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Semaphorin-4D (A8) (BB18) (GR3) (CD antigen CD100)

 SEM4D_HUMAN             Reviewed;         862 AA.
Q92854; B2RPM6; Q7Z5S4; Q8N8B0;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
22-NOV-2017, entry version 185.
RecName: Full=Semaphorin-4D;
AltName: Full=A8;
AltName: Full=BB18;
AltName: Full=GR3;
AltName: CD_antigen=CD100;
Flags: Precursor;
Name=SEMA4D; Synonyms=C9orf164, CD100, SEMAJ;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=T-cell;
PubMed=8876214; DOI=10.1073/pnas.93.21.11780;
Hall K.T., Boumsell L., Schultze J.L., Boussiotis V.A., Dorfman D.M.,
Cardoso A.A., Bensussan A., Nadler L.M., Freeman G.J.;
"Human CD100, a novel leukocyte semaphorin that promotes B-cell
aggregation and differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 93:11780-11785(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
INTERACTION WITH PLXNB1.
PubMed=10520995; DOI=10.1016/S0092-8674(00)80063-X;
Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L.,
Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M.,
Tessier-Lavigne M., Comoglio P.M.;
"Plexins are a large family of receptors for transmembrane, secreted
and GPI-anchored semaphorins in vertebrates.";
Cell 99:71-80(1999).
[6]
FUNCTION.
PubMed=16055703; DOI=10.1128/MCB.25.16.6889-6898.2005;
Basile J.R., Afkhami T., Gutkind J.S.;
"Semaphorin 4D/plexin-B1 induces endothelial cell migration through
the activation of PYK2, Src, and the phosphatidylinositol 3-kinase-Akt
pathway.";
Mol. Cell. Biol. 25:6889-6898(2005).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-419.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[8]
FUNCTION.
PubMed=19788569; DOI=10.1111/j.1460-9568.2009.06934.x;
Vodrazka P., Korostylev A., Hirschberg A., Swiercz J.M., Worzfeld T.,
Deng S., Fazzari P., Tamagnone L., Offermanns S., Kuner R.;
"The semaphorin 4D-plexin-B signalling complex regulates dendritic and
axonal complexity in developing neurons via diverse pathways.";
Eur. J. Neurosci. 30:1193-1208(2009).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49; ASN-74; ASN-77;
ASN-379 AND ASN-419.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-684, AND DISULFIDE BONDS.
PubMed=12958590; DOI=10.1038/nsb977;
Love C.A., Harlos K., Mavaddat N., Davis S.J., Stuart D.I.,
Jones E.Y., Esnouf R.M.;
"The ligand-binding face of the semaphorins revealed by the high-
resolution crystal structure of SEMA4D.";
Nat. Struct. Biol. 10:843-848(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 22-677 IN COMPLEX WITH
PLXNB1, SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF
100-LYS-GLY-101; 181-PHE-LEU-182; PHE-244; PHE-246 AND LYS-395,
GLYCOSYLATION AT ASN-49; ASN-77; ASN-139; ASN-191; ASN-329 AND
ASN-419, AND DISULFIDE BONDS.
PubMed=20877282; DOI=10.1038/nature09468;
Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H.,
Mitchell K.J., Siebold C., Jones E.Y.;
"Structural basis of semaphorin-plexin signalling.";
Nature 467:1118-1122(2010).
-!- FUNCTION: Cell surface receptor for PLXN1B and PLXNB2 that plays
an important role in cell-cell signaling. Promotes reorganization
of the actin cytoskeleton and plays a role in axonal growth cone
guidance in the developing central nervous system. Regulates
dendrite and axon branching and morphogenesis. Promotes the
migration of cerebellar granule cells and of endothelial cells.
Plays a role in the immune system; induces B-cells to aggregate
and improves their viability (in vitro). Promotes signaling via
SRC and PTK2B/PYK2, which then mediates activation of
phosphatidylinositol 3-kinase and of the AKT1 signaling cascade.
Interaction with PLXNB1 mediates activation of RHOA.
{ECO:0000269|PubMed:16055703, ECO:0000269|PubMed:19788569,
ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:8876214}.
-!- SUBUNIT: Homodimer. Interacts with PLXNB2 (By similarity). Binds
PLXNB1. {ECO:0000250, ECO:0000269|PubMed:10520995,
ECO:0000269|PubMed:20877282}.
-!- INTERACTION:
O43157-1:PLXNB1; NbExp=3; IntAct=EBI-15880903, EBI-15880891;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20877282,
ECO:0000269|PubMed:8876214}; Single-pass type I membrane protein
{ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:8876214}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92854-1; Sequence=Displayed;
Name=2;
IsoId=Q92854-2; Sequence=VSP_039483, VSP_039484;
-!- TISSUE SPECIFICITY: Strongly expressed in skeletal muscle,
peripheral blood lymphocytes, spleen, and thymus and also
expressed at lower levels in testes, brain, kidney, small
intestine, prostate, heart, placenta, lung and pancreas, but not
in colon and liver. {ECO:0000269|PubMed:8876214}.
-!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI37516.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
Sequence=AAI37519.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
Sequence=BAC04938.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
Sequence=CAI95794.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SEMA4DID42255ch9q22.html";
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EMBL; U60800; AAC50810.1; -; mRNA.
EMBL; AL590233; CAI17379.2; -; Genomic_DNA.
EMBL; AL929575; CAI43250.2; -; Genomic_DNA.
EMBL; AL929575; CAI95794.1; ALT_SEQ; Genomic_DNA.
EMBL; BC054500; AAH54500.1; -; mRNA.
EMBL; BC137515; AAI37516.1; ALT_SEQ; mRNA.
EMBL; BC137518; AAI37519.1; ALT_SEQ; mRNA.
EMBL; AK097056; BAC04938.1; ALT_SEQ; mRNA.
CCDS; CCDS47991.1; -. [Q92854-2]
CCDS; CCDS6685.1; -. [Q92854-1]
RefSeq; NP_001135759.1; NM_001142287.1. [Q92854-2]
RefSeq; NP_006369.3; NM_006378.3. [Q92854-1]
RefSeq; XP_005251711.1; XM_005251654.3. [Q92854-1]
RefSeq; XP_011516425.1; XM_011518123.2. [Q92854-1]
RefSeq; XP_011516426.1; XM_011518124.2. [Q92854-1]
RefSeq; XP_011516427.1; XM_011518125.1. [Q92854-1]
RefSeq; XP_011516429.1; XM_011518127.2. [Q92854-1]
RefSeq; XP_011516430.1; XM_011518128.2. [Q92854-1]
RefSeq; XP_011516431.1; XM_011518129.1. [Q92854-1]
RefSeq; XP_011516432.1; XM_011518130.2. [Q92854-1]
RefSeq; XP_011516433.1; XM_011518131.2. [Q92854-1]
RefSeq; XP_011516435.1; XM_011518133.2. [Q92854-1]
RefSeq; XP_011516436.1; XM_011518134.2. [Q92854-1]
RefSeq; XP_016869682.1; XM_017014193.1. [Q92854-1]
RefSeq; XP_016869683.1; XM_017014194.1. [Q92854-1]
RefSeq; XP_016869684.1; XM_017014195.1. [Q92854-1]
RefSeq; XP_016869685.1; XM_017014196.1. [Q92854-1]
RefSeq; XP_016869686.1; XM_017014197.1. [Q92854-1]
RefSeq; XP_016869687.1; XM_017014198.1. [Q92854-1]
UniGene; Hs.494406; -.
PDB; 1OLZ; X-ray; 2.00 A; A/B=22-677.
PDB; 3OL2; X-ray; 2.99 A; A=22-677.
PDBsum; 1OLZ; -.
PDBsum; 3OL2; -.
ProteinModelPortal; Q92854; -.
SMR; Q92854; -.
BioGrid; 115766; 12.
CORUM; Q92854; -.
DIP; DIP-59221N; -.
IntAct; Q92854; 4.
STRING; 9606.ENSP00000348822; -.
GuidetoPHARMACOLOGY; 2883; -.
iPTMnet; Q92854; -.
PhosphoSitePlus; Q92854; -.
SwissPalm; Q92854; -.
BioMuta; SEMA4D; -.
DMDM; 8134701; -.
EPD; Q92854; -.
MaxQB; Q92854; -.
PaxDb; Q92854; -.
PeptideAtlas; Q92854; -.
PRIDE; Q92854; -.
Ensembl; ENST00000339861; ENSP00000344923; ENSG00000187764. [Q92854-2]
Ensembl; ENST00000356444; ENSP00000348822; ENSG00000187764. [Q92854-1]
Ensembl; ENST00000420987; ENSP00000391733; ENSG00000187764. [Q92854-2]
Ensembl; ENST00000422704; ENSP00000388768; ENSG00000187764. [Q92854-1]
Ensembl; ENST00000438547; ENSP00000405102; ENSG00000187764. [Q92854-1]
Ensembl; ENST00000450295; ENSP00000416523; ENSG00000187764. [Q92854-1]
Ensembl; ENST00000455551; ENSP00000411981; ENSG00000187764. [Q92854-2]
GeneID; 10507; -.
KEGG; hsa:10507; -.
UCSC; uc004aqo.2; human. [Q92854-1]
CTD; 10507; -.
DisGeNET; 10507; -.
EuPathDB; HostDB:ENSG00000187764.11; -.
GeneCards; SEMA4D; -.
HGNC; HGNC:10732; SEMA4D.
HPA; HPA015662; -.
HPA; HPA023277; -.
MIM; 601866; gene.
neXtProt; NX_Q92854; -.
OpenTargets; ENSG00000187764; -.
PharmGKB; PA35654; -.
eggNOG; KOG3611; Eukaryota.
eggNOG; ENOG410XQZC; LUCA.
GeneTree; ENSGT00760000118854; -.
HOGENOM; HOG000111669; -.
HOVERGEN; HBG061627; -.
InParanoid; Q92854; -.
KO; K06521; -.
OMA; FCQATGP; -.
OrthoDB; EOG091G01W0; -.
PhylomeDB; Q92854; -.
TreeFam; TF316102; -.
Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-416700; Other semaphorin interactions.
SIGNOR; Q92854; -.
ChiTaRS; SEMA4D; human.
EvolutionaryTrace; Q92854; -.
GeneWiki; SEMA4D; -.
GenomeRNAi; 10507; -.
PRO; PR:Q92854; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000187764; -.
CleanEx; HS_SEMA4D; -.
ExpressionAtlas; Q92854; baseline and differential.
Genevisible; Q92854; HS.
GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004872; F:receptor activity; IDA:HGNC.
GO; GO:0005102; F:receptor binding; IDA:UniProtKB.
GO; GO:0030215; F:semaphorin receptor binding; IPI:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0070486; P:leukocyte aggregation; IMP:UniProtKB.
GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0043931; P:ossification involved in bone maturation; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0048672; P:positive regulation of collateral sprouting; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0031344; P:regulation of cell projection organization; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:UniProtKB.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IDA:UniProtKB.
GO; GO:1900220; P:semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis; ISS:BHF-UCL.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR002165; Plexin_repeat.
InterPro; IPR016201; PSI.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR027231; Semaphorin.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR11036; PTHR11036; 1.
Pfam; PF00047; ig; 1.
Pfam; PF01437; PSI; 1.
Pfam; PF01403; Sema; 1.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00423; PSI; 1.
SMART; SM00630; Sema; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 862 Semaphorin-4D.
/FTId=PRO_0000032327.
TOPO_DOM 22 734 Extracellular. {ECO:0000255}.
TRANSMEM 735 755 Helical. {ECO:0000255}.
TOPO_DOM 756 862 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 500 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 502 551 PSI.
DOMAIN 554 636 Ig-like C2-type.
MOD_RES 833 833 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:20877282}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:20877282}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20877282}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20877282}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20877282}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 419 419 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:20877282}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 632 632 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 97 108
DISULFID 126 135
DISULFID 257 370
DISULFID 281 326
DISULFID 503 520
DISULFID 509 553
DISULFID 512 529
DISULFID 576 624
VAR_SEQ 555 738 DKSKGSYRQHFFKHGGTAELKCSQKSNLARVFWKFQNGVLK
AESPKYGLMGRKNLLIFNLSEGDSGVYQCLSEERVKNKTVF
QVVAKHVLEVKVVPKPVVAPTLSVVQTEGSRIATKVLVAST
QGSSPPTPAVQATSSGAITLPPKPAPTGTSCEPKIVINTVP
QLHSEKTMYLKSSDNRLLMS -> ASSPKPLPPPGSSSLSC
LGHVGDRRLSSPWTPWPASGAGPDSSSRVSLLPPFLSDQAQ
HVHALGNFYLFCQATGPADIRFVWEKNGRALETCVPVQTHA
LPDGRAHALSWLQDAIRESAEYRCSVLSSAGNKTSKVQVAV
MRPEVTHQERWTRELSAWRAVAGEHDRMMQSWRKAWESCSK
DTL (in isoform 2). {ECO:0000305}.
/FTId=VSP_039483.
VAR_SEQ 739 862 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_039484.
VARIANT 72 72 A -> T (in dbSNP:rs13284404).
/FTId=VAR_030293.
VARIANT 327 327 A -> T (in dbSNP:rs11526468).
/FTId=VAR_057175.
MUTAGEN 100 101 KG->DT: Abolishes PLXNB1 binding.
{ECO:0000269|PubMed:20877282}.
MUTAGEN 181 182 FL->ER: Abolishes PLXNB1 binding.
{ECO:0000269|PubMed:20877282}.
MUTAGEN 244 244 F->N: Abolishes homodimerization,
abolishes collapse of growth cones and
reduces PLXNB1 binding; when associated
with S-246.
{ECO:0000269|PubMed:20877282}.
MUTAGEN 246 246 F->S: Abolishes homodimerization,
abolishes collapse of growth cones and
reduces PLXNB1 binding; when associated
with N-244.
{ECO:0000269|PubMed:20877282}.
MUTAGEN 395 395 K->E: Strongly reduces PLXNB1 binding.
{ECO:0000269|PubMed:20877282}.
CONFLICT 592 592 G -> D (in Ref. 3; AAH54500).
{ECO:0000305}.
STRAND 29 32 {ECO:0000244|PDB:1OLZ}.
TURN 34 36 {ECO:0000244|PDB:1OLZ}.
STRAND 40 42 {ECO:0000244|PDB:1OLZ}.
STRAND 52 55 {ECO:0000244|PDB:1OLZ}.
STRAND 59 65 {ECO:0000244|PDB:1OLZ}.
STRAND 67 74 {ECO:0000244|PDB:1OLZ}.
STRAND 77 86 {ECO:0000244|PDB:1OLZ}.
HELIX 91 99 {ECO:0000244|PDB:1OLZ}.
TURN 104 107 {ECO:0000244|PDB:1OLZ}.
STRAND 111 117 {ECO:0000244|PDB:1OLZ}.
STRAND 119 127 {ECO:0000244|PDB:1OLZ}.
TURN 129 131 {ECO:0000244|PDB:1OLZ}.
STRAND 134 139 {ECO:0000244|PDB:1OLZ}.
TURN 140 143 {ECO:0000244|PDB:1OLZ}.
TURN 153 155 {ECO:0000244|PDB:1OLZ}.
STRAND 164 169 {ECO:0000244|PDB:1OLZ}.
STRAND 172 180 {ECO:0000244|PDB:1OLZ}.
STRAND 185 191 {ECO:0000244|PDB:1OLZ}.
STRAND 193 195 {ECO:0000244|PDB:3OL2}.
TURN 203 205 {ECO:0000244|PDB:1OLZ}.
STRAND 210 217 {ECO:0000244|PDB:1OLZ}.
STRAND 230 238 {ECO:0000244|PDB:1OLZ}.
STRAND 249 257 {ECO:0000244|PDB:1OLZ}.
STRAND 264 267 {ECO:0000244|PDB:1OLZ}.
STRAND 275 279 {ECO:0000244|PDB:1OLZ}.
HELIX 284 286 {ECO:0000244|PDB:1OLZ}.
STRAND 292 299 {ECO:0000244|PDB:1OLZ}.
STRAND 308 314 {ECO:0000244|PDB:1OLZ}.
STRAND 316 318 {ECO:0000244|PDB:1OLZ}.
STRAND 320 329 {ECO:0000244|PDB:1OLZ}.
HELIX 330 339 {ECO:0000244|PDB:1OLZ}.
STRAND 342 346 {ECO:0000244|PDB:1OLZ}.
TURN 349 351 {ECO:0000244|PDB:3OL2}.
STRAND 354 357 {ECO:0000244|PDB:1OLZ}.
HELIX 373 376 {ECO:0000244|PDB:1OLZ}.
TURN 377 379 {ECO:0000244|PDB:1OLZ}.
HELIX 383 385 {ECO:0000244|PDB:1OLZ}.
HELIX 388 396 {ECO:0000244|PDB:1OLZ}.
STRAND 399 404 {ECO:0000244|PDB:1OLZ}.
HELIX 407 409 {ECO:0000244|PDB:1OLZ}.
