larp

Functionⁱ

RNA-binding protein required during male meiosis and development of the syncytial embryo (PubMed:17951964, PubMed:19631203, PubMed:30772175). Binds poly-(A) tails of mRNAs and regulates their expression by regulating their stability or translation (PubMed:17951964, PubMed:19631203).3 Publications

GO - Molecular functionⁱ

RNA binding Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

male meiotic nuclear division
Source: FlyBase
Inferred from mutant phenotypeⁱ
- Ref.7
  "A Drosophila orthologue of larp protein family is required for multiple processes in male meiosis."
  Ichihara K., Shimizu H., Taguchi O., Yamaguchi M., Inoue Y.H.
  Cell Struct. Funct. 32:89-100(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
- Ref.10
  "Drosophila Larp associates with poly(A)-binding protein and is required for male fertility and syncytial embryo development."
  Blagden S.P., Gatt M.K., Archambault V., Lada K., Ichihara K., Lilley K.S., Inoue Y.H., Glover D.M.
  Dev. Biol. 334:186-197(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: RNA-BINDING, FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PABP.
mitochondrion inheritance
Source: FlyBase
Inferred from mutant phenotypeⁱ
- Ref.7
  "A Drosophila orthologue of larp protein family is required for multiple processes in male meiosis."
  Ichihara K., Shimizu H., Taguchi O., Yamaguchi M., Inoue Y.H.
  Cell Struct. Funct. 32:89-100(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
positive regulation of mitochondrial DNA replication
Source: FlyBase
Inferred from mutant phenotypeⁱ
- Ref.11
  "PINK1 Inhibits Local Protein Synthesis to Limit Transmission of Deleterious Mitochondrial DNA Mutations."
  Zhang Y., Wang Z.H., Liu Y., Chen Y., Sun N., Gucek M., Zhang F., Xu H.
  Mol. Cell 73:1127-1137(2019) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-66; THR-107; SER-182; SER-186; SER-219; SER-221; THR-828; SER-1119; SER-1510 AND SER-1512, MUTAGENESIS OF SER-66; THR-107; SER-182; SER-186; 219-SER--SER-221; THR-828; SER-1119 AND 1510-SER--SER-1512.
positive regulation of mitochondrial translation
Source: FlyBase
Inferred from mutant phenotypeⁱ
- Ref.11
  "PINK1 Inhibits Local Protein Synthesis to Limit Transmission of Deleterious Mitochondrial DNA Mutations."
  Zhang Y., Wang Z.H., Liu Y., Chen Y., Sun N., Gucek M., Zhang F., Xu H.
  Mol. Cell 73:1127-1137(2019) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-66; THR-107; SER-182; SER-186; SER-219; SER-221; THR-828; SER-1119; SER-1510 AND SER-1512, MUTAGENESIS OF SER-66; THR-107; SER-182; SER-186; 219-SER--SER-221; THR-828; SER-1119 AND 1510-SER--SER-1512.
spindle assembly involved in male meiosis
Source: FlyBase
Inferred from mutant phenotypeⁱ
- Ref.7
  "A Drosophila orthologue of larp protein family is required for multiple processes in male meiosis."
  Ichihara K., Shimizu H., Taguchi O., Yamaguchi M., Inoue Y.H.
  Cell Struct. Funct. 32:89-100(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
syncytial blastoderm mitotic cell cycle
Source: FlyBase
Inferred from mutant phenotypeⁱ
- Ref.10
  "Drosophila Larp associates with poly(A)-binding protein and is required for male fertility and syncytial embryo development."
  Blagden S.P., Gatt M.K., Archambault V., Lada K., Ichihara K., Lilley K.S., Inoue Y.H., Glover D.M.
  Dev. Biol. 334:186-197(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: RNA-BINDING, FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PABP.

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	RNA-binding
Biological process	Meiosis

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: La-related protein 1 Alternative name(s): dLarp
Gene namesⁱ	Name:larp ORF Names:CG42551
Organismⁱ	Drosophila melanogaster (Fruit fly)
Taxonomic identifierⁱ	7227 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophila › Sophophora › melanogaster group › melanogaster subgroup
Proteomesⁱ	UP000000803 Componentⁱ: Chromosome 3R

Organism-specific databases

Drosophila genome database More...FlyBaseⁱ	FBgn0261618, larp

FlyBaseⁱ

FBgn0261618, larp

Keywords - Cellular componentⁱ

Cytoplasm, Mitochondrion

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Mutant males show multiple meiotic phenotypes such as a failure of chromosome segregation, cytokinesis and mitochondrial partition. Defects in spindle pole organization and spindle formation. Mutant-derived syncytial embryos show a range of mitotic phenotypes, including failure of centrosomes to migrate around the nuclear envelope, detachment of centrosomes from spindle poles, the formation of multipolar spindle arrays and cytokinetic defects.2 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	66	S → A: Partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with A-107. In larp-10A, loss of phosphorylation by Pink1; when associated with A-107; A-182; A-186; 219-A-A-221; A-828; A-1119 and 1510-A-A-1512. 1 Publication	1
Mutagenesisⁱ	66	S → D: Phosphomimetic mutant, partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with D-107. 1 Publication	1
Mutagenesisⁱ	107	T → A: Partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with A-66. In larp-10A, loss of phosphorylation by Pink1; when associated with A-66; A-182; A-186; 219-A-A-221; A-828; A-1119 and 1510-A-A-1512. 1 Publication	1
Mutagenesisⁱ	107	T → D: Phosphomimetic mutant, partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with D-66. 1 Publication	1
Mutagenesisⁱ	182	S → A: Partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with A-186. In larp-10A, loss of phosphorylation by Pink1; when associated with A-66; A-107; A-186; 219-A-A-221; A-828; A-1119 and 1510-A-A-1512. 1 Publication	1
Mutagenesisⁱ	182	S → D: Phosphomimetic mutant, partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with D-186. 1 Publication	1
Mutagenesisⁱ	186	S → A: Partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with A-182. In larp-10A, loss of phosphorylation by Pink1; when associated with A-66; A-107; A-182; 219-A-A-221; A-828; A-1119 and 1510-A-A-1512. 1 Publication	1
Mutagenesisⁱ	186	S → D: Phosphomimetic mutant, partially rescues mtDNA levels and hatching rate in spoon null mutants; when associated with D-182. 1 Publication	1
Mutagenesisⁱ	219 – 221	SPS → APA: Partially rescues mtDNA levels and hatching rate in spoon null mutants. In larp-10A, loss of phosphorylation by Pink1; when associated with A-66; A-107; A-182; A-186; A-828; A-1119 and 1510-A-A-1512. 1 Publication	3
Mutagenesisⁱ	828	T → A: Partially rescues mtDNA levels and hatching rate in spoon null mutants. In larp-10A, loss of phosphorylation by Pink1; when associated with A-66; A-107; A-182; A-186; 219-A-A-221; A-1119 and 1510-A-A-1512. 1 Publication	1
Mutagenesisⁱ	828	T → D: Phosphomimetic mutant, partially rescues mtDNA levels and hatching rate in spoon null mutants. 1 Publication	1
Mutagenesisⁱ	1119	S → A: Partially rescues nascent protein synthesis and tam expression in mitochondria containing deleterious mutations. Partially rescues mtDNA levels and hatching rate in spoon null mutants. In larp-10A, loss of phosphorylation by Pink1; when associated with A-66; A-107; A-182; A-186; 219-A-A-221; A-828 and 1510-A-A-1512. 1 Publication	1
Mutagenesisⁱ	1119	S → D: Phosphomimetic mutant, severe reduction in ability to rescue mtDNA levels and hatching rate in spoon null mutants. 1 Publication	1
Mutagenesisⁱ	1510 – 1512	SVS → AVA: Partially rescues mtDNA levels and hatching rate in spoon null mutants. In larp-10A, loss of phosphorylation by Pink1; when associated with A-66; A-107; A-182; A-186; 219-A-A-221; A-828 and A-1119. 1 Publication	3
Mutagenesisⁱ	1510 – 1512	SVS → DVD: Phosphomimetic mutant, partially rescues mtDNA levels and hatching rate in spoon null mutants. 1 Publication	3

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000207613	1 – 1673	La-related protein 1Add BLAST		1673

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	66	Phosphoserine2 Publications	1
Modified residueⁱ	69	Phosphoserine2 Publications	1
Modified residueⁱ	102	Phosphoserine1 Publication	1
Modified residueⁱ	107	Phosphothreonine2 Publications	1
Modified residueⁱ	111	Phosphoserine1 Publication	1
Modified residueⁱ	112	Phosphoserine1 Publication	1
Modified residueⁱ	182	Phosphoserine1 Publication	1
Modified residueⁱ	186	Phosphoserine1 Publication	1
Modified residueⁱ	219	Phosphoserine2 Publications	1
Modified residueⁱ	221	Phosphoserine2 Publications	1
Modified residueⁱ	223	Phosphoserine1 Publication	1
Modified residueⁱ	229	Phosphoserine1 Publication	1
Modified residueⁱ	230	Phosphoserine1 Publication	1
Modified residueⁱ	236	Phosphoserine1 Publication	1
Modified residueⁱ	284	Phosphoserine1 Publication	1
Modified residueⁱ	562	Phosphoserine1 Publication	1
Modified residueⁱ	608	Phosphoserine1 Publication	1
Modified residueⁱ	828	Phosphothreonine1 Publication	1
Modified residueⁱ	851	Phosphoserine1 Publication	1
Modified residueⁱ	1119	Phosphoserine2 Publications	1
Modified residueⁱ	1124	Phosphoserine1 Publication	1
Modified residueⁱ	1261	Phosphoserine1 Publication	1
Modified residueⁱ	1315	Phosphotyrosine1 Publication	1
Modified residueⁱ	1510	Phosphoserine2 Publications	1
Modified residueⁱ	1512	Phosphoserine2 Publications	1
Modified residueⁱ	1578	Phosphoserine1 Publication	1
Modified residueⁱ	1585	Phosphoserine1 Publication	1
Modified residueⁱ	1610	Phosphoserine1 Publication	1

Post-translational modificationⁱ

Phosphorylated on threonine and serine residues (PubMed:30772175). During oogenesis, phosphorylation on Ser-1119 by Pink1 at the outer membrane of defective mitochondria, impairs its ability to promote local translation and mtDNA replication thus reducing transmission of deleterious mtDNA mutations to the mature oocyte (PubMed:30772175).1 Publication

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

PaxDbⁱ	Q9VAW5
PRIDEⁱ	Q9VAW5

PTM databases

iPTMnetⁱ	Q9VAW5

iPTMnetⁱ

Q9VAW5

Expressionⁱ

Developmental stageⁱ

At the end of embryogenesis, accumulates in the gut and muscles.1 Publication

Gene expression databases

Bgeeⁱ	FBgn0261618, Expressed in pupa and 61 other tissues
ExpressionAtlasⁱ	Q9VAW5, baseline and differential
Genevisibleⁱ	Q9VAW5, DM

Interactionⁱ

Subunit structureⁱ

Interacts with pAbp.

1 Publication

Protein-protein interaction databases

BioGRIDⁱ	72798, 22 interactors
IntActⁱ	Q9VAW5, 20 interactors
Molecular INTeraction database More...MINTⁱ	Q9VAW5
STRINGⁱ	7227.FBpp0290398

Structureⁱ

3D structure databases

SMRⁱ	Q9VAW5
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	723 – 814	HTH La-type RNA-bindingPROSITE-ProRule annotationAdd BLAST		92

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	296 – 301	Poly-Gln	6
Compositional biasⁱ	322 – 329	Poly-Gln	8
Compositional biasⁱ	332 – 339	Poly-Thr	8
Compositional biasⁱ	340 – 354	Poly-AlaAdd BLAST	15
Compositional biasⁱ	372 – 380	Poly-Thr	9
Compositional biasⁱ	480 – 487	Poly-Thr	8
Compositional biasⁱ	869 – 874	Poly-Pro	6
Compositional biasⁱ	985 – 988	Poly-Gln	4
Compositional biasⁱ	996 – 1001	Poly-Asn	6
Compositional biasⁱ	1042 – 1055	Poly-ThrAdd BLAST	14
Compositional biasⁱ	1221 – 1225	Poly-Pro	5
Compositional biasⁱ	1543 – 1553	Poly-GlnAdd BLAST	11
Compositional biasⁱ	1620 – 1623	Poly-Gln	4
Compositional biasⁱ	1665 – 1671	Poly-Ser	7

Phylogenomic databases

eggNOGⁱ	KOG2590, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000169209
InParanoidⁱ	Q9VAW5
OMAⁱ	GMWKEVK
PhylomeDBⁱ	Q9VAW5

