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Semaphorin-6A (Semaphorin Q) (Sema Q) (Semaphorin VIA) (Sema VIA) (Semaphorin-6A-1) (SEMA6A-1)

 SEM6A_MOUSE             Reviewed;        1031 AA.
O35464; Q6P5A8; Q6PCN9; Q9EQ71;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 2.
23-MAY-2018, entry version 153.
RecName: Full=Semaphorin-6A;
AltName: Full=Semaphorin Q;
Short=Sema Q;
AltName: Full=Semaphorin VIA;
Short=Sema VIA;
AltName: Full=Semaphorin-6A-1;
Short=SEMA6A-1;
Flags: Precursor;
Name=Sema6a; Synonyms=Semaq;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH EVL.
TISSUE=Brain;
PubMed=10993894; DOI=10.1074/jbc.M006316200;
Klostermann A., Lutz B., Gertler F., Behl C.;
"The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-
like protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
J. Biol. Chem. 275:39647-39653(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-888 (ISOFORM 1).
PubMed=9204478; DOI=10.1006/mcne.1997.0607;
Zhou L., White F.A., Lentz S.I., Wright D.E., Fisher D.A.,
Snider W.D.;
"Cloning and expression of a novel murine semaphorin with structural
similarity to insect semaphorin I.";
Mol. Cell. Neurosci. 9:26-41(1997).
[4]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=16205717; DOI=10.1038/nn1555;
Kerjan G., Dolan J., Haumaitre C., Schneider-Maunoury S., Fujisawa H.,
Mitchell K.J., Chedotal A.;
"The transmembrane semaphorin Sema6A controls cerebellar granule cell
migration.";
Nat. Neurosci. 8:1516-1524(2005).
[5]
FUNCTION.
PubMed=19063725; DOI=10.1186/1749-8104-3-34;
Runker A.E., Little G.E., Suto F., Fujisawa H., Mitchell K.J.;
"Semaphorin-6A controls guidance of corticospinal tract axons at
multiple choice points.";
Neural Dev. 3:34-34(2008).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-571 IN COMPLEX WITH
PLXNA2, FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-65; ASN-282 AND
ASN-434, DISULFIDE BONDS, AND MUTAGENESIS OF LEU-191 AND ILE-322.
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).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-570 IN COMPLEX WITH
PLXNA2, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT
ASN-282 AND ASN-434, DISULFIDE BONDS, AND MUTAGENESIS OF HIS-212;
LYS-393 AND MET-415.
PubMed=20881961; DOI=10.1038/nature09473;
Nogi T., Yasui N., Mihara E., Matsunaga Y., Noda M., Yamashita N.,
Toyofuku T., Uchiyama S., Goshima Y., Kumanogoh A., Takagi J.;
"Structural basis for semaphorin signalling through the plexin
receptor.";
Nature 467:1123-1127(2010).
-!- FUNCTION: Cell surface receptor for PLXNA2 that plays an important
role in cell-cell signaling. Required for normal granule cell
migration in the developing cerebellum. Promotes reorganization of
the actin cytoskeleton and plays an important role in axon
guidance in the developing central nervous system. Can act as
repulsive axon guidance cue. Has repulsive action towards
migrating granular neurons. May play a role in channeling
sympathetic axons into the sympathetic chains and controlling the
temporal sequence of sympathetic target innervation.
{ECO:0000269|PubMed:16205717, ECO:0000269|PubMed:19063725,
ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}.
-!- SUBUNIT: Active as a homodimer or oligomer. The SEMA6A homodimer
interacts with a PLXNA2 homodimer, giving rise to a
heterotetramer. Interacts with EVL. {ECO:0000269|PubMed:10993894,
ECO:0000269|PubMed:20877282, ECO:0000269|PubMed:20881961}.
-!- INTERACTION:
P70207:Plxna2; NbExp=5; IntAct=EBI-15880936, EBI-771272;
Q80UG2:Plxna4; NbExp=3; IntAct=EBI-8057848, EBI-8057809;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20881961};
Single-pass type I membrane protein {ECO:0000269|PubMed:20881961}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O35464-1; Sequence=Displayed;
Name=2;
IsoId=O35464-2; Sequence=VSP_012097;
Name=3;
IsoId=O35464-3; Sequence=VSP_012098;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Particularly high levels in spinal cord,
cerebellum, metencephalon, superior and inferior colliculus,
diencephalon, olfactory bulb and eye.
{ECO:0000269|PubMed:16205717}.
-!- DEVELOPMENTAL STAGE: Temporally and spatially regulated during
development.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and
fertile, and do not show any major behavioral defects. In
developing cerebellum, migration of granule cells is impaired.
Granule cells can form normal cell processes, but the movement of
the nucleus seems to be impaired. {ECO:0000269|PubMed:16205717}.
-!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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EMBL; AF288666; AAG29494.1; -; mRNA.
EMBL; BC059238; AAH59238.1; -; mRNA.
EMBL; BC062979; AAH62979.1; -; mRNA.
EMBL; AF030430; AAB86408.1; -; mRNA.
CCDS; CCDS37813.1; -. [O35464-1]
CCDS; CCDS79642.1; -. [O35464-3]
RefSeq; NP_001298026.1; NM_001311097.1. [O35464-3]
RefSeq; NP_061214.2; NM_018744.2. [O35464-1]
UniGene; Mm.40909; -.
PDB; 3AFC; X-ray; 2.50 A; A/B=19-570.
PDB; 3AL