Q92854 (SEM4D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Semaphorin-4D

Alternative name(s):
A8
BB18
GR3
CD_antigen=CD100

Gene names

Name:	SEMA4D
Synonyms:	C9orf164, CD100, SEMAJ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	862 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.8 Ref.11
Subunit structure	Homodimer. Interacts with PLXNB2 By similarity. Binds PLXNB1. Ref.5 Ref.11
Subcellular location	Cell membrane; Single-pass type I membrane protein Ref.1 Ref.11.
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. Ref.1
Sequence similarities	Belongs to the semaphorin family. Contains 1 Ig-like C2-type (immunoglobulin-like) domain. Contains 1 PSI domain. Contains 1 Sema domain.
Sequence caution	The sequence AAI37516.1 differs from that shown. Reason: Cloning artifact. The sequence AAI37519.1 differs from that shown. Reason: Cloning artifact. The sequence BAC04938.1 differs from that shown. Reason: Cloning artifact. The sequence CAI95794.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome immune response Traceable author statement Ref.1. Source: ProtInc leukocyte aggregation Inferred from mutant phenotype Ref.1. Source: UniProtKB negative regulation of alkaline phosphatase activity Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL negative regulation of apoptotic process Traceable author statement Ref.1. Source: ProtInc negative regulation of osteoblast differentiation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL ossification involved in bone maturation Inferred from mutant phenotype PubMed 22019888. Source: BHF-UCL positive regulation of Rho GTPase activity Inferred from mutant phenotype Ref.8. Source: UniProtKB positive regulation of cell migration Inferred from direct assay Ref.6. Source: UniProtKB positive regulation of collateral sprouting Inferred from mutant phenotype Ref.8. Source: UniProtKB positive regulation of peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase cascade Inferred from mutant phenotype Ref.6. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype Ref.11. Source: UniProtKB regulation of dendrite morphogenesis Inferred from mutant phenotype Ref.8. Source: UniProtKB semaphorin-plexin signaling pathway involved in bone trabecula morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	extracellular space Inferred from sequence or structural similarity. Source: BHF-UCL integral to plasma membrane Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	semaphorin receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL transmembrane signaling receptor activity Inferred from mutant phenotype Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92854-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q92854-2)

The sequence of this isoform differs from the canonical sequence as follows:
     555-738: DKSKGSYRQH...KSSDNRLLMS → ASSPKPLPPP...AWESCSKDTL
     739-862: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 862

841

Semaphorin-4D

PRO_0000032327

Regions

Topological domain

22 – 734

713

Extracellular Potential

Transmembrane

735 – 755

21

Helical; Potential

Topological domain

756 – 862

107

Cytoplasmic Potential

Domain

22 – 500

479

Sema

Domain

502 – 551

50

PSI

Domain

554 – 636

83

Ig-like C2-type

Amino acid modifications

Glycosylation

49

1

N-linked (GlcNAc...) Ref.9 Ref.11

Glycosylation

74

1

N-linked (GlcNAc...) Ref.9

Glycosylation

77

1

N-linked (GlcNAc...) Ref.9 Ref.11

Glycosylation

139

1

N-linked (GlcNAc...) Ref.11

Glycosylation

191

1

N-linked (GlcNAc...) Ref.11

Glycosylation

329

1

N-linked (GlcNAc...) Ref.11

Glycosylation

379

1

N-linked (GlcNAc...) Ref.9

Glycosylation

419

1

N-linked (GlcNAc...) Ref.7 Ref.9 Ref.11

Glycosylation

613

1

N-linked (GlcNAc...) Potential

Glycosylation

632

1

N-linked (GlcNAc...) Potential

Disulfide bond

97 ↔ 108

Ref.10 Ref.11

Disulfide bond

126 ↔ 135

Ref.10 Ref.11

Disulfide bond

257 ↔ 370

Ref.10 Ref.11

Disulfide bond

281 ↔ 326

Ref.10 Ref.11

Disulfide bond

503 ↔ 520

Ref.10 Ref.11

Disulfide bond

509 ↔ 553

Ref.10 Ref.11

Disulfide bond

512 ↔ 529

Ref.10 Ref.11

Disulfide bond

576 ↔ 624

Ref.10 Ref.11

Natural variations

Alternative sequence

555 – 738

184

DKSKG…RLLMS → ASSPKPLPPPGSSSLSCLGH VGDRRLSSPWTPWPASGAGP DSSSRVSLLPPFLSDQAQHV HALGNFYLFCQATGPADIRF VWEKNGRALETCVPVQTHAL PDGRAHALSWLQDAIRESAE YRCSVLSSAGNKTSKVQVAV MRPEVTHQERWTRELSAWRA VAGEHDRMMQSWRKAWESCS KDTL in isoform 2.

VSP_039483

Alternative sequence

739 – 862

124

Missing in isoform 2.

VSP_039484

Natural variant

72

1

A → T.
Corresponds to variant rs13284404 [ dbSNP | Ensembl ].

VAR_030293

Natural variant

327

1

A → T.
Corresponds to variant rs11526468 [ dbSNP | Ensembl ].

VAR_057175

Experimental info

Mutagenesis

100 – 101

2

KG → DT: Abolishes PLXNB1 binding.

Mutagenesis

181 – 182

2

FL → ER: Abolishes PLXNB1 binding.

Mutagenesis

244

1

F → N: Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with S-246. Ref.11

Mutagenesis

246

1

F → S: Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with N-244. Ref.11

Mutagenesis

395

1

K → E: Strongly reduces PLXNB1 binding. Ref.11

Sequence conflict

592

1

G → D in AAH54500. Ref.3

Secondary structure

1

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862

Helix Strand Turn

Details...

Beta strand

29 – 32

4

Turn

34 – 36

3

Beta strand

40 – 42

3

Beta strand

52 – 55

4

Beta strand

59 – 65

7

Beta strand

67 – 74

8

Beta strand

77 – 86

10

Helix

91 – 99

9

Turn

104 – 107

4

Beta strand

111 – 117

7

Beta strand

119 – 127

9

Turn

129 – 131

3

Beta strand

134 – 139

6

Turn

140 – 143

4

Turn

153 – 155

3

Beta strand

164 – 169

6

Beta strand

172 – 180

9

Beta strand

185 – 191

7

Beta strand

193 – 195

3

Turn

203 – 205

3

Beta strand

210 – 217

8

Beta strand

230 – 238

9

Beta strand

249 – 257

9

Beta strand

264 – 267

4

Beta strand

275 – 279

5

Helix

284 – 286

3

Beta strand

292 – 299

8

Beta strand

308 – 314

7

Beta strand

316 – 318

3

Beta strand

320 – 329

10

Helix

330 – 339

10

Beta strand

342 – 346

5

Turn

349 – 351

3

Beta strand

354 – 357

4

Helix

373 – 376

4

Turn

377 – 379

3

Helix

383 – 385

3

Helix

388 – 396

9

Beta strand

399 – 404

6

Helix

407 – 409

3

Beta strand

412 – 417

6

Beta strand

420 – 429

10

Beta strand

431 – 433

3

Beta strand

435 – 443

9

Beta strand

446 – 453

8

Beta strand

455 – 465

11

Beta strand

475 – 478

4

Beta strand

481 – 484

4

Beta strand

486 – 490

5

Beta strand

495 – 500

6

Helix

503 – 505

3

Helix

509 – 514

6

Beta strand

520 – 523

4

Turn

524 – 527

4

Beta strand

528 – 531

4

Turn

532 – 534

3

Helix

539 – 541

3

Helix

550 – 552

3

Beta strand

553 – 555

3

Beta strand

560 – 567

8

Beta strand

572 – 574

3

Beta strand

584 – 593

10

Beta strand

598 – 602

5

Turn

604 – 607

4

Beta strand

609 – 611

3

Helix

616 – 618

3

Beta strand

620 – 629

10

Beta strand

631 – 647

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 7B18EFEA98789371	FASTA	862	96,150
	10 20 30 40 50 60 MRMCTPIRGL LMALAVMFGT AMAFAPIPRI TWEHREVHLV QFHEPDIYNY SALLLSEDKD 70 80 90 100 110 120 TLYIGAREAV FAVNALNISE KQHEVYWKVS EDKKAKCAEK GKSKQTECLN YIRVLQPLSA 130 140 150 160 170 180 TSLYVCGTNA FQPACDHLNL TSFKFLGKNE DGKGRCPFDP AHSYTSVMVD GELYSGTSYN 190 200 210 220 230 240 FLGSEPIISR NSSHSPLRTE YAIPWLNEPS FVFADVIRKS PDSPDGEDDR VYFFFTEVSV 250 260 270 280 290 300 EYEFVFRVLI PRIARVCKGD QGGLRTLQKK WTSFLKARLI CSRPDSGLVF NVLRDVFVLR 310 320 330 340 350 360 SPGLKVPVFY ALFTPQLNNV GLSAVCAYNL STAEEVFSHG KYMQSTTVEQ SHTKWVRYNG 370 380 390 400 410 420 PVPKPRPGAC IDSEARAANY TSSLNLPDKT LQFVKDHPLM DDSVTPIDNR PRLIKKDVNY 430 440 450 460 470 480 TQIVVDRTQA LDGTVYDVMF VSTDRGALHK AISLEHAVHI IEETQLFQDF EPVQTLLLSS 490 500 510 520 530 540 KKGNRFVYAG SNSGVVQAPL AFCGKHGTCE DCVLARDPYC AWSPPTATCV ALHQTESPSR 550 560 570 580 590 600 GLIQEMSGDA SVCPDKSKGS YRQHFFKHGG TAELKCSQKS NLARVFWKFQ NGVLKAESPK 610 620 630 640 650 660 YGLMGRKNLL IFNLSEGDSG VYQCLSEERV KNKTVFQVVA KHVLEVKVVP KPVVAPTLSV 670 680 690 700 710 720 VQTEGSRIAT KVLVASTQGS SPPTPAVQAT SSGAITLPPK PAPTGTSCEP KIVINTVPQL 730 740 750 760 770 780 HSEKTMYLKS SDNRLLMSLF LFFFVLFLCL FFYNCYKGYL PRQCLKFRSA LLIGKKKPKS 790 800 810 820 830 840 DFCDREQSLK ETLVEPGSFS QQNGEHPKPA LDTGYETEQD TITSKVPTDR EDSQRIDDLS 850 860 ARDKPFDVKC ELKFADSDAD GD
	Isoform 2 [UniParc]. Checksum: 93ED5D62D6A17ED1	FASTA	738	82,164
	10 20 30 40 50 60 MRMCTPIRGL LMALAVMFGT AMAFAPIPRI TWEHREVHLV QFHEPDIYNY SALLLSEDKD 70 80 90 100 110 120 TLYIGAREAV FAVNALNISE KQHEVYWKVS EDKKAKCAEK GKSKQTECLN YIRVLQPLSA 130 140 150 160 170 180 TSLYVCGTNA FQPACDHLNL TSFKFLGKNE DGKGRCPFDP AHSYTSVMVD GELYSGTSYN 190 200 210 220 230 240 FLGSEPIISR NSSHSPLRTE YAIPWLNEPS FVFADVIRKS PDSPDGEDDR VYFFFTEVSV 250 260 270 280 290 300 EYEFVFRVLI PRIARVCKGD QGGLRTLQKK WTSFLKARLI CSRPDSGLVF NVLRDVFVLR 310 320 330 340 350 360 SPGLKVPVFY ALFTPQLNNV GLSAVCAYNL STAEEVFSHG KYMQSTTVEQ SHTKWVRYNG 370 380 390 400 410 420 PVPKPRPGAC IDSEARAANY TSSLNLPDKT LQFVKDHPLM DDSVTPIDNR PRLIKKDVNY 430 440 450 460 470 480 TQIVVDRTQA LDGTVYDVMF VSTDRGALHK AISLEHAVHI IEETQLFQDF EPVQTLLLSS 490 500 510 520 530 540 KKGNRFVYAG SNSGVVQAPL AFCGKHGTCE DCVLARDPYC AWSPPTATCV ALHQTESPSR 550 560 570 580 590 600 GLIQEMSGDA SVCPASSPKP LPPPGSSSLS CLGHVGDRRL SSPWTPWPAS GAGPDSSSRV 610 620 630 640 650 660 SLLPPFLSDQ AQHVHALGNF YLFCQATGPA DIRFVWEKNG RALETCVPVQ THALPDGRAH 670 680 690 700 710 720 ALSWLQDAIR ESAEYRCSVL SSAGNKTSKV QVAVMRPEVT HQERWTRELS AWRAVAGEHD 730 RMMQSWRKAW ESCSKDTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human CD100, a novel leukocyte semaphorin that promotes B-cell aggregation and differentiation." 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. Proc. Natl. Acad. Sci. U.S.A. 93:11780-11785(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: T-cell.
[2]	"DNA sequence and analysis of human chromosome 9." 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. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain and Eye.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Small intestine.
[5]	"Plexins are a large family of receptors for transmembrane, secreted and GPI-anchored semaphorins in vertebrates." 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. Cell 99:71-80(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLXNB1.
[6]	"Semaphorin 4D/plexin-B1 induces endothelial cell migration through the activation of PYK2, Src, and the phosphatidylinositol 3-kinase-Akt pathway." Basile J.R., Afkhami T., Gutkind J.S. Mol. Cell. Biol. 25:6889-6898(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-419, MASS SPECTROMETRY. Tissue: Platelet.
[8]	"The semaphorin 4D-plexin-B signalling complex regulates dendritic and axonal complexity in developing neurons via diverse pathways." Vodrazka P., Korostylev A., Hirschberg A., Swiercz J.M., Worzfeld T., Deng S., Fazzari P., Tamagnone L., Offermanns S., Kuner R. Eur. J. Neurosci. 30:1193-1208(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49; ASN-74; ASN-77; ASN-379 AND ASN-419, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D." Love C.A., Harlos K., Mavaddat N., Davis S.J., Stuart D.I., Jones E.Y., Esnouf R.M. Nat. Struct. Biol. 10:843-848(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-684, DISULFIDE BONDS.
[11]	"Structural basis of semaphorin-plexin signalling." Janssen B.J., Robinson R.A., Perez-Branguli F., Bell C.H., Mitchell K.J., Siebold C., Jones E.Y. Nature 467:1118-1122(2010) [PubMed] [Europe PMC] [Abstract] Cited for: 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, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U60800 mRNA. Translation: AAC50810.1.
AL590233 Genomic DNA. Translation: CAI17379.2.
AL929575 Genomic DNA. Translation: CAI43250.2.
AL929575 Genomic DNA. Translation: CAI95794.1. Sequence problems.
BC054500 mRNA. Translation: AAH54500.1.
BC137515 mRNA. Translation: AAI37516.1. Sequence problems.
BC137518 mRNA. Translation: AAI37519.1. Sequence problems.
AK097056 mRNA. Translation: BAC04938.1. Sequence problems.

IPI

IPI00023807.
IPI00915390.

RefSeq

NP_001135759.1. NM_001142287.1.
NP_006369.3. NM_006378.3.

UniGene

Hs.494406.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OLZ	X-ray	2.00	A/B	22-677	[»]
3OL2	X-ray	2.99	A	22-677	[»]

ProteinModelPortal

Q92854.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59221N.

IntAct

Q92854. 1 interaction.

STRING

9606.ENSP00000343418.

PTM databases

PhosphoSite

Q92854.

Polymorphism databases

DMDM

8134701.

Proteomic databases

PaxDb

Q92854.

PeptideAtlas

Q92854.

PRIDE

Q92854.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000339861; ENSP00000344923; ENSG00000187764.
ENST00000343780; ENSP00000343418; ENSG00000187764.
ENST00000356444; ENSP00000348822; ENSG00000187764.
ENST00000420101; ENSP00000399948; ENSG00000187764.
ENST00000420987; ENSP00000391733; ENSG00000187764.
ENST00000422704; ENSP00000388768; ENSG00000187764.
ENST00000438547; ENSP00000405102; ENSG00000187764.
ENST00000450295; ENSP00000416523; ENSG00000187764.
ENST00000455551; ENSP00000411981; ENSG00000187764.

GeneID

10507.

KEGG

hsa:10507.

UCSC

uc004aqo.1. human.
uc011ltm.1. human.

Organism-specific databases

CTD

10507.

GeneCards

GC09M091975.

HGNC

HGNC:10732. SEMA4D.

HPA

HPA015662.
HPA023277.

MIM

601866. gene.

neXtProt

NX_Q92854.

PharmGKB

PA35654.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG326211.

HOGENOM

HOG000111669.

HOVERGEN

HBG061627.

InParanoid

Q8N8B0.

KO

K06521.

OMA

FCQATGP.

PhylomeDB

Q92854.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q92854.

Bgee

Q92854.

CleanEx

HS_SEMA4D.

Genevestigator

Q92854.

GermOnline

ENSG00000187764. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 1 hit.
2.60.40.10. 1 hit.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
IPR003659. Plexin-like.
IPR016201. Plexin-like_fold.
IPR002165. Plexin_repeat.
IPR027231. Semaphorin.
IPR001627. Semaphorin/CD100_Ag.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]

PANTHER

PTHR11036. PTHR11036. 1 hit.

Pfam

PF00047. ig. 1 hit.
PF01437. PSI. 1 hit.
PF01403. Sema. 1 hit.
[Graphical view]

SMART

SM00409. IG. 1 hit.
SM00423. PSI. 1 hit.
SM00630. Sema. 1 hit.
[Graphical view]

SUPFAM

SSF103575. Plexin-like_fold. 1 hit.
SSF101912. Sema. 1 hit.

PROSITE

PS50835. IG_LIKE. 1 hit.
PS51004. SEMA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q92854.

GenomeRNAi

10507.

NextBio

39858.

SOURCE

Search...

Entry information

Entry name

SEM4D_HUMAN

Accession

Primary (citable) accession number: Q92854
Secondary accession number(s): B2RPM6, Q7Z5S4, Q8N8B0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.