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D3ZTD8

- SEM5A_RAT

UniProt

D3ZTD8 - SEM5A_RAT

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Protein

Semaphorin-5A

Gene

Sema5a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis.By similarity2 Publications

GO - Molecular functioni

  1. axon guidance receptor activity Source: Ensembl
  2. chondroitin sulfate proteoglycan binding Source: UniProtKB
  3. heparan sulfate proteoglycan binding Source: UniProtKB
  4. semaphorin receptor binding Source: UniProtKB
  5. syndecan binding Source: UniProtKB

GO - Biological processi

  1. axonal fasciculation Source: UniProtKB
  2. blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: UniProtKB
  3. cell chemotaxis Source: UniProtKB
  4. diencephalon development Source: UniProtKB
  5. negative regulation of axon extension involved in axon guidance Source: UniProtKB
  6. negative regulation of cell adhesion Source: UniProtKB
  7. negative regulation of endothelial cell apoptotic process Source: UniProtKB
  8. patterning of blood vessels Source: Ensembl
  9. positive chemotaxis Source: UniProtKB
  10. positive regulation of actin filament depolymerization Source: UniProtKB
  11. positive regulation of angiogenesis Source: UniProtKB
  12. positive regulation of axon extension involved in axon guidance Source: UniProtKB
  13. positive regulation of catenin import into nucleus Source: UniProtKB
  14. positive regulation of endothelial cell chemotaxis Source: UniProtKB
  15. positive regulation of endothelial cell proliferation Source: UniProtKB
  16. positive regulation of protein kinase B signaling Source: UniProtKB
  17. semaphorin-plexin signaling pathway Source: UniProtKB
  18. signal clustering Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_238902. Other semaphorin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Semaphorin-5ABy similarity
Alternative name(s):
Semaphorin-F
Short name:
Sema F
Gene namesi
Name:Sema5aImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi1308650. Sema5a.

Subcellular locationi

Membrane Sequence Analysis; Single-pass membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei969 – 98921HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 10741052Semaphorin-5ASequence AnalysisPRO_0000420236Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 ↔ 114Sequence Analysis
Disulfide bondi131 ↔ 140Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi254 ↔ 357Sequence Analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi278 ↔ 320Sequence Analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi607 ↔ 644Sequence Analysis
Disulfide bondi611 ↔ 650Sequence Analysis
Disulfide bondi622 ↔ 634Sequence Analysis
Disulfide bondi665 ↔ 696Sequence Analysis
Disulfide bondi669 ↔ 701Sequence Analysis
Disulfide bondi680 ↔ 686Sequence Analysis
Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi796 ↔ 833Sequence Analysis
Disulfide bondi800 ↔ 838Sequence Analysis
Disulfide bondi811 ↔ 823Sequence Analysis
Disulfide bondi853 ↔ 890Sequence Analysis
Disulfide bondi857 ↔ 895Sequence Analysis
Disulfide bondi868 ↔ 880Sequence Analysis
Glycosylationi898 – 8981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi933 – 9331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1015 – 10151N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Developmental stagei

At E15.5, detected in axons extending from habenula nucleus explants (at protein level). Expressed in the habenula nucleus at E13.5 and E15.5, and in the prosomere 2 adjacent to the fasciculus retroflexus at E15.5.1 Publication

Interactioni

Subunit structurei

Binds PLXNB3.By similarity

Structurei

3D structure databases

ProteinModelPortaliD3ZTD8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 484450SemaPROSITE-ProRule annotationAdd
BLAST
Domaini486 – 53348PSISequence AnalysisAdd
BLAST
Domaini540 – 59354TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini595 – 65157TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini653 – 70250TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini784 – 83956TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini841 – 89656TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini897 – 94448TSP type-1 6PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PSI domain.Sequence Analysis
Contains 1 Sema domain.PROSITE-ProRule annotation
Contains 6 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000119134.
InParanoidiD3ZTD8.
KOiK06841.
OMAiYSNAYFT.
OrthoDBiEOG7SN8C0.
PhylomeDBiD3ZTD8.
TreeFamiTF329951.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR016201. Plexin-like_fold.
IPR001627. Semap_dom.
IPR027231. Semaphorin.
IPR000884. Thrombospondin_1_rpt.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR11036. PTHR11036. 1 hit.
PfamiPF01403. Sema. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
SMARTiSM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
SM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMiSSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
SSF82895. SSF82895. 6 hits.
PROSITEiPS51004. SEMA. 1 hit.
PS50092. TSP1. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

