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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 similarity3 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

Names & Taxonomyi

Protein namesi
Recommended name:
Semaphorin-5A
Alternative name(s):
Semaphorin-F
Short name:
Sema F
Gene namesi
Name:Sema5a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi1308650. Sema5a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei969 – 98921Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 10741052Semaphorin-5A
PRO_0000420236Add
BLAST

Amino acid modifications

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

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 E15.5.2 Publications

Interactioni

Subunit structurei

Binds PLXNB3 By similarity.By similarity

Structurei

3D structure databases

ProteinModelPortaliD3ZTD8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 484450Sema
Add
BLAST
Domaini486 – 53348PSI
Add
BLAST
Domaini540 – 59354TSP type-1 1
Add
BLAST
Domaini595 – 65157TSP type-1 2
Add
BLAST
Domaini653 – 70250TSP type-1 3
Add
BLAST
Domaini784 – 83956TSP type-1 4
Add
BLAST
Domaini841 – 89656TSP type-1 5
Add
BLAST
Domaini897 – 94448TSP type-1 6
Add
BLAST

Sequence similaritiesi

Contains 1 PSI domain.
Contains 1 Sema domain.
Contains 6 TSP type-1 domains.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00690000101974.
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

MKGACILAWL FSSLGVWRLA RPETQDPAKC QRAEHPVVSY KEIGPWLREF     50
RAENAVDFSR LTFDPGQKEL VVGARNYLFR LQLEDLSLIQ AVQWECDEAT 100
KKACYSKGKS KEECQNYIRV LLVGGDRLFT CGTNAFTPVC TIRSLSNLTE 150
IHDQISGMAR CPYSPQHNST ALLTASGELY AATAMDFPGR DPAIYRSLGT 200
LPPLRTAQYN SKWLNEPNFV SSYDIGNFTY FFFRENAVEH DCGKTVFSRA 250
ARVCKNDIGG RFLLEDTWTT FMKARLNCSR PGEVPFYYNE LQSTFFLPEL 300
DLIYGIFTTN VNSIAASAVC VFNLSAISQA FNGPFKYQEN SRSAWLPYPN 350
PNPNFQCGTM DQGLYVNLTE RNLQDAQKFI LMHEVVQPVT TVPSFMEDNS 400
RFSHVAVDVV QGRDTLVHII YLATDYGTIK KVRAPLSQSS GSCLLEEIEL 450
FPERKSEPIR SLKILHSQSV LFVGLQEHVV KIPLKRCHFH QTRGACIGAQ 500
DPYCGWDAVM KKCTSLEESL SMTQWDQSVP TCPTRNLTVD GSFGPWSPWT 550
PCTHTDGTAV GSCLCRSRSC DSPAPQCGGW QCEGPRMEIT NCSRNGGWTP 600
WTSWSPCSTT CGIGFQVRQR SCSNPTPRHG GRVCVGQNRE ERYCNEHLLC 650
PPHVFWTGWG PWERCTAQCG GGIQARRRTC ENGPDCAGCN VEYQPCNTNA 700
CPELKKTTPW TPWTPVNISD NGGHYEQRFR YTCKARLPDP NLLEVGRQRI 750
EMRYCSSDGT SGCSTDGLSG DFLRAGRYSA HTVNGAWSAW TSWSQCSRDC 800
SRGIRNRKRV CNNPEPKYGG MPCLGPSLEF QECNILPCPV DGVWSCWSSW 850
SKCSATCGGG HYMRTRSCTN PAPAYGGDIC LGLHTEEALC NTQTCPENWS 900
EWSEWSVCDA SGTQVRTRQC ILLFPVGSQC SGNTTESRPC VFDSNFIPEV 950
SVARSSSVEE KRCGEFNMFH MMAVGLSSSI LGCLLTLLVY TYCQRYQQQS 1000
HDATVIHPVS PAALNSSITN HINKLDKYDS VEAIKAFNKN NLILEERNKY 1050
FNPHLTGKTY SNAYFTDLNN YDEY 1074
Length:1,074
Mass (Da):120,378
Last modified:April 20, 2010 - v1
Checksum:iBFFBCEB5F9084FF7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 ENSGT00690000101974.
KOi K06841.
OMAi YSNAYFT.
OrthoDBi EOG7SN8C0.
PhylomeDBi D3ZTD8.
TreeFami TF329951.

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 Norway.
  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 Norway and Sprague-Dawley.
  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: June 11, 2014
This is version 34 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

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