STRAND 412 417 {ECO:0000244|PDB:1OLZ}.
STRAND 420 429 {ECO:0000244|PDB:1OLZ}.
STRAND 431 433 {ECO:0000244|PDB:3OL2}.
STRAND 435 443 {ECO:0000244|PDB:1OLZ}.
STRAND 446 453 {ECO:0000244|PDB:1OLZ}.
STRAND 455 465 {ECO:0000244|PDB:1OLZ}.
STRAND 475 478 {ECO:0000244|PDB:1OLZ}.
STRAND 481 484 {ECO:0000244|PDB:1OLZ}.
STRAND 486 490 {ECO:0000244|PDB:1OLZ}.
STRAND 495 500 {ECO:0000244|PDB:1OLZ}.
HELIX 503 505 {ECO:0000244|PDB:1OLZ}.
HELIX 509 514 {ECO:0000244|PDB:1OLZ}.
STRAND 520 523 {ECO:0000244|PDB:1OLZ}.
TURN 524 527 {ECO:0000244|PDB:1OLZ}.
STRAND 528 531 {ECO:0000244|PDB:1OLZ}.
TURN 532 534 {ECO:0000244|PDB:1OLZ}.
HELIX 539 541 {ECO:0000244|PDB:1OLZ}.
HELIX 550 552 {ECO:0000244|PDB:1OLZ}.
STRAND 553 555 {ECO:0000244|PDB:1OLZ}.
STRAND 560 567 {ECO:0000244|PDB:1OLZ}.
STRAND 572 574 {ECO:0000244|PDB:1OLZ}.
STRAND 584 593 {ECO:0000244|PDB:1OLZ}.
STRAND 598 602 {ECO:0000244|PDB:1OLZ}.
TURN 604 607 {ECO:0000244|PDB:1OLZ}.
STRAND 609 611 {ECO:0000244|PDB:1OLZ}.
HELIX 616 618 {ECO:0000244|PDB:1OLZ}.
STRAND 620 629 {ECO:0000244|PDB:1OLZ}.
STRAND 631 647 {ECO:0000244|PDB:1OLZ}.
SEQUENCE 862 AA; 96150 MW; 7B18EFEA98789371 CRC64;
MRMCTPIRGL LMALAVMFGT AMAFAPIPRI TWEHREVHLV QFHEPDIYNY SALLLSEDKD
TLYIGAREAV FAVNALNISE KQHEVYWKVS EDKKAKCAEK GKSKQTECLN YIRVLQPLSA
TSLYVCGTNA FQPACDHLNL TSFKFLGKNE DGKGRCPFDP AHSYTSVMVD GELYSGTSYN
FLGSEPIISR NSSHSPLRTE YAIPWLNEPS FVFADVIRKS PDSPDGEDDR VYFFFTEVSV
EYEFVFRVLI PRIARVCKGD QGGLRTLQKK WTSFLKARLI CSRPDSGLVF NVLRDVFVLR
SPGLKVPVFY ALFTPQLNNV GLSAVCAYNL STAEEVFSHG KYMQSTTVEQ SHTKWVRYNG
PVPKPRPGAC IDSEARAANY TSSLNLPDKT LQFVKDHPLM DDSVTPIDNR PRLIKKDVNY
TQIVVDRTQA LDGTVYDVMF VSTDRGALHK AISLEHAVHI IEETQLFQDF EPVQTLLLSS
KKGNRFVYAG SNSGVVQAPL AFCGKHGTCE DCVLARDPYC AWSPPTATCV ALHQTESPSR
GLIQEMSGDA SVCPDKSKGS YRQHFFKHGG TAELKCSQKS NLARVFWKFQ NGVLKAESPK
YGLMGRKNLL IFNLSEGDSG VYQCLSEERV KNKTVFQVVA KHVLEVKVVP KPVVAPTLSV
VQTEGSRIAT KVLVASTQGS SPPTPAVQAT SSGAITLPPK PAPTGTSCEP KIVINTVPQL
HSEKTMYLKS SDNRLLMSLF LFFFVLFLCL FFYNCYKGYL PRQCLKFRSA LLIGKKKPKS
DFCDREQSLK ETLVEPGSFS QQNGEHPKPA LDTGYETEQD TITSKVPTDR EDSQRIDDLS
ARDKPFDVKC ELKFADSDAD GD


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