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Entry version 170 (12 Aug 2020)
Sequence version 2 (10 May 2005)
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Protein

Laminin subunit alpha

Gene

LanA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Activates presynaptic signaling involving integrin alpha-PS3/beta-nu and Fak to suppress neuromuscular junction (NMJ) growth during larval development and during low crawling activity, but not during higher-crawling conditions. Mediates, together with integrin alpha-PS3/beta-nu, glutamate receptor-modulated NMJ growth.2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-3000157, Laminin interactions

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Laminin subunit alpha
Alternative name(s):
Laminin A chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LanA
Synonyms:lamA
ORF Names:CG10236
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0002526, LanA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Cell junction, Cell projection, Cytoplasmic vesicle, Extracellular matrix, Secreted, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Flies show late embryonic lethality. Certain partial loss-of-function mutations give raise to escaper adults, which have rough eyes associated with changes in cell fate and pattern, misshappen legs and defects in wing structure.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22Sequence analysisAdd BLAST22
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001706423 – 3712Laminin subunit alphaAdd BLAST3690

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi116N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi219N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi273 ↔ 282By similarity
Disulfide bondi275 ↔ 296By similarity
Disulfide bondi298 ↔ 307By similarity
Disulfide bondi310 ↔ 330By similarity
Disulfide bondi333 ↔ 342By similarity
Disulfide bondi335 ↔ 367By similarity
Disulfide bondi370 ↔ 379By similarity
Disulfide bondi382 ↔ 400By similarity
Glycosylationi395N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi403 ↔ 414By similarity
Disulfide bondi405 ↔ 421By similarity
Disulfide bondi423 ↔ 432By similarity
Disulfide bondi435 ↔ 445By similarity
Disulfide bondi448 ↔ 460By similarity
Disulfide bondi450 ↔ 468By similarity
Glycosylationi453N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi470 ↔ 479By similarity
Disulfide bondi482 ↔ 492By similarity
Disulfide bondi495 ↔ 507By similarity
Disulfide bondi497 ↔ 514By similarity
Glycosylationi508N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi528 ↔ 538By similarity
Disulfide bondi541 ↔ 553By similarity
Disulfide bondi543 ↔ 560By similarity
Disulfide bondi562 ↔ 571By similarity
Disulfide bondi574 ↔ 584By similarity
Disulfide bondi587 ↔ 599By similarity
Glycosylationi588N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi589 ↔ 605By similarity
Disulfide bondi607 ↔ 616By similarity
Disulfide bondi619 ↔ 629By similarity
Disulfide bondi632 ↔ 644By similarity
Disulfide bondi634 ↔ 650By similarity
Disulfide bondi652 ↔ 661By similarity
Disulfide bondi664 ↔ 674By similarity
Disulfide bondi677 ↔ 691By similarity
Disulfide bondi679 ↔ 700By similarity
Disulfide bondi702 ↔ 711By similarity
Disulfide bondi714 ↔ 729By similarity
Glycosylationi722N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi732 ↔ 746By similarity
Disulfide bondi734 ↔ 753By similarity
Disulfide bondi755 ↔ 764By similarity
Disulfide bondi767 ↔ 782By similarity
Disulfide bondi785 ↔ 797By similarity
Disulfide bondi787 ↔ 804By similarity
Disulfide bondi806 ↔ 815By similarity
Glycosylationi897N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1352N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1375 ↔ 1387By similarity
Disulfide bondi1377 ↔ 1394By similarity
Disulfide bondi1396 ↔ 1405By similarity
Disulfide bondi1408 ↔ 1418By similarity
Disulfide bondi1421 ↔ 1429By similarity
Disulfide bondi1423 ↔ 1436By similarity
Disulfide bondi1438 ↔ 1447By similarity
Disulfide bondi1450 ↔ 1463By similarity
Disulfide bondi1466 ↔ 1480By similarity
Disulfide bondi1468 ↔ 1487By similarity
Glycosylationi1484N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1489 ↔ 1498By similarity
Disulfide bondi1501 ↔ 1511By similarity
Disulfide bondi1514 ↔ 1526By similarity
Disulfide bondi1516 ↔ 1533By similarity
Disulfide bondi1535 ↔ 1544By similarity
Disulfide bondi1547 ↔ 1562By similarity
Glycosylationi1583N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1617N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1778 ↔ 1787By similarity
Disulfide bondi1790 ↔ 1806By similarity
Disulfide bondi1809 ↔ 1818By similarity
Disulfide bondi1811 ↔ 1825By similarity
Disulfide bondi1828 ↔ 1837By similarity
Disulfide bondi1840 ↔ 1856By similarity
Glycosylationi1847N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1859 ↔ 1874By similarity
Disulfide bondi1861 ↔ 1885By similarity
Disulfide bondi1887 ↔ 1896By similarity
Disulfide bondi1899 ↔ 1914By similarity
Disulfide bondi1917 ↔ 1931By similarity
Disulfide bondi1919 ↔ 1938By similarity
Disulfide bondi1941 ↔ 1950By similarity
Glycosylationi1943N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1953 ↔ 1967By similarity
Disulfide bondi1970 ↔ 1980By similarity
Disulfide bondi1972 ↔ 1987By similarity
Disulfide bondi1989 ↔ 1998By similarity
Disulfide bondi2001 ↔ 2014By similarity
Disulfide bondi2017 ↔ 2028By similarity
Disulfide bondi2019 ↔ 2035By similarity
Glycosylationi2024N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2037 ↔ 2046By similarity
Disulfide bondi2049 ↔ 2061By similarity
Disulfide bondi2064 ↔ 2076By similarity
Disulfide bondi2066 ↔ 2083By similarity
Disulfide bondi2085 ↔ 2094By similarity
Disulfide bondi2097 ↔ 2109By similarity
Disulfide bondi2112InterchainCurated
Disulfide bondi2115InterchainCurated
Glycosylationi2196N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi2215N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2267N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2301N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2323N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2482N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2524N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2538N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi2569N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2699N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2720N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2890N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2938N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3010N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3022 ↔ 3048By similarity
Glycosylationi3070N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3196 ↔ 3223By similarity
Glycosylationi3491N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3505 ↔ 3528By similarity
Glycosylationi3612N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3682 ↔ 3709By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q00174

