Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q62217 (SEM5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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-5A
Alternative name(s):
Semaphorin-F
Short name=Sema F
Gene names
Name:Sema5a
Synonyms:Semaf, SemF
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1077 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Bifunctional axonal guidance cue regulated by sulfated proteoglycans; attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs). Ligand for receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1 By similarity. May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis. Ref.3

Subunit structure

Binds PLXNB3 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

In adult, detected in liver, brain, kidney, heart, lung and spleen.

Developmental stage

Differentially expressed in embryonic and adult tissues. Its abundance decreases from E10 to birth. At E10.5, detected in the atrial septum and endocardial cushions, and at lower levels in the atrial and ventricular endocardium. Strong expression detected in embryonic and postnatal retina. At P0 and P3, expression detected in the outer neuroblastic layer. After P7, the expression becomes more restricted and is observed in the middle to outer part of inner nuclear layer, and is not detectable at P21 when retinal development is almost complete. Ref.2 Ref.4

Disruption phenotype

Mutant mice die between E11.5 and E12.5. At this stage, no defects are detected in the development of extraembryonic tissues, cardiovascular system, axonal trajectories and peripheral nervous system. Mutants display decreased complexity of the hierarchically organized branches of the cranial blood vessels (Ref.2). Mutant mice are viable and fertile (Ref.4). Ref.2 Ref.4

Sequence similarities

Belongs to the semaphorin family.

Contains 1 PSI domain.

Contains 1 Sema domain.

Contains 7 TSP type-1 domains.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpatterning of blood vessels

Inferred from mutant phenotype Ref.2. Source: MGI

   Cellular_componentintegral to membrane

Inferred from direct assay PubMed 12506007. Source: MGI

   Molecular_functionaxon guidance receptor activity

Inferred from direct assay PubMed 12506007. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 10771056Semaphorin-5A
PRO_0000032336

Regions

Topological domain22 – 971950Extracellular Potential
Transmembrane972 – 99221Helical; Potential
Topological domain993 – 107785Cytoplasmic Potential
Domain35 – 484450Sema
Domain540 – 59354TSP type-1 1
Domain595 – 65157TSP type-1 2
Domain653 – 70250TSP type-1 3
Domain707 – 76559TSP type-1 4
Domain784 – 83956TSP type-1 5
Domain841 – 89656TSP type-1 6
Domain897 – 94448TSP type-1 7

Amino acid modifications

Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation7171N-linked (GlcNAc...) Potential
Glycosylation9331N-linked (GlcNAc...) Potential
Disulfide bond104 ↔ 114 By similarity
Disulfide bond131 ↔ 140 By similarity
Disulfide bond254 ↔ 357 By similarity
Disulfide bond278 ↔ 320 By similarity
Disulfide bond487 ↔ 504 By similarity
Disulfide bond496 ↔ 513 By similarity
Disulfide bond607 ↔ 644 By similarity
Disulfide bond611 ↔ 650 By similarity
Disulfide bond622 ↔ 634 By similarity
Disulfide bond665 ↔ 696 By similarity
Disulfide bond669 ↔ 701 By similarity
Disulfide bond680 ↔ 686 By similarity
Disulfide bond796 ↔ 833 By similarity
Disulfide bond800 ↔ 838 By similarity
Disulfide bond811 ↔ 823 By similarity
Disulfide bond853 ↔ 890 By similarity
Disulfide bond857 ↔ 895 By similarity
Disulfide bond868 ↔ 880 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62217 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EDAB0DDDA42789FF

FASTA1,077120,826
        10         20         30         40         50         60 
MKGACILAWL FSSLGVWRLA RPETQDPAKC QRAEHPVVSY KEIGPWLREF RAENAVDFSR 

        70         80         90        100        110        120 
LTFDPGQKEL VVGARNYLFR LELEDLSLIQ AVEWECDEAT KKACYSKGKS KEECQNYIRV 

       130        140        150        160        170        180 
LLVGGDRLFT CGTNAFTPVC TIRSLSNLTE IHDQISGMAR CPYSPQHNST ALLTASGELY 

       190        200        210        220        230        240 
AATAMDFPGR DPAIYRSLGT LPPLRTAQYN SKWLNEPNFV SSYDIGNFTY FFFRENAVEH 

       250        260        270        280        290        300 
DCGKTVFSRP ARVCKNDIGG RFLLEDTWTT FMKARLNCSR PGEVPFYYNE LQGTFFLPEL 

       310        320        330        340        350        360 
DLIYGIFTTN VNSIASSAVC VFNLSAISQA FNGPFKYQEN SRSAWLPYPN PNPNFQCGTM 

