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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

GO - Biological processi

  • ion transport Source: UniProtKB

Keywordsi

Molecular functionActin-binding
Biological processIon transport, Transport
LigandMetal-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000757641 – 263LIM and SH3 domain protein 1Add BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei42N6-acetyllysineBy similarity1
Modified residuei68PhosphothreonineBy similarity1
Modified residuei75N6-methyllysineBy similarity1
Modified residuei99PhosphoserineBy similarity1
Modified residuei104PhosphothreonineCombined sources1
Modified residuei112N6-succinyllysineBy similarity1
Modified residuei118PhosphoserineBy similarity1
Modified residuei134PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ99MZ8.
PRIDEiQ99MZ8.

PTM databases

iPTMnetiQ99MZ8.
PhosphoSitePlusiQ99MZ8.

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

BgeeiENSRNOG00000004132.
GenevisibleiQ99MZ8. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ99MZ8.
SMRiQ99MZ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 63LIM zinc-bindingPROSITE-ProRule annotationAdd BLAST61
Repeati64 – 95Nebulin 1Add BLAST32
Repeati97 – 131Nebulin 2Add BLAST35
Domaini204 – 263SH3PROSITE-ProRule annotationAdd BLAST60

Keywords - Domaini

LIM domain, Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG1702. Eukaryota.
ENOG4111GQ8. LUCA.
GeneTreeiENSGT00530000062924.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiQ99MZ8.
OMAiYGYKEPA.
OrthoDBiEOG091G0U2O.
PhylomeDBiQ99MZ8.

Family and domain databases

InterProiView protein in InterPro
IPR000900. Nebulin_repeat.
IPR001452. SH3_domain.
IPR001781. Znf_LIM.
PfamiView protein in Pfam
PF00412. LIM. 1 hit.
PF00880. Nebulin. 2 hits.
PF14604. SH3_9. 1 hit.
PRINTSiPR00452. SH3DOMAIN.
SMARTiView protein in SMART
SM00132. LIM. 1 hit.
SM00227. NEBU. 2 hits.
SM00326. SH3. 1 hit.
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiView protein in PROSITE
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
PS51216. NEBULIN. 2 hits.
PS50002. SH3. 1 hit.

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.

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.

Entry informationi

Entry nameiLASP1_RAT
AccessioniPrimary (citable) accession number: Q99MZ8
Secondary accession number(s): Q499R9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: July 5, 2017
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome