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Q13591

- SEM5A_HUMAN

UniProt

Q13591 - SEM5A_HUMAN

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Protein

Semaphorin-5A

Gene

SEMA5A

Organism
Homo sapiens (Human)
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) By similarity. 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 similarity4 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. axon guidance Source: Reactome
  3. blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: UniProtKB
  4. cell adhesion Source: ProtInc
  5. cell-cell signaling Source: ProtInc
  6. cell chemotaxis Source: UniProtKB
  7. diencephalon development Source: UniProtKB
  8. negative regulation of axon extension involved in axon guidance Source: UniProtKB
  9. negative regulation of cell adhesion Source: UniProtKB
  10. negative regulation of endothelial cell apoptotic process Source: UniProtKB
  11. nervous system development Source: ProtInc
  12. patterning of blood vessels Source: Ensembl
  13. positive chemotaxis Source: UniProtKB
  14. positive regulation of actin filament depolymerization Source: UniProtKB
  15. positive regulation of angiogenesis Source: UniProtKB
  16. positive regulation of axon extension involved in axon guidance Source: UniProtKB
  17. positive regulation of catenin import into nucleus Source: UniProtKB
  18. positive regulation of endothelial cell chemotaxis Source: UniProtKB
  19. positive regulation of endothelial cell proliferation Source: UniProtKB
  20. positive regulation of protein kinase B signaling Source: UniProtKB
  21. signal clustering Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiREACT_19200. Other semaphorin interactions.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Semaphorin-5A
Alternative name(s):
Semaphorin-F
Short name:
Sema F
Gene namesi
Name:SEMA5A
Synonyms:SEMAF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:10736. SEMA5A.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti281. Monosomy 5p.
PharmGKBiPA35658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 10741052Semaphorin-5APRO_0000032335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 ↔ 114By similarity
Disulfide bondi131 ↔ 140By similarity
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi254 ↔ 357By similarity
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi278 ↔ 320By similarity
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi487 ↔ 504By similarity
Disulfide bondi496 ↔ 513By similarity
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi607 ↔ 644By similarity
Disulfide bondi611 ↔ 650By similarity
Disulfide bondi622 ↔ 634By similarity
Disulfide bondi665 ↔ 696By similarity
Disulfide bondi669 ↔ 701By similarity
Disulfide bondi680 ↔ 686By similarity
Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi796 ↔ 833By similarity
Disulfide bondi800 ↔ 838By similarity
Disulfide bondi811 ↔ 823By similarity
Disulfide bondi853 ↔ 890By similarity
Disulfide bondi857 ↔ 895By similarity
Disulfide bondi868 ↔ 880By similarity
Glycosylationi933 – 9331N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ13591.
PRIDEiQ13591.

PTM databases

PhosphoSiteiQ13591.

Expressioni

Gene expression databases

BgeeiQ13591.
CleanExiHS_SEMA5A.
ExpressionAtlasiQ13591. baseline and differential.
GenevestigatoriQ13591.

Organism-specific databases

HPAiHPA004632.

Interactioni

Subunit structurei

Binds PLXNB3.

Protein-protein interaction databases

BioGridi114501. 1 interaction.
IntActiQ13591. 1 interaction.
STRINGi9606.ENSP00000371936.

Structurei

3D structure databases

ProteinModelPortaliQ13591.
SMRiQ13591. Positions 68-506, 540-647, 656-723, 783-838, 840-940.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 968946ExtracellularSequence AnalysisAdd
BLAST
Topological domaini990 – 107485CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 484450SemaPROSITE-ProRule annotationAdd
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
Domaini707 – 76559TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini784 – 83956TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini841 – 89656TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini897 – 94448TSP type-1 7PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the semaphorin family.Curated
Contains 1 PSI domain.Curated
Contains 1 Sema domain.PROSITE-ProRule annotation
Contains 7 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG316291.
HOGENOMiHOG000047106.
HOVERGENiHBG062356.
InParanoidiQ13591.
KOiK06841.
OMAiYSNAYFT.
OrthoDBiEOG7SN8C0.
PhylomeDBiQ13591.
TreeFamiTF329951.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR016201. Plexin-like_fold.
IPR002165. Plexin_repeat.
IPR001627. Semap_dom.
IPR027231. Semaphorin.
IPR000884. Thrombospondin_1_rpt.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PANTHERiPTHR11036. PTHR11036. 1 hit.
PfamiPF01437. PSI. 1 hit.
PF01403. 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.

Q13591-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKGTCVIAWL FSSLGLWRLA HPEAQGTTQC QRTEHPVISY KEIGPWLREF
60 70 80 90 100
RAKNAVDFSQ LTFDPGQKEL VVGARNYLFR LQLEDLSLIQ AVEWECDEAT
110 120 130 140 150
KKACYSKGKS KEECQNYIRV LLVGGDRLFT CGTNAFTPVC TNRSLSNLTE
160 170 180 190 200
IHDQISGMAR CPYSPQHNST ALLTAGGELY AATAMDFPGR DPAIYRSLGI
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 VFNLSAIAQA FSGPFKYQEN SRSAWLPYPN
360 370 380 390 400
PNPHFQCGTV DQGLYVNLTE RNLQDAQKFI LMHEVVQPVT TVPSFMEDNS
410 420 430 440 450
RFSHVAVDVV QGREALVHII YLATDYGTIK KVRVPLNQTS SSCLLEEIEL
460 470 480 490 500
FPERRREPIR SLQILHSQSV LFVGLREHVV KIPLKRCQFY RTRSTCIGAQ
510 520 530 540 550
DPYCGWDVVM KKCTSLEESL SMTQWEQSIS ACPTRNLTVD GHFGVWSPWT
560 570 580 590 600
PCTHTDGSAV GSCLCRTRSC DSPAPQCGGW QCEGPGMEIA NCSRNGGWTP
610 620 630 640 650
WTSWSPCSTT CGIGFQVRQR SCSNPTPRHG GRVCVGQNRE ERYCNEHLLC
660 670 680 690 700
PPHMFWTGWG PWERCTAQCG GGIQARRRIC ENGPDCAGCN VEYQSCNTNP
710 720 730 740 750
CPELKKTTPW TPWTPVNISD NGGHYEQRFR YTCKARLADP NLLEVGRQRI
760 770 780 790 800
EMRYCSSDGT SGCSTDGLSG DFLRAGRYSA HTVNGAWSAW TSWSQCSRDC
810 820 830 840 850
SRGIRNRKRV CNNPEPKYGG MPCLGPSLEY QECNILPCPV DGVWSCWSPW
860 870 880 890 900
TKCSATCGGG HYMRTRSCSN PAPAYGGDIC LGLHTEEALC NTQPCPESWS
910 920 930 940 950
EWSDWSECEA SGVQVRARQC ILLFPMGSQC SGNTTESRPC VFDSNFIPEV
960 970 980 990 1000
SVARSSSVEE KRCGEFNMFH MIAVGLSSSI LGCLLTLLVY TYCQRYQQQS
1010 1020 1030 1040 1050
HDATVIHPVS PAPLNTSITN HINKLDKYDS VEAIKAFNKN NLILEERNKY
1060 1070
FNPHLTGKTY SNAYFTDLNN YDEY
Length:1,074
Mass (Da):120,615
Last modified:May 30, 2006 - v3
Checksum:iAE073413AC974CCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561V → A in AAC09473. (PubMed:9464278)Curated
Sequence conflicti149 – 1491T → A in AAC09473. (PubMed:9464278)Curated
Sequence conflicti382 – 3821M → V in AAC09473. (PubMed:9464278)Curated
Sequence conflicti494 – 4941S → R in AAC14668. (PubMed:15372022)Curated
Sequence conflicti723 – 7231G → D in AAC09473. (PubMed:9464278)Curated
Sequence conflicti835 – 8351I → T in AAC09473. (PubMed:9464278)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti246 – 2461V → L.
Corresponds to variant rs1806079 [ dbSNP | Ensembl ].
VAR_030294
Natural varianti792 – 7921S → L.
Corresponds to variant rs2290734 [ dbSNP | Ensembl ].
VAR_030295

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52840 mRNA. Translation: AAC09473.1.
AC004615 Genomic DNA. Translation: AAC14668.1.
AC022446 Genomic DNA. No translation available.
AC027336 Genomic DNA. No translation available.
AC091906 Genomic DNA. No translation available.
CH471102 Genomic DNA. Translation: EAX08078.1.
CH471102 Genomic DNA. Translation: EAX08079.1.
BC115696 mRNA. Translation: AAI15697.1.
CCDSiCCDS3875.1.
PIRiJC5928.
RefSeqiNP_003957.2. NM_003966.2.
XP_006714569.1. XM_006714506.1.
XP_006714570.1. XM_006714507.1.
UniGeneiHs.27621.

Genome annotation databases

EnsembliENST00000382496; ENSP00000371936; ENSG00000112902.
GeneIDi9037.
KEGGihsa:9037.
UCSCiuc003jek.2. human.

Polymorphism databases

DMDMi109939725.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52840 mRNA. Translation: AAC09473.1 .
AC004615 Genomic DNA. Translation: AAC14668.1 .
AC022446 Genomic DNA. No translation available.
AC027336 Genomic DNA. No translation available.
AC091906 Genomic DNA. No translation available.
CH471102 Genomic DNA. Translation: EAX08078.1 .
CH471102 Genomic DNA. Translation: EAX08079.1 .
BC115696 mRNA. Translation: AAI15697.1 .
CCDSi CCDS3875.1.
PIRi JC5928.
RefSeqi NP_003957.2. NM_003966.2.
XP_006714569.1. XM_006714506.1.
XP_006714570.1. XM_006714507.1.
UniGenei Hs.27621.

3D structure databases

ProteinModelPortali Q13591.
SMRi Q13591. Positions 68-506, 540-647, 656-723, 783-838, 840-940.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114501. 1 interaction.
IntActi Q13591. 1 interaction.
STRINGi 9606.ENSP00000371936.

PTM databases

PhosphoSitei Q13591.

Polymorphism databases

DMDMi 109939725.

Proteomic databases

PaxDbi Q13591.
PRIDEi Q13591.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000382496 ; ENSP00000371936 ; ENSG00000112902 .
GeneIDi 9037.
KEGGi hsa:9037.
UCSCi uc003jek.2. human.

Organism-specific databases

CTDi 9037.
GeneCardsi GC05M009036.
HGNCi HGNC:10736. SEMA5A.
HPAi HPA004632.
MIMi 609297. gene.
neXtProti NX_Q13591.
Orphaneti 281. Monosomy 5p.
PharmGKBi PA35658.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316291.
HOGENOMi HOG000047106.
HOVERGENi HBG062356.
InParanoidi Q13591.
KOi K06841.
OMAi YSNAYFT.
OrthoDBi EOG7SN8C0.
PhylomeDBi Q13591.
TreeFami TF329951.

Enzyme and pathway databases

Reactomei REACT_19200. Other semaphorin interactions.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GeneWikii SEMA5A.
GenomeRNAii 9037.
NextBioi 33851.
PROi Q13591.
SOURCEi Search...

Gene expression databases

Bgeei Q13591.
CleanExi HS_SEMA5A.
ExpressionAtlasi Q13591. baseline and differential.
Genevestigatori Q13591.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR016201. Plexin-like_fold.
IPR002165. Plexin_repeat.
IPR001627. Semap_dom.
IPR027231. Semaphorin.
IPR000884. Thrombospondin_1_rpt.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view ]
PANTHERi PTHR11036. PTHR11036. 1 hit.
Pfami PF01437. PSI. 1 hit.
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. "Molecular cloning and mapping of human semaphorin F from the Cri-du-chat candidate interval."
    Simmons A.D., Puschel A.W., McPherson J.D., Overhauser J., Lovett M.
    Biochem. Biophys. Res. Commun. 242:685-691(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: FUNCTION, INTERACTION WITH PLXNB3.
  6. "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.
  7. "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.
  8. "Semaphorin 5A and plexin-B3 regulate human glioma cell motility and morphology through Rac1 and the actin cytoskeleton."
    Li X., Law J.W., Lee A.Y.
    Oncogene 31:595-610(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSEM5A_HUMAN
AccessioniPrimary (citable) accession number: Q13591
Secondary accession number(s): D3DTC6, O60408, Q1RLL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2006
Last modified: October 29, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3