Family and domain databases

Gene3Dⁱ	1.10.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR006607, DM15 IPR006630, La_HTH IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF05383, La, 1 hit
SMARTⁱ	View protein in SMART SM00684, DM15, 3 hits SM00715, LA, 1 hit
SUPFAMⁱ	SSF46785, SSF46785, 1 hit
PROSITEⁱ	View protein in PROSITE PS50961, HTH_LA, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform D (identifier: Q9VAW5-3) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSKEETPST GGAAPVATVA ASGSATTSYA NVVQNLETKK SGTSNTTTTT 
        60         70         80         90        100
ARATVDNKEN QPNLKSFKSW SEEAAAAEAA GESPIVGSVS LAQTGEKRAA 
       110        120        130        140        150
ASGGDNTAEN SSELDDNNDF VPVLSHHRRD RKKARKEKPR DQQPAGGRGD 
       160        170        180        190        200
GQKPQQAGGR RVPGSSDTER KSVRPRAPRG GSPRKSAAGA AGAAGSNAGA 
       210        220        230        240        250
VSSAVPGGPK VHKDRKDTSP SASIEGAGSS GNEAKSADGD QQAGEKGAAG 
       260        270        280        290        300
AAPPPKRFIA APPPKVNAWK ISAKQSGSPK AGTSPLDKRV LQPKAQQQQQ 
       310        320        330        340        350
QTKQTASQNN NAQNTASNKK TQQQQQPQQG ATTTTQTTTA AAAAATAAAA 
       360        370        380        390        400
ATAATTSAAA ATSSAAAVPA ATTETATTTT VDASQADALA KVVVKDKKKV 
       410        420        430        440        450
NQKASDFSNV GDWPTLIGGT SGSGKATSNE PKRNPTKKQQ SAKTAAAVAA 
       460        470        480        490        500
SSNTTSSEVA TESNVAGTTS SSNSNPSSST TTTNTTTNSQ ATTAPVASTS 
       510        520        530        540        550
HDAKAQRDAE PAANSAAGTT GTAAGPALTK KIPKHKWRPL PIDLAKSSRP 
       560        570        580        590        600
KPIGGRPNRR FSDDIADQRR PPRVYHDRQP GAGGAGVESR HPHAGRHPYG 
       610        620        630        640        650
SRPATATSER VDSWRSSSST TTAAFDEQRS GAAGGAGAAG TGVGSATRGP 
       660        670        680        690        700
RRYRTPYRGG RQGRGGFSRQ GPGRPTYRIP RHLLASGEYA NYLPADAAGA 
       710        720        730        740        750
DSQSSYVLMG THYFGNVPAA YIELDANSIK EAIKKQVEYY FSVDNLTGDF 
       760        770        780        790        800
FLRRKMDPEG YIPVTLIASF HRVLALTTDV AVIVNAIKES DKLELFEGYK 
       810        820        830        840        850
VRTKTTPTTW PITEVPEVNE GEPKAIGTLE QEQLEQNDGQ EKLEEQTEAD 
       860        870        880        890        900
SPPPILTSAM ATKPLNSIPP PPMPRNPQNL VPKMLQDKQQ SRSSTIAALN 
       910        920        930        940        950
SVNAISALTQ QVEGGAAELA GHLSGLAESV KPKSTSTPDK RNAASAGNGA 
       960        970        980        990       1000
GSAAALVAEP EGIWKEVKRR SKTNAIKENA TTPPQQQQPP LSQTLNNNND 
      1010       1020       1030       1040       1050
NVKTNNTSSK SKSSSNNAPS NASSSATVCV TTNNASSATK ATTKTTTTST 
      1060       1070       1080       1090       1100
ATTTTNNNIK SGNAAYSKTH SKSSSKTAAP PSAQCHAEKE ELDFQFDEEL 
      1110       1120       1130       1140       1150
MDPLPPGTGR INNFTENFSD DDESDYEFAD RDINKLLIVA QVGRAPKHEG 
      1160       1170       1180       1190       1200
YDRTADFTSR TKITQDLENI INDGLVNYEE DLWTTTNVVA DYKTVNVISQ 
      1210       1220       1230       1240       1250
ADFEKLAGGR NKSVLPPQVV PPPPPFEEDL DETLVGDTTL NSTLNNTLKS 
      1260       1270       1280       1290       1300
RRARFYAAPN SHSIDPRTPR KRKLRHTANP PVEAHVGWLL DTVEHRPRTT 
      1310       1320       1330       1340       1350
SMGSSAGTSP TASSYGSFGS SVPQSLPVFQ HPSHALLKEN NFTQQAYHKY 
      1360       1370       1380       1390       1400
HSRCLKERRR LGYGQSQEMN TLYRFWSFFL RENFNKSMYN EFRSLALEDA 
      1410       1420       1430       1440       1450
GNGFRYGLEC LFRFFSYGLE KKFRPNIYQD FQDETIADYE TGQLYGLEKF 
      1460       1470       1480       1490       1500
WAFLKYYKNG EKLEVQPKLA EYLKSFKNIE DFRVVEPEIN EMLQGVGSLN 
      1510       1520       1530       1540       1550
PGRQLNRHRS VSESDGTAVI AAGGRRLNTT ITNRSDYVGR LLQQQHQQQQ 
      1560       1570       1580       1590       1600
QQQHHQYQQG YGGYNQQQNR RRTGSFGSTT VRIRSGSLGN KPQVANRNQG 
      1610       1620       1630       1640       1650
SQHELRRGGS NSGLAPHKRQ QQQKPKPGAG SQTGSTRATT SAAATATTAA 
      1660       1670 
SAATSTAATP AVTVSSGSSS SKK

Length:1,673

Mass (Da):178,145

Last modified:September 21, 2011 - v5

Checksum:ⁱD865CDA3103B1429

GO

Isoform C (identifier: Q9VAW5-1) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-270: Missing.
271-271: I → M

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        10         20         30         40         50
MSAKQSGSPK AGTSPLDKRV LQPKAQQQQQ QTKQTASQNN NAQNTASNKK 
        60         70         80         90        100
TQQQQQPQQG ATTTTQTTTA AAAAATAAAA ATAATTSAAA ATSSAAAVPA 
       110        120        130        140        150
ATTETATTTT VDASQADALA KVVVKDKKKV NQKASDFSNV GDWPTLIGGT 
       160        170        180        190        200
SGSGKATSNE PKRNPTKKQQ SAKTAAAVAA SSNTTSSEVA TESNVAGTTS 
       210        220        230        240        250
SSNSNPSSST TTTNTTTNSQ ATTAPVASTS HDAKAQRDAE PAANSAAGTT 
       260        270        280        290        300
GTAAGPALTK KIPKHKWRPL PIDLAKSSRP KPIGGRPNRR FSDDIADQRR 
       310        320        330        340        350
PPRVYHDRQP GAGGAGVESR HPHAGRHPYG SRPATATSER VDSWRSSSST 
       360        370        380        390        400
TTAAFDEQRS GAAGGAGAAG TGVGSATRGP RRYRTPYRGG RQGRGGFSRQ 
       410        420        430        440        450
GPGRPTYRIP RHLLASGEYA NYLPADAAGA DSQSSYVLMG THYFGNVPAA 
       460        470        480        490        500
YIELDANSIK EAIKKQVEYY FSVDNLTGDF FLRRKMDPEG YIPVTLIASF 
       510        520        530        540        550
HRVLALTTDV AVIVNAIKES DKLELFEGYK VRTKTTPTTW PITEVPEVNE 
       560        570        580        590        600
GEPKAIGTLE QEQLEQNDGQ EKLEEQTEAD SPPPILTSAM ATKPLNSIPP 
       610        620        630        640        650
PPMPRNPQNL VPKMLQDKQQ SRSSTIAALN SVNAISALTQ QVEGGAAELA 
       660        670        680        690        700
GHLSGLAESV KPKSTSTPDK RNAASAGNGA GSAAALVAEP EGIWKEVKRR 
       710        720        730        740        750
SKTNAIKENA TTPPQQQQPP LSQTLNNNND NVKTNNTSSK SKSSSNNAPS 
       760        770        780        790        800
NASSSATVCV TTNNASSATK ATTKTTTTST ATTTTNNNIK SGNAAYSKTH 
       810        820        830        840        850
SKSSSKTAAP PSAQCHAEKE ELDFQFDEEL MDPLPPGTGR INNFTENFSD 
       860        870        880        890        900
DDESDYEFAD RDINKLLIVA QVGRAPKHEG YDRTADFTSR TKITQDLENI 
       910        920        930        940        950
INDGLVNYEE DLWTTTNVVA DYKTVNVISQ ADFEKLAGGR NKSVLPPQVV 
       960        970        980        990       1000
PPPPPFEEDL DETLVGDTTL NSTLNNTLKS RRARFYAAPN SHSIDPRTPR 
      1010       1020       1030       1040       1050
KRKLRHTANP PVEAHVGWLL DTVEHRPRTT SMGSSAGTSP TASSYGSFGS 
      1060       1070       1080       1090       1100
SVPQSLPVFQ HPSHALLKEN NFTQQAYHKY HSRCLKERRR LGYGQSQEMN 
      1110       1120       1130       1140       1150
TLYRFWSFFL RENFNKSMYN EFRSLALEDA GNGFRYGLEC LFRFFSYGLE 
      1160       1170       1180       1190       1200
KKFRPNIYQD FQDETIADYE TGQLYGLEKF WAFLKYYKNG EKLEVQPKLA 
      1210       1220       1230       1240       1250
EYLKSFKNIE DFRVVEPEIN EMLQGVGSLN PGRQLNRHRS VSESDGTAVI 
      1260       1270       1280       1290       1300
AAGGRRLNTT ITNRSDYVGR LLQQQHQQQQ QQQHHQYQQG YGGYNQQQNR 
      1310       1320       1330       1340       1350
RRTGSFGSTT VRIRSGSLGN KPQVANRNQG SQHELRRGGS NSGLAPHKRQ 
      1360       1370       1380       1390       1400
QQQKPKPGAG SQTGSTRATT SAAATATTAA SAATSTAATP AVTVSSGSSS 

SKK

Show »

Length:1,403

Mass (Da):150,937

Checksum:ⁱB90DC1BB792454EF

GO

Isoform A (identifier: Q9VAW5-2) [UniParc]FASTA Add to basket

Also known as: B, E

The sequence of this isoform differs from the canonical sequence as follows:
1-708: Missing.

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        10         20         30         40         50
MGTHYFGNVP AAYIELDANS IKEAIKKQVE YYFSVDNLTG DFFLRRKMDP 
        60         70         80         90        100
EGYIPVTLIA SFHRVLALTT DVAVIVNAIK ESDKLELFEG YKVRTKTTPT 
       110        120        130        140        150
TWPITEVPEV NEGEPKAIGT LEQEQLEQND GQEKLEEQTE ADSPPPILTS 
       160        170        180        190        200
AMATKPLNSI PPPPMPRNPQ NLVPKMLQDK QQSRSSTIAA LNSVNAISAL 
       210        220        230        240        250
TQQVEGGAAE LAGHLSGLAE SVKPKSTSTP DKRNAASAGN GAGSAAALVA 
       260        270        280        290        300
EPEGIWKEVK RRSKTNAIKE NATTPPQQQQ PPLSQTLNNN NDNVKTNNTS 
       310        320        330        340        350
SKSKSSSNNA PSNASSSATV CVTTNNASSA TKATTKTTTT STATTTTNNN 
       360        370        380        390        400
IKSGNAAYSK THSKSSSKTA APPSAQCHAE KEELDFQFDE ELMDPLPPGT 
       410        420        430        440        450
GRINNFTENF SDDDESDYEF ADRDINKLLI VAQVGRAPKH EGYDRTADFT 
       460        470        480        490        500
SRTKITQDLE NIINDGLVNY EEDLWTTTNV VADYKTVNVI SQADFEKLAG 
       510        520        530        540        550
GRNKSVLPPQ VVPPPPPFEE DLDETLVGDT TLNSTLNNTL KSRRARFYAA 
       560        570        580        590        600
PNSHSIDPRT PRKRKLRHTA NPPVEAHVGW LLDTVEHRPR TTSMGSSAGT 
       610        620        630        640        650
SPTASSYGSF GSSVPQSLPV FQHPSHALLK ENNFTQQAYH KYHSRCLKER 
       660        670        680        690        700
RRLGYGQSQE MNTLYRFWSF FLRENFNKSM YNEFRSLALE DAGNGFRYGL 
       710        720        730        740        750
ECLFRFFSYG LEKKFRPNIY QDFQDETIAD YETGQLYGLE KFWAFLKYYK 
       760        770        780        790        800
NGEKLEVQPK LAEYLKSFKN IEDFRVVEPE INEMLQGVGS LNPGRQLNRH 
       810        820        830        840        850
RSVSESDGTA VIAAGGRRLN TTITNRSDYV GRLLQQQHQQ QQQQQHHQYQ 
       860        870        880        890        900
QGYGGYNQQQ NRRRTGSFGS TTVRIRSGSL GNKPQVANRN QGSQHELRRG 
       910        920        930        940        950
GSNSGLAPHK RQQQQKPKPG AGSQTGSTRA TTSAAATATT AASAATSTAA 
       960 
TPAVTVSSGS SSSKK

Show »

Length:965

Mass (Da):106,221

Checksum:ⁱ83B79ACAF6B9FB66

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A0B4K7Y7	A0A0B4K7Y7_DROME	La related protein, isoform G La related protein, isoform G (La related protein, isoform H)	larp 0031, 0225, 08, 29, BcDNA:LD02611	1,673	Annotation score:
A0A0B4K6K9	A0A0B4K6K9_DROME	La related protein, isoform F La related protein, isoform F	larp 0031, 0225, 08, 29, BcDNA:LD02611	1,409	Annotation score:

Sequence cautionⁱ

The sequence AAF35862 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.Curated