PRoteomics IDEntifications database

More...
PRIDEi
Q00174

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q00174

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Newly formed mesoderm and later prominently expressed in hemocytes, which also synthesize collagen IV. Expressed in muscles.2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

During morphogenesis, mostly in embryo development at 10-12 hours.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0002526, Expressed in embryonic/larval hemocyte (Drosophila) and 67 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q00174, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q00174, DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
64176, 23 interactors

Protein interaction database and analysis system

More...
IntActi
Q00174, 9 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0076722

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q00174

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini23 – 272Laminin N-terminalPROSITE-ProRule annotationAdd BLAST250
Domaini273 – 332Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST60
Domaini333 – 402Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini403 – 447Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST45
Domaini448 – 494Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST47
Domaini495 – 540Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST46
Domaini541 – 586Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST46
Domaini587 – 631Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST45
Domaini632 – 676Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST45
Domaini677 – 731Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST55
Domaini732 – 784Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST53
Domaini785 – 815Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd BLAST31
Domaini1375 – 1420Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST46
Domaini1421 – 1465Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST45
Domaini1466 – 1513Laminin EGF-like 14PROSITE-ProRule annotationAdd BLAST48
Domaini1514 – 1564Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST51
Domaini1565 – 1574Laminin EGF-like 16; first partPROSITE-ProRule annotation10
Domaini1585 – 1775Laminin IV type APROSITE-ProRule annotationAdd BLAST191
Domaini1776 – 1808Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd BLAST33
Domaini1809 – 1858Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST50
Domaini1859 – 1916Laminin EGF-like 18PROSITE-ProRule annotationAdd BLAST58
Domaini1917 – 1969Laminin EGF-like 19PROSITE-ProRule annotationAdd BLAST53
Domaini1970 – 2016Laminin EGF-like 20PROSITE-ProRule annotationAdd BLAST47
Domaini2017 – 2063Laminin EGF-like 21PROSITE-ProRule annotationAdd BLAST47
Domaini2064 – 2111Laminin EGF-like 22PROSITE-ProRule annotationAdd BLAST48
Domaini2672 – 2868Laminin G-like 1PROSITE-ProRule annotationAdd BLAST197
Domaini2876 – 3048Laminin G-like 2PROSITE-ProRule annotationAdd BLAST173
Domaini3055 – 3223Laminin G-like 3PROSITE-ProRule annotationAdd BLAST169
Domaini3349 – 3528Laminin G-like 4PROSITE-ProRule annotationAdd BLAST180
Domaini3534 – 3709Laminin G-like 5PROSITE-ProRule annotationAdd BLAST176

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni816 – 1374Domain IV''Add BLAST559
Regioni2112 – 2671Domain II and IAdd BLAST560

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili2178 – 2249Sequence analysisAdd BLAST72
Coiled coili2301 – 2321Sequence analysisAdd BLAST21
Coiled coili2376 – 2450Sequence analysisAdd BLAST75
Coiled coili2541 – 2676Sequence analysisAdd BLAST136

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi3270 – 3296Poly-ThrAdd BLAST27

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI, IV and G are globular.

