949. 1 interaction.
IntActiQ99MZ8. 1 interaction.
MINTiMINT-4579484.
STRINGi10116.ENSRNOP00000005522.

Structurei

3D structure databases

ProteinModelPortaliQ99MZ8.
SMRiQ99MZ8. Positions 1-30, 205-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 6361LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati64 – 9532Nebulin 1Add
BLAST
Repeati97 – 13135Nebulin 2Add
BLAST
Domaini204 – 26360SH3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation
Contains 2 nebulin repeats.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG1702. Eukaryota.
ENOG4111GQ8. LUCA.
GeneTreeiENSGT00530000062924.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiQ99MZ8.
OMAiYGYKEPA.
OrthoDBiEOG771280.
PhylomeDBiQ99MZ8.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99MZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK
60 70 80 90 100
PYCNAHYPKQ SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV
110 120 130 140 150
VADTPELQRI KKTQDQISNI KYHEEFEKSR MGPSGGEGIE PERREAQDSS
160 170 180 190 200
SYRRPTEQQQ PQPHHIPTSA PVYQQPQQQQ VTPSYGGYKE PAAPVSIQRS
210 220 230 240 250
APGGGGKRYR AVYDYSAADE DEVSFQDGDT IVNVQQIDDG WMYGTVERTG
260
DTGMLPANYV EAI
Length:263
Mass (Da):29,970
Last modified:June 1, 2001 - v1
Checksum:i63D416C4FA8B0744
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242187 mRNA. Translation: AAK28338.1.
BC099791 mRNA. Translation: AAH99791.1.
RefSeqiNP_116002.1. NM_032613.2.
UniGeneiRn.94195.

Genome annotation databases

EnsembliENSRNOT00000005522; ENSRNOP00000005522; ENSRNOG00000004132.
GeneIDi29278.
KEGGirno:29278.
UCSCiRGD:68408. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF242187 mRNA. Translation: AAK28338.1.
BC099791 mRNA. Translation: AAH99791.1.
RefSeqiNP_116002.1. NM_032613.2.
UniGeneiRn.94195.

3D structure databases

ProteinModelPortaliQ99MZ8.
SMRiQ99MZ8. Positions 1-30, 205-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247949. 1 interaction.
IntActiQ99MZ8. 1 interaction.
MINTiMINT-4579484.
STRINGi10116.ENSRNOP00000005522.

PTM databases

iPTMnetiQ99MZ8.
PhosphoSiteiQ99MZ8.

Proteomic databases

PaxDbiQ99MZ8.
PRIDEiQ99MZ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005522; ENSRNOP00000005522; ENSRNOG00000004132.
GeneIDi29278.
KEGGirno:29278.
UCSCiRGD:68408. rat.

Organism-specific databases

CTDi3927.
RGDi68408. Lasp1.

Phylogenomic databases

eggNOGiKOG1702. Eukaryota.
ENOG4111GQ8. LUCA.
GeneTreeiENSGT00530000062924.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiQ99MZ8.
OMAiYGYKEPA.
OrthoDBiEOG771280.
PhylomeDBiQ99MZ8.

Miscellaneous databases

PROiQ99MZ8.

Gene expression databases

GenevisibleiQ99MZ8. RN.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the lasp-1 ORF from primary cultures of rat type I astrocytes."
    Chew C.S., Cameron P.A., Chen X., Cameron R.S.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-17; 97-109 AND 131-144, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "The LIM and SH3 domain-containing protein, lasp-1, may link the cAMP signaling pathway with dynamic membrane restructuring activities in ion transporting epithelia."
    Chew C.S., Parente J.A. Jr., Chen X., Chaponnier C., Cameron R.S.
    J. Cell Sci. 113:2035-2045(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLASP1_RAT
AccessioniPrimary (citable) accession number: Q99MZ8
Secondary accession number(s): Q499R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.