The sequence AAM29658 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.Curated

The sequence AAM29658 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

The sequence AAM29658 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

The sequence AAM49837 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	21	A → V in ACY39986 (Ref. 5) Curated	1
Sequence conflictⁱ	42	G → D in ACY39986 (Ref. 5) Curated	1
Sequence conflictⁱ	205	V → A in ACY39986 (Ref. 5) Curated	1
Sequence conflictⁱ	248	A → T in ACY39986 (Ref. 5) Curated	1
Sequence conflictⁱ	348	A → V in ACY39986 (Ref. 5) Curated	1
Sequence conflictⁱ	351 – 352	AT → TA in ACY39986 (Ref. 5) Curated	2
Sequence conflictⁱ	355 – 356	TT → KA in ACY39986 (Ref. 5) Curated	2
Sequence conflictⁱ	369	P → A in AAM29658 (PubMed:12537569).Curated	1
Sequence conflictⁱ	476	P → S in AAF35862 (PubMed:10878606).Curated	1
Sequence conflictⁱ	489	S → R in AAF35862 (PubMed:10878606).Curated	1
Sequence conflictⁱ	512	A → E in AAM29658 (PubMed:12537569).Curated	1
Sequence conflictⁱ	641	T → A in AAM29658 (PubMed:12537569).Curated	1
Sequence conflictⁱ	668	S → T in AAM29658 (PubMed:12537569).Curated	1
Sequence conflictⁱ	677	Y → H in AAM29658 (PubMed:12537569).Curated	1
Sequence conflictⁱ	819	N → T in AAF35862 (PubMed:10878606).Curated	1
Sequence conflictⁱ	819	N → T in AAM29658 (PubMed:12537569).Curated	1
Sequence conflictⁱ	1100	L → V in AAF35862 (PubMed:10878606).Curated	1
Sequence conflictⁱ	1648	T → A in AAF35862 (PubMed:10878606).Curated	1
Sequence conflictⁱ	1648	T → A in AAM49837 (PubMed:12537569).Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_015117	1 – 708	Missing in isoform A. CuratedAdd BLAST	708
Alternative sequenceⁱVSP_041775	1 – 270	Missing in isoform C. 2 PublicationsAdd BLAST	270
Alternative sequenceⁱVSP_041776	271	I → M in isoform C. 2 Publications	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF221108 mRNA Translation: AAF35862.1 Sequence problems. AE014297 Genomic DNA Translation: AAF56783.3 AE014297 Genomic DNA Translation: AAN14138.5 AE014297 Genomic DNA Translation: AAN14139.1 AE014297 Genomic DNA Translation: ACZ95051.1 AY113653 mRNA Translation: AAM29658.1 Sequence problems. AY118468 mRNA Translation: AAM49837.1 Different initiation. BT100187 mRNA Translation: ACY39986.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001163757.1, NM_001170286.3 [Q9VAW5-2] NP_001247347.1, NM_001260418.2 [Q9VAW5-3] NP_001247348.1, NM_001260419.2 [Q9VAW5-3] NP_524998.1, NM_080259.3 [Q9VAW5-2] NP_733244.5, NM_170365.4 [Q9VAW5-3] NP_733245.1, NM_170366.4 [Q9VAW5-2]

Genome annotation databases

EnsemblMetazoaⁱ	FBtr0089680; FBpp0088622; FBgn0261618 [Q9VAW5-2] FBtr0089682; FBpp0088624; FBgn0261618 [Q9VAW5-2] FBtr0301180; FBpp0290398; FBgn0261618 [Q9VAW5-3] FBtr0301181; FBpp0290399; FBgn0261618 [Q9VAW5-2] FBtr0306389; FBpp0297481; FBgn0261618 [Q9VAW5-3] FBtr0306390; FBpp0297482; FBgn0261618 [Q9VAW5-3]
GeneIDⁱ	53567
KEGGⁱ	dme:Dmel_CG42551
UCSC genome browser More...UCSCⁱ	CG14066-RB, d. melanogaster

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9VAW5	La related protein, isoform G		DROME		1673	UniRef100_Q9VAW5
FI14823p1		DROME		965
Isoform A of La-related protein 1		DROME		965

Protein	Similar proteins		Species	Score	Length	Source
Q9VAW5	La related protein, isoform G		DROME		1673	UniRef90_Q9VAW5
la-related protein 1		DROMA		1675
CG14066 (Fragment)		DROSI		177
FI14823p1		DROME		965
Isoform A of La-related protein 1		DROME		965
+7

Protein	Similar proteins		Species	Score	Length	Source
Q9VAW5	La related protein, isoform G		DROME		1673	UniRef50_Q9VAW5
la-related protein 1		DROMA		1675
CG14066 (Fragment)		DROSI		177
Blast:La-related protein 1		DROGU		1565
GG12072 (Fragment)		DROER		1396
+103

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF221108 mRNA Translation: AAF35862.1 Sequence problems. AE014297 Genomic DNA Translation: AAF56783.3 AE014297 Genomic DNA Translation: AAN14138.5 AE014297 Genomic DNA Translation: AAN14139.1 AE014297 Genomic DNA Translation: ACZ95051.1 AY113653 mRNA Translation: AAM29658.1 Sequence problems. AY118468 mRNA Translation: AAM49837.1 Different initiation. BT100187 mRNA Translation: ACY39986.1
RefSeqⁱ	NP_001163757.1, NM_001170286.3 [Q9VAW5-2] NP_001247347.1, NM_001260418.2 [Q9VAW5-3] NP_001247348.1, NM_001260419.2 [Q9VAW5-3] NP_524998.1, NM_080259.3 [Q9VAW5-2] NP_733244.5, NM_170365.4 [Q9VAW5-3] NP_733245.1, NM_170366.4 [Q9VAW5-2]

3D structure databases

SMRⁱ	Q9VAW5
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	72798, 22 interactors
IntActⁱ	Q9VAW5, 20 interactors
MINTⁱ	Q9VAW5
STRINGⁱ	7227.FBpp0290398

PTM databases

iPTMnetⁱ	Q9VAW5

iPTMnetⁱ

Q9VAW5

Proteomic databases

PaxDbⁱ	Q9VAW5
PRIDEⁱ	Q9VAW5

Genome annotation databases

EnsemblMetazoaⁱ	FBtr0089680; FBpp0088622; FBgn0261618 [Q9VAW5-2] FBtr0089682; FBpp0088624; FBgn0261618 [Q9VAW5-2] FBtr0301180; FBpp0290398; FBgn0261618 [Q9VAW5-3] FBtr0301181; FBpp0290399; FBgn0261618 [Q9VAW5-2] FBtr0306389; FBpp0297481; FBgn0261618 [Q9VAW5-3] FBtr0306390; FBpp0297482; FBgn0261618 [Q9VAW5-3]
GeneIDⁱ	53567
KEGGⁱ	dme:Dmel_CG42551
UCSCⁱ	CG14066-RB, d. melanogaster

Organism-specific databases

CTDⁱ	53567
FlyBaseⁱ	FBgn0261618, larp

Phylogenomic databases

eggNOGⁱ	KOG2590, Eukaryota
GeneTreeⁱ	ENSGT00940000169209
InParanoidⁱ	Q9VAW5
OMAⁱ	GMWKEVK
PhylomeDBⁱ	Q9VAW5

Miscellaneous databases

BioGRID-ORCSⁱ	53567, 0 hits in 3 CRISPR screens
ChiTaRSⁱ	larp, fly
GenomeRNAiⁱ	53567
Protein Ontology More...PROⁱ	PR:Q9VAW5

Gene expression databases

Bgeeⁱ	FBgn0261618, Expressed in pupa and 61 other tissues
ExpressionAtlasⁱ	Q9VAW5, baseline and differential
Genevisibleⁱ	Q9VAW5, DM

Family and domain databases

Gene3Dⁱ	1.10.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR006607, DM15 IPR006630, La_HTH IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf
Pfamⁱ	View protein in Pfam PF05383, La, 1 hit
SMARTⁱ	View protein in SMART SM00684, DM15, 3 hits SM00715, LA, 1 hit
SUPFAMⁱ	SSF46785, SSF46785, 1 hit
PROSITEⁱ	View protein in PROSITE PS50961, HTH_LA, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LARP_DROME
Accessionⁱ	Q9VAW5Primary (citable) accession number: Q9VAW5 Secondary accession number(s): A4V3J4 Q9VAW4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
	Last sequence update:	September 21, 2011
	Last modified:	April 7, 2021
	This is version 148 of the entry and version 5 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Drosophila annotation project

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UniProtKB - Q9VAW5 (LARP_DROME)

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La-related protein 1

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<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

<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>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

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<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

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Keywords - Cellular componenti

<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

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<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

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Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Gene expression databases

<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

Protein-protein interaction databases

<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

<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

Compositional bias

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

3D structure databases

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PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

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Gene expression databases

Family and domain databases

<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 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