Sex muscle abnormal protein 5 - Caenorhabditis elegans

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P29355 (SEM5_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sex muscle abnormal protein 5

Gene names

Name:	sem-5
ORF Names:	C14F5.5

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function

Acts both in vulval induction and sex myoblast migration. Presumably interacts with the kinase receptor let-23 and with a target that modifies the Ras-like protein let-60.

Sequence similarities

Belongs to the GRB2/sem-5/DRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Ontologies

Keywords
Domain	Repeat SH2 domain SH3 domain
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell migration Inferred from mutant phenotype Ref.1. Source: WormBase male genitalia development Inferred from mutant phenotype PubMed 7607066. Source: WormBase muscle organ development Inferred from mutant phenotype PubMed 16495308. Source: WormBase nematode larval development Inferred from mutant phenotype Ref.1. Source: WormBase regulation of cell projection organization Inferred from mutant phenotype PubMed 16495308. Source: WormBase regulation of vulval development Inferred from mutant phenotype Ref.1. Source: WormBase
Molecular_function	SH3/SH2 adaptor activity Inferred from sequence or structural similarity Ref.1. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 228

228

Sex muscle abnormal protein 5

PRO_0000088212

Regions

Domain

1 – 58

SH3 1

Domain

60 – 152

SH2

Domain

154 – 213

SH3 2

Experimental info

Mutagenesis

P → L in N1619. Ref.1

Mutagenesis

E → K in N1779. Ref.1

Mutagenesis

S → N in N1781. Ref.1

Mutagenesis

201

G → R in N2195. Ref.1

Secondary structure

228

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29355 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 2D684C9520646C41
Show »

FASTA

228

26,210

        10         20         30         40         50         60 
MEAVAEHDFQ AGSPDELSFK RGNTLKVLNK DEDPHWYKAE LDGNEGFIPS NYIRMTECNW 

        70         80         90        100        110        120 
YLGKITRNDA EVLLKKPTVR DGHFLVRQCE SSPGEFSISV RFQDSVQHFK VLRDQNGKYY 

       130        140        150        160        170        180 
LWAVKFNSLN ELVAYHRTAS VSRTHTILLS DMNVETKFVQ ALFDFNPQES GELAFKRGDV 

       190        200        210        220 
ITLINKDDPN WWEGQLNNRR GIFPSNYVCP YNSNKSNSNV APGFNFGN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains." Clark S.G., Stern M.J., Horvitz H.R. Nature 356:340-344(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF PRO-49; GLU-90; SER-91 AND GLY-201.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains." Lim W.A., Richards F.M., Fox R.O. Nature 372:375-379(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 153-214.
[4]	"Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors." Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A. Science 282:2088-2092(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 155-214.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S88446 mRNA. Translation: AAB21850.1.
FO080456 Genomic DNA. Translation: CCD63850.1.

PIR

S25730.

RefSeq

NP_509342.1. NM_076941.5.

UniGene

Cel.19703.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K76	NMR	-	A	155-214	[»]
1KFZ	NMR	-	A	155-214	[»]
1SEM	X-ray	2.00	A/B	155-212	[»]
2SEM	X-ray	2.20	A/B	155-214	[»]
3SEM	X-ray	2.20	A/B	155-214	[»]

ProteinModelPortal

P29355.

SMR

P29355. Positions 1-55, 60-151, 155-212.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27394N.

IntAct

P29355. 12 interactions.

MINT

MINT-114046.

STRING

6239.C14F5.5.

Proteomic databases

PaxDb

P29355.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

C14F5.5; C14F5.5; C14F5.5.

GeneID

181055.

KEGG

cel:CELE_C14F5.5.

UCSC

C14F5.5. c. elegans.

Organism-specific databases

CTD

181055.

WormBase

C14F5.5; CE01784; WBGene00004774; sem-5.

Phylogenomic databases

eggNOG

NOG298780.

GeneTree

ENSGT00550000074482.

HOGENOM

HOG000251625.

InParanoid

P29355.

K04364.

OMA

VETKFVQ.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR000108. p67phox.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P29355.

NextBio

912202.

Entry information

Entry name

SEM5_CAEEL

Accession

Primary (citable) accession number: P29355

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents