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O42237 (SEM3E_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Semaphorin-3E
Alternative name(s):
Collapsin-5
Short name=COLL-5
Gene names
Name:SEMA3E
Synonyms:COLL5
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length785 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays an important role in signaling via the cell surface receptor PLXND1. Mediates reorganization of the actin cytoskeleton, leading to the retraction of cell projections. Promotes focal adhesion disassembly and inhibits adhesion of endothelial cells to the extracellular matrix. Regulates angiogenesis. Can down-regulate sprouting angiogenesis. Required for normal vascular patterning during embryogenesis. Induces the collapse and paralysis of neuronal growth cones. Plays an important role in ensuring the specificity of synapse formation By similarity.

Subcellular location

Secreted.

Tissue specificity

Collapsin-1, -2, -3, and -5 bind to overlapping but distinct axon tracts.

Domain

Strong binding to neuropilin is mediated by the carboxy third of the protein.

Sequence similarities

Belongs to the semaphorin family.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 Sema domain.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Neurogenesis
   Cellular componentSecreted
   DomainImmunoglobulin domain
Signal
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionreceptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 785760Semaphorin-3E
PRO_0000032319

Regions

Domain36 – 520485Sema
Domain651 – 74090Ig-like C2-type
Compositional bias741 – 78040Arg/Lys-rich (basic)

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation6001N-linked (GlcNAc...) Potential
Disulfide bond109 ↔ 119 By similarity
Disulfide bond137 ↔ 146 By similarity
Disulfide bond274 ↔ 386 By similarity
Disulfide bond298 ↔ 346 By similarity
Disulfide bond523 ↔ 541 By similarity
Disulfide bond658 ↔ 733 By similarity

Experimental info

Sequence conflict2461N → D Ref.2
Sequence conflict2481V → I Ref.2
Sequence conflict2501L → F Ref.2

Sequences

Sequence LengthMass (Da)Tools
O42237 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E551EBF717630632

FASTA78590,979
        10         20         30         40         50         60 
MLGRMASAQD LLILALCGLL LELPAGYHAT DTRQPRLRLS HKELWDLNRT SVFHSPFGYL 

        70         80         90        100        110        120 
GLHIMLLDEY QERLFVGGRD LLYSLSLDRI SNNYREIHWP STPLQAEECI IKGRDADECA 

       130        140        150        160        170        180 
NYVRVLHRYN RTHLLACGTG AFDPVCTFIR VGHPSEDHLF QLESHKFERG RGRCPFDPTS 

       190        200        210        220        230        240 
SFTSILIGGE LFTGLYSDYW GRDAAVFRTM NRMAHLRTEP DSEHLLKEPK FVGSYMIPDN 

       250        260        270        280        290        300 
EDHDDNKVYL FFTEKALEAE TSTHAIYTRV GRVCVNDMGG QRIVVNKWST FLKTRLVCSV 

       310        320        330        340        350        360 
PGRNGIDTHF DELEDVFLLQ TRDNKNPVIF GLFSTTSNIF RGYAICVYHM AIVRAAFNGP 

       370        380        390        400        410        420 
YAHKEGPEYY WALYEGKVPY PRPGSCASKV NGGLYTTTKD YPDEAVHFAR SHPLMYQPIK 

       430        440        450        460        470        480 
PVHKRPILVK TDGKYNLKQI AVDRVEAEDG QYDVLFIGTD NGIVLKVITI YNQETESMEE 

       490        500        510        520        530        540 
VILEELQVFK VPIPILSMEI SSKRQQLYIG TESVIAQVKF HQCDMYGTAC ADCCLARDPY 

       550        560        570        580        590        600 
CAWDGISCSR YYPTGMQAKR RFRRQDVRHG NAAQQCFGQQ FIGEVLEKTE ERLVYGIEYN 

       610        620        630        640        650        660 
STLLEYTPRT LQAKVNWFVQ RAHETKKEEV KTDERIIKMD LGLLFLKLHR LDAGTYFCQT 

       670        680        690        700        710        720 
VEHSIVHTVR KITLEIVEEE RVDEMFSKDY EEEISHKMPC PMQSNIPQVS KPWYKEFLQL 

       730        740        750        760        770        780 
IGYSNFQRVE EYCEKVWCTD KKRKKLKMSP SKWKYANPQE KRQDQEKKAR IRPEHYRLPR 


NIADS 

« Hide

References

[1]"Secreted chick semaphorins bind recombinant neuropilin with similar affinities but bind different subsets of neurons in situ."
Feiner L., Koppel A.M., Kobayashi H., Raper J.A.
Neuron 19:539-545(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"A family of molecules related to collapsin in the embryonic chick nervous system."
Luo Y., Shepherd I., Li J., Renzi M.J., Chang S., Raper J.A.
Neuron 14:1131-1140(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 244-543.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF022947 mRNA. Translation: AAB80952.1.
U28243 mRNA. Translation: AAA86899.1.
RefSeqNP_989573.1. NM_204242.1.
UniGeneGga.136.

3D structure databases

ProteinModelPortalO42237.
SMRO42237. Positions 33-526.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000013846.

Proteomic databases

PaxDbO42237.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID374089.
KEGGgga:374089.

Organism-specific databases

CTD9723.

Phylogenomic databases

eggNOGNOG324739.
HOGENOMHOG000039964.
HOVERGENHBG055071.
InParanoidO42237.
KOK06840.
PhylomeDBO42237.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR016201. Plexin-like_fold.
IPR001627. Semap_dom.
IPR027231. Semaphorin.
IPR015513. Semaphorin_3E.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERPTHR11036. PTHR11036. 1 hit.
PTHR11036:SF22. PTHR11036:SF22. 1 hit.
PfamPF01403. Sema. 1 hit.
[Graphical view]
SMARTSM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
[Graphical view]
SUPFAMSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
PROSITEPS51004. SEMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20813608.
PROO42237.

Entry information

Entry nameSEM3E_CHICK
AccessionPrimary (citable) accession number: O42237
Secondary accession number(s): Q90666
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families