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1836, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000301_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q00174

KEGG Orthology (KO)

More...
KOi
K06240

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q00174

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.1490, 1 hit
2.60.120.260, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013320, ConA-like_dom_sf
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR008979, Galactose-bd-like_sf
IPR009254, Laminin_aI
IPR010307, Laminin_dom_II
IPR002049, Laminin_EGF
IPR001791, Laminin_G
IPR000034, Laminin_IV
IPR008211, Laminin_N
IPR038684, Laminin_N_sf
IPR011641, Tyr-kin_ephrin_A/B_rcpt-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00052, Laminin_B, 1 hit
PF00053, Laminin_EGF, 20 hits
PF00054, Laminin_G_1, 1 hit
PF02210, Laminin_G_2, 4 hits
PF06008, Laminin_I, 1 hit
PF06009, Laminin_II, 1 hit
PF00055, Laminin_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181, EGF, 14 hits
SM00180, EGF_Lam, 21 hits
SM01411, Ephrin_rec_like, 4 hits
SM00281, LamB, 1 hit
SM00282, LamG, 5 hits
SM00136, LamNT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899, SSF49899, 5 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00022, EGF_1, 17 hits
PS01186, EGF_2, 5 hits
PS01248, EGF_LAM_1, 19 hits
PS50027, EGF_LAM_2, 22 hits
PS50025, LAM_G_DOMAIN, 5 hits
PS51115, LAMININ_IVA, 1 hit
PS51117, LAMININ_NTER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q00174-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGHGVASIGA LLVILAISYC QAELTPPYFN LATGRKIYAT ATCGQDTDGP
60 70 80 90 100
ELYCKLVGAN TEHDHIDYSV IQGQVCDYCD PTVPERNHPP ENAIDGTEAW
110 120 130 140 150
WQSPPLSRGM KFNEVNLTIN FEQEFHVAYL FIRMGNSPRP GLWTLEKSTD
160 170 180 190 200
YGKTWTPWQH FSDTPADCET YFGKDTYKPI TRDDDVICTT EYSKIVPLEN
210 220 230 240 250
GEIPVMLLNE RPSSTNYFNS TVLQEWTRAT NVRIRLLRTK NLLGHLMSVA
260 270 280 290 300
RQDPTVTRRY FYSIKDISIG GRCMCNGHAD TCDVKDPKSP VRILACRCQH
310 320 330 340 350
HTCGIQCNEC CPGFEQKKWR QNTNARPFNC EPCNCHGHSN ECKYDEEVNR
360 370 380 390 400
KGLSLDIHGH YDGGGVCQNC QHNTVGINCN KCKPKYYRPK GKHWNETDVC
410 420 430 440 450
SPCQCDYFFS TGHCEEETGN CECRAAFQPP SCDSCAYGYY GYPNCRECEC
460 470 480 490 500
NLNGTNGYHC EAESGQQCPC KINFAGAYCK QCAEGYYGFP ECKACECNKI
510 520 530 540 550
GSITNDCNVT TGECKCLTNF GGDNCERCKH GYFNYPTCSY CDCDNQGTES
560 570 580 590 600
EICNKQSGQC ICREGFGGPR CDQCLPGFYN YPDCKPCNCS STGSSAITCD
610 620 630 640 650
NTGKCNCLNN FAGKQCTLCT AGYYSYPDCL PCHCDSHGSQ GVSCNSDGQC
660 670 680 690 700
LCQPNFDGRQ CDSCKEGFYN FPSCEDCNCD PAGVIDKFAG CGSVPVGELC
710 720 730 740 750
KCKERVTGRI CNECKPLYWN LNISNTEGCE ICDCWTDGTI SALDTCTSKS
760 770 780 790 800
GQCPCKPHTQ GRRCQECRDG TFDLDSASLF GCKDCSCDVG GSWQSVCDKI
810 820 830 840 850
SGQCKCHPRI TGLACTQPLT THFFPTLHQF QYEYEDGSLP SGTQVRYDYD
860 870 880 890 900
EAAFPGFSSK GYVVFNAIQN DVRNEVNVFK SSLYRIVLRY VNPNAENVTA
910 920 930 940 950
TISVTSDNPL EVDQHVKVLL QPTSEPQFVT VAGPLGVKPS AIVLDPGRYV
960 970 980 990 1000
FTTKANKNVM LDYFVLLPAA YYEAGILTRH ISNPCELGNM ELCRHYKYAS
1010 1020 1030 1040 1050
VEVFSPAATP FVIGENSKPT NPVETYTDPE HLQIVSHVGD IPVLSGSQNE
1060 1070 1080 1090 1100
LHYIVDVPRS GRYIFVIDYI SDRNFPDSYY INLKLKDNPD SETSVLLYPC
1110 1120 1130 1140 1150
LYSTICRTSV NEDGMEKSFY INKEDLQPVI ISADIEDGSR FPIISVTAIP
1160 1170 1180 1190 1200
VDQWSIDYIN PSPVCVIHDQ QCATPKFRSV PDSKKIEFET DHEDRIATNK
1210 1220 1230 1240 1250
PPYASLDERV KLVHLDSQNE ATIVIESKVD ATKPNLFVIL VKYYQPSHPK
1260 1270 1280 1290 1300
YQVYYTLTAG KNQYDGKFDI QHCPSSSGCR GVIRPAGEGS FEIDDEFKFT
1310 1320 1330 1340 1350
ITTDRSQSVW LDYLVVVPLK QYNDDLLVEE TFDQTKEFIQ NCGHDHFHIT
1360 1370 1380 1390 1400
HNASDFCKKS VFSLTADYNS GALPCNCDYA GSTSFECHPF GGQCQCKPNV
1410 1420 1430 1440 1450
IERTCGACRS RYYGFPDCKP CKCPNSAMCE PTTGECMCPP NVIGDLCEKC
1460 1470 1480 1490 1500
APNTYGFHQV IGCEECACNP MGIANGNSQC DLFNGTCECR QNIEGRACDV
1510 1520 1530 1540 1550
CSNGYFNFPH CEQCSCHKPG TELEVCDKID GACFCKKNVV GRDCDQCVDG
1560 1570 1580 1590 1600
TYNLQESNPD GCTTCFCFGK TSRCDSAYLR VYNVSLLKHV SITTPEFHEE
1610 1620 1630 1640 1650
SIKFDMWPVP ADEILLNETT LKADFTLREV NDERPAYFGV LDYLLNQNNH
1660 1670 1680 1690 1700
ISAYGGDLAY TLHFTSGFDG KYIVAPDVIL FSEHNALVHT SYEQPSRNEP
1710 1720 1730 1740 1750
FTNRVNIVES NFQTISGKPV SRADFMMVLR DLKVIFIRAN YWEQTLVTHL
1760 1770 1780 1790 1800
SDVYLTLADE DADGTGEYQF LAVERCSCPP GYSGHSCEDC APGYYRDPSG
1810 1820 1830 1840 1850
PYGGYCIPCE CNGHSETCDC ATGICSKCQH GTEGDHCERC VSGYYGNATN
1860 1870 1880 1890 1900
GTPGDCMICA CPLPFDSNNF ATSCEISESG DQIHCECKPG YTGPRCESCA
1910 1920 1930 1940 1950
NGFYGEPESI GQVCKPCECS GNINPEDQGS CDTRTGECLR CLNNTFGAAC
1960 1970 1980 1990 2000
NLCAPGFYGD AIKLKNCQSC DCDDLGTQTC DPFVGVCTCH ENVIGDRCDR
2010 2020 2030 2040 2050
CKPDHYGFES GVGCRACDCG AASNSTQCDP HTGHCACKSG VTGRQCDRCA
2060 2070 2080 2090 2100
VDHWKYEKDG CTPCNCNQGY SRGFGCNPNT GKCQCLPGVI GDRCDACPNR
2110 2120 2130 2140 2150
WVLIKDEGCQ ECNNCHHALL DVTDRMRYQI DSVLEDFNSV TLAFFTSQKL
2160 2170 2180 2190 2200
NYYDQLADEL EPKVKLLDPN SVDLSPSKKA NSELESDAKS YAKQVNQTLA
2210 2220 2230 2240 2250
NAFDIRERSS TTLGNITVAY DEAVKSADQA KEAIASVEAL SKNLEAAAST
2260 2270 2280 2290 2300
KIDAALEQAQ HILGQINGTS IELTPNEQVL EKARKLYEEV NTLVLPIKAQ
2310 2320 2330 2340 2350
NKSLNALKND IGEFSDHLED LFNWSEASQA KSADVERRNV ANQKAFDNSK
2360 2370 2380 2390 2400
FDTVSEQKLQ AEKNIKDAGN FLINGDLTLN QINQKLDNLR DALNELNSFN
2410 2420 2430 2440 2450
KNVDEELPVR EDQHKEADAL TDQAEQKAAE LAIKAQDLAA QYTDMTASAE
2460 2470 2480 2490 2500
PAIKAATAYS GIVEAVEAAQ KLSQDAISAA GNATDKTDGI EERAHLADTG
2510 2520 2530 2540 2550
STDLLQRARQ SLQKVQDDLE PRLNASAGKV QKISAVNNAT EHQLKDINKL
2560 2570 2580 2590 2600
IDQLPAESQR DMWKNSNANA SDALEILKNV LEILEPVSVQ TPKELEKAHG
2610 2620 2630 2640 2650
INRDLDLTNK DVSQANKQLD DVEGSVSKLN ELAEDIEEQQ HRVGSQSRQL
2660 2670 2680 2690 2700
GQEIENLKAQ VEAARQLANS IKVGVNFKPS TILELKTPEK TKLLATRTNL
2710 2720 2730 2740 2750
STYFRTTEPS GFLLYLGNDN KTAQKNNDFV AVEIVNGYPI LTIDLGNGPE
2760 2770 2780 2790 2800
RITSDKYVAD GRWYQAVVDR MGPNAKLTIR EELPNGDVVE HSKSGYLEGS
2810 2820 2830 2840 2850
QNILHVDKNS RLFVGGYPGI SDFNAPPDLT TNSFSGDIED LKIGDESVGL
2860 2870 2880 2890 2900
WNFVYGDDND QGARERDVLL EKKKPVTGLR FKGNGYVQLN ATSNLKSRSS
2910 2920 2930 2940 2950
IQFSFKADKD TSNGLLFFYG RDKHYMSIEM IDGAIFFNIS LGEGGGVQSG
2960 2970 2980 2990 3000
SQDRYNDNQW HKVQAERENR NGLLKVDDIV ISRTNAPLEA DLELPKLRRL
3010 3020 3030 3040 3050
YFGGHPRRLN TSISLQPNFD GCIDNVVINQ GVVDLTEYVT GGGVEEGCSA
3060 3070 3080 3090 3100
KFSTVVSYAP HEYGFLRMNN VSSDNNLHVV LHFKTTQPNG VLFYAANHDQ
3110 3120 3130 3140 3150
SSTIGLSLQD GLLKLNSMGS QLVIDDRILN DGEDHVVTVQ HTQGELRLTV
3160 3170 3180 3190 3200
DDVDNKRLGS PQPLILEGGD IFFAGLPDNY RTPRNALASL AYFVGCISDV
3210 3220 3230 3240 3250
TVNEEIINFA NSAEKKNGNI NGCPPHVLAY EPSLVPSYYP SGDNEVESPW
3260 3270 3280 3290 3300
SNADTLPPLK PDIESTLPPT TPTTTTTTTT TTTSTTTTST TTTTTTPSPI
3310 3320 3330 3340 3350
VIDEEKEIEA KTPQKILTTR PPAKLNLPSD ERCKLPEQPN FDVDFTEAGY
3360 3370 3380 3390 3400
RFYGLREQRL QINSLPVKVR RHHDIGISFR TERPNGLLIY AGSKQRDDFI
3410 3420 3430 3440 3450
AVYLLDGRVT YEIRVGAQLQ AKITTEAELN DGTWHTVEVV RTQRKVSLLI
3460 3470 3480 3490 3500
DKLEQPGSVD LNAERSAPVL AVELPIYLGG VNKFLESEVK NLTDFKTEVP
3510 3520 3530 3540 3550
YFNGCLKNIK FDAMDLETPP EEFGVVPCSE QVERGLFFNN QKAFVKIFDH
3560 3570 3580 3590 3600
FDVGTEMKIS FDFRPRDPNG LLFSVHGKNS YAILELVDNT LYFTVKTDLK
3610 3620 3630 3640 3650
NIVSTNYKLP NNESFCDGKT RNVQAIKSKF VINIAVDFIS SNPGVGNEGS
3660 3670 3680 3690 3700
VITRTNRPLF LGGHVAFQRA PGIKTKKSFK GCISKVEVNQ RMINITPNMV
3710
VGDIWQGYCP LN
Length:3,712
Mass (Da):411,157
Last modified:May 10, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF8DB4D0CC88BBEC1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti45Q → P in AAA28662 (PubMed:1425586).Curated1
Sequence conflicti1032L → R in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti1407A → R in AAA28662 (PubMed:1425586).Curated1
Sequence conflicti1559P → Q in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti1598H → Q in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti1912Q → E in AAC37178 (PubMed:8223265).Curated1
Sequence conflicti2630N → S in AAF50672 (PubMed:10731132).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M96388 Genomic DNA Translation: AAA28662.1
L07288 mRNA Translation: AAC37178.1
AE014296 Genomic DNA Translation: AAF50672.2
M75882 mRNA Translation: AAA28661.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S28399, S18253