D3ZTD8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKGACILAWL FSSLGVWRLA RPETQDPAKC QRAEHPVVSY KEIGPWLREF
60 70 80 90 100
RAENAVDFSR LTFDPGQKEL VVGARNYLFR LQLEDLSLIQ AVQWECDEAT
110 120 130 140 150
KKACYSKGKS KEECQNYIRV LLVGGDRLFT CGTNAFTPVC TIRSLSNLTE
160 170 180 190 200
IHDQISGMAR CPYSPQHNST ALLTASGELY AATAMDFPGR DPAIYRSLGT
210 220 230 240 250
LPPLRTAQYN SKWLNEPNFV SSYDIGNFTY FFFRENAVEH DCGKTVFSRA
260 270 280 290 300
ARVCKNDIGG RFLLEDTWTT FMKARLNCSR PGEVPFYYNE LQSTFFLPEL
310 320 330 340 350
DLIYGIFTTN VNSIAASAVC VFNLSAISQA FNGPFKYQEN SRSAWLPYPN
360 370 380 390 400
PNPNFQCGTM DQGLYVNLTE RNLQDAQKFI LMHEVVQPVT TVPSFMEDNS
410 420 430 440 450
RFSHVAVDVV QGRDTLVHII YLATDYGTIK KVRAPLSQSS GSCLLEEIEL
460 470 480 490 500
FPERKSEPIR SLKILHSQSV LFVGLQEHVV KIPLKRCHFH QTRGACIGAQ
510 520 530 540 550
DPYCGWDAVM KKCTSLEESL SMTQWDQSVP TCPTRNLTVD GSFGPWSPWT
560 570 580 590 600
PCTHTDGTAV GSCLCRSRSC DSPAPQCGGW QCEGPRMEIT NCSRNGGWTP
610 620 630 640 650
WTSWSPCSTT CGIGFQVRQR SCSNPTPRHG GRVCVGQNRE ERYCNEHLLC
660 670 680 690 700
PPHVFWTGWG PWERCTAQCG GGIQARRRTC ENGPDCAGCN VEYQPCNTNA
710 720 730 740 750
CPELKKTTPW TPWTPVNISD NGGHYEQRFR YTCKARLPDP NLLEVGRQRI
760 770 780 790 800
EMRYCSSDGT SGCSTDGLSG DFLRAGRYSA HTVNGAWSAW TSWSQCSRDC
810 820 830 840 850
SRGIRNRKRV CNNPEPKYGG MPCLGPSLEF QECNILPCPV DGVWSCWSSW
860 870 880 890 900
SKCSATCGGG HYMRTRSCTN PAPAYGGDIC LGLHTEEALC NTQTCPENWS
910 920 930 940 950
EWSEWSVCDA SGTQVRTRQC ILLFPVGSQC SGNTTESRPC VFDSNFIPEV
960 970 980 990 1000
SVARSSSVEE KRCGEFNMFH MMAVGLSSSI LGCLLTLLVY TYCQRYQQQS
1010 1020 1030 1040 1050
HDATVIHPVS PAALNSSITN HINKLDKYDS VEAIKAFNKN NLILEERNKY
1060 1070
FNPHLTGKTY SNAYFTDLNN YDEY
Length:1,074
Mass (Da):120,378
Last modified:April 20, 2010 - v1
Checksum:iBFFBCEB5F9084FF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473992 Genomic DNA. Translation: EDL82657.1.
RefSeqiNP_001101129.1. NM_001107659.2.
UniGeneiRn.14619.

Genome annotation databases

EnsembliENSRNOT00000016506; ENSRNOP00000016506; ENSRNOG00000011977.
GeneIDi310207.
KEGGirno:310207.
UCSCiRGD:1308650. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473992 Genomic DNA. Translation: EDL82657.1 .
RefSeqi NP_001101129.1. NM_001107659.2.
UniGenei Rn.14619.

3D structure databases

ProteinModelPortali D3ZTD8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000016506 ; ENSRNOP00000016506 ; ENSRNOG00000011977 .
GeneIDi 310207.
KEGGi rno:310207.
UCSCi RGD:1308650. rat.

Organism-specific databases

CTDi 9037.
RGDi 1308650. Sema5a.

Phylogenomic databases

GeneTreei ENSGT00760000119134.
InParanoidi D3ZTD8.
KOi K06841.
OMAi YSNAYFT.
OrthoDBi EOG7SN8C0.
PhylomeDBi D3ZTD8.
TreeFami TF329951.

Enzyme and pathway databases

Reactomei REACT_238902. Other semaphorin interactions.

Miscellaneous databases

NextBioi 661717.
PROi D3ZTD8.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR016201. Plexin-like_fold.
IPR001627. Semap_dom.
IPR027231. Semaphorin.
IPR000884. Thrombospondin_1_rpt.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view ]
PANTHERi PTHR11036. PTHR11036. 1 hit.
Pfami PF01403. Sema. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view ]
SMARTi SM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
SM00209. TSP1. 6 hits.
[Graphical view ]
SUPFAMi SSF101912. SSF101912. 1 hit.
SSF103575. SSF103575. 1 hit.
SSF82895. SSF82895. 6 hits.
PROSITEi PS51004. SEMA. 1 hit.
PS50092. TSP1. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported and Sprague-DawleyImported.
  3. "Semaphorin 5A is a bifunctional axon guidance cue regulated by heparan and chondroitin sulfate proteoglycans."
    Kantor D.B., Chivatakarn O., Peer K.L., Oster S.F., Inatani M., Hansen M.J., Flanagan J.G., Yamaguchi Y., Sretavan D.W., Giger R.J., Kolodkin A.L.
    Neuron 44:961-975(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  4. "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through RhoGDIalpha-mediated inactivation of Rac1 GTPase."
    Li X., Lee A.Y.
    J. Biol. Chem. 285:32436-32445(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSEM5A_RAT
AccessioniPrimary (citable) accession number: D3ZTD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: April 20, 2010
Last modified: November 26, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3