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Protein

LIM and SH3 domain protein 1

Gene

LASP1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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
Alternative name(s):
40 kDa phosphoprotein
Short name:
pp40
Gene namesi
Name:LASP1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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_0000223476Add
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 – 1041PhosphothreonineBy similarity
Modified residuei112 – 1121N6-succinyllysineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei146 – 1461PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on serine residues after stimulation with histamine.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiO77506.

PTM databases

iPTMnetiO77506.

Expressioni

Tissue specificityi

Widely expressed with highest levels in mucosal tissues throughout the gastrointestinal tract as well as in heart, lung, liver, kidney, adrenal and smooth muscle. Lowest level is observed in skeletal muscle.1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000022303.

Structurei

3D structure databases

ProteinModelPortaliO77506.
SMRiO77506. Positions 1-30, 205-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 5652LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati61 – 9535Nebulin 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.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiO77506.

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.

O77506-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK
60 70 80 90 100
PYCNAHYPKQ SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGRGFSV
110 120 130 140 150
VADTPELQRI KKTQDQISNI KYHEEFEKSR MGPSGGEGAE PERRDSQDSS
160 170 180 190 200
NYRRPPEQQQ PPQPHHIPTS TPAYQQPQPQ QVAQSYGYKE PAAPVSTQRG
210 220 230 240 250
APGGGGKRYR AVFDYSAADE DEVSFQDGDT IVNVQQIDDG WMYGTVERTG
260
DTGMLPANYV EAI
Length:263
Mass (Da):29,935
Last modified:November 1, 1998 - v1
Checksum:iF7FBD59E1CB88193
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017438 mRNA. Translation: AAC39264.1.
RefSeqiNP_001076247.1. NM_001082778.1.
UniGeneiOcu.6268.

Genome annotation databases

GeneIDi100009568.
KEGGiocu:100009568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017438 mRNA. Translation: AAC39264.1.
RefSeqiNP_001076247.1. NM_001082778.1.
UniGeneiOcu.6268.

3D structure databases

ProteinModelPortaliO77506.
SMRiO77506. Positions 1-30, 205-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000022303.

PTM databases

iPTMnetiO77506.

Proteomic databases

PRIDEiO77506.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009568.
KEGGiocu:100009568.

Organism-specific databases

CTDi3927.

Phylogenomic databases

eggNOGiKOG1702. Eukaryota.
ENOG4111GQ8. LUCA.
HOGENOMiHOG000006616.
HOVERGENiHBG054636.
InParanoidiO77506.

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

  1. "Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell."
    Chew C.S., Parente J.A. Jr., Zhou C.-J., Baranco E., Chen X.
    Am. J. Physiol. 275:C56-C67(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 128-133, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Strain: New Zealand white.
    Tissue: Gastric mucosa.

Entry informationi

Entry nameiLASP1_RABIT
AccessioniPrimary (citable) accession number: O77506
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 95 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.