NCBI Reference Sequences

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RefSeqi
NP_476617.1, NM_057269.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
38723

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG10236

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96388 Genomic DNA Translation: AAA28662.1
L07288 mRNA Translation: AAC37178.1
AE014296 Genomic DNA Translation: AAF50672.2
M75882 mRNA Translation: AAA28661.1
PIRiS28399, S18253
RefSeqiNP_476617.1, NM_057269.3

3D structure databases

SMRiQ00174
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi64176, 23 interactors
IntActiQ00174, 9 interactors
STRINGi7227.FBpp0076722

PTM databases

iPTMnetiQ00174

Proteomic databases

PaxDbiQ00174
PRIDEiQ00174

Genome annotation databases

GeneIDi38723
KEGGidme:Dmel_CG10236

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
38723
FlyBaseiFBgn0002526, LanA

Phylogenomic databases

eggNOGiKOG1836, Eukaryota
HOGENOMiCLU_000301_1_0_1
InParanoidiQ00174
KOiK06240
PhylomeDBiQ00174

Enzyme and pathway databases

ReactomeiR-DME-3000157, Laminin interactions

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
38723, 0 hits in 5 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
LanA, fly

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
38723

Protein Ontology

More...
PROi
PR:Q00174

Gene expression databases

BgeeiFBgn0002526, Expressed in embryonic/larval hemocyte (Drosophila) and 67 other tissues
ExpressionAtlasiQ00174, baseline and differential
GenevisibleiQ00174, DM

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
2.60.120.260, 1 hit
InterProiView protein in InterPro
IPR013320, ConA-like_dom_sf
IPR013032, EGF-like_CS
IPR000742, EGF-like_dom
IPR008979, Galactose-bd-like_sf
IPR009254, Laminin_aI
IPR010307, Laminin_dom_II
IPR002049, Laminin_EGF
IPR001791, Laminin_G
IPR000034, Laminin_IV
IPR008211, Laminin_N
IPR038684, Laminin_N_sf
IPR011641, Tyr-kin_ephrin_A/B_rcpt-like
PfamiView protein in Pfam
PF00052, Laminin_B, 1 hit
PF00053, Laminin_EGF, 20 hits
PF00054, Laminin_G_1, 1 hit
PF02210, Laminin_G_2, 4 hits
PF06008, Laminin_I, 1 hit
PF06009, Laminin_II, 1 hit
PF00055, Laminin_N, 1 hit
SMARTiView protein in SMART
SM00181, EGF, 14 hits
SM00180, EGF_Lam, 21 hits
SM01411, Ephrin_rec_like, 4 hits
SM00281, LamB, 1 hit
SM00282, LamG, 5 hits
SM00136, LamNT, 1 hit
SUPFAMiSSF49899, SSF49899, 5 hits
PROSITEiView protein in PROSITE
PS00022, EGF_1, 17 hits
PS01186, EGF_2, 5 hits
PS01248, EGF_LAM_1, 19 hits
PS50027, EGF_LAM_2, 22 hits
PS50025, LAM_G_DOMAIN, 5 hits
PS51115, LAMININ_IVA, 1 hit
PS51117, LAMININ_NTER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLAMA_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q00174
Secondary accession number(s): Q9VRW0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 10, 2005
Last modified: August 12, 2020
This is version 170 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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