       370        380        390        400        410        420 
DQGLYVNLTE RNLQDAQKFI LMHEVVQPVT TVPSFMEDNS RFSHLAVDVV QGRETLVHII 

       430        440        450        460        470        480 
YLGTDYGTIK KVRAPLSQSS GSCLLEEIEL FPERRSEPIR SLQILHSQSV LFVGLQEHVA 

       490        500        510        520        530        540 
KIPLKRCHFH QTRSACIGAQ DPYCGWDAVM KKCTSLEESL SMTQWDQSIP TCPTRNLTVD 

       550        560        570        580        590        600 
GSFGPWSPWT PCTHTDGTAV GSCLCRSRSC DRPAPQCGGW QCEGPRMEIT NCSRNGGWTP 

       610        620        630        640        650        660 
WTSWSPCSTT CGIGFQVRQR SCSNPTPRHG GRVCVGQNRE ERYCNEHLLC PPHVFWTGWG 

       670        680        690        700        710        720 
PWERCTAQCG GGIQARRRTC ENGPDCAGSN VEYHPCNTNA CPELKKTTPW TPWTPVNISD 

       730        740        750        760        770        780 
NGGHYEQRFR YTCKARLPDP NLLEVGRQRI EMRYCSSDGT SGCSTDGLSG DFLRAGRYSA 

       790        800        810        820        830        840 
HTVNGAWSAW TSWSQCSRDC SRGIRNRKRV CNNPEPKFGG MPCLGPSLEF QECNILPCPV 

       850        860        870        880        890        900 
DGVWSCWSSW SKCSATCGGG HYMRTRSCSN PAPAYGGDIC LGLHTEEALC NTQTCPESWS 

       910        920        930        940        950        960 
EWSDWSVCDA SGTQVRARQC ILLFPVGSQC SGNTTESRPC VFDSNFIPEV SVARSSSVEE 

       970        980        990       1000       1010       1020 
KRCGEFNMFH MFHMMAVGLS SSILGCLLTL LVYTYCQRYQ QQSHDATVIH PVSPAALNSS 

      1030       1040       1050       1060       1070 
ITNHINKLDK YDSVEAIKAF NKNNLILEER NKYFNPHLTG KTYSNAYFTD LNNYDEY

« Hide

References

[1]"A novel class of murine semaphorins with homology to thrombospondin is differentially expressed during early embryogenesis."
Adams R.H., Betz H., Pueschel A.W.
Mech. Dev. 57:33-45(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NMRI.
[2]"Inactivation of the Sema5a gene results in embryonic lethality and defective remodeling of the cranial vascular system."
Fiore R., Rahim B., Christoffels V.M., Moorman A.F., Puschel A.W.
Mol. Cell. Biol. 25:2310-2319(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[3]"Semaphorin 5A promotes angiogenesis by increasing endothelial cell proliferation, migration, and decreasing apoptosis."
Sadanandam A., Rosenbaugh E.G., Singh S., Varney M., Singh R.K.
Microvasc. Res. 79:1-9(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Class 5 transmembrane semaphorins control selective Mammalian retinal lamination and function."
Matsuoka R.L., Chivatakarn O., Badea T.C., Samuels I.S., Cahill H., Katayama K., Kumar S.R., Suto F., Chedotal A., Peachey N.S., Nathans J., Yoshida Y., Giger R.J., Kolodkin A.L.
Neuron 71:460-473(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X97817 mRNA. Translation: CAA66397.1.
IPIIPI00816983.
UniGeneMm.260374.

3D structure databases

ProteinModelPortalQ62217.
SMRQ62217. Positions 68-506, 540-731, 783-940.
ModBaseSearch...

PTM databases

PhosphoSiteQ62217.

Proteomic databases

PRIDEQ62217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:107556. Sema5a.

Phylogenomic databases

eggNOGNOG316291.
HOGENOMHOG000047106.
HOVERGENHBG062356.
InParanoidQ62217.
OrthoDBEOG4PG603.

Gene expression databases

GenevestigatorQ62217.
GermOnlineENSMUSG00000022231. Mus musculus.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR003659. Plexin-like.
IPR016201. Plexin-like_fold.
IPR002165. Plexin_repeat.
IPR027231. Semaphorin.
IPR001627. Semaphorin/CD100_Ag.
IPR000884. Thrombospondin_1_rpt.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERPTHR11036. PTHR11036. 1 hit.
PfamPF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
SMARTSM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
SM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMSSF103575. Plexin-like_fold. 1 hit.
SSF101912. Sema. 1 hit.
SSF82895. TSP1. 6 hits.
PROSITEPS51004. SEMA. 1 hit.
PS50092. TSP1. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameSEM5A_MOUSE
AccessionPrimary (citable) accession number: Q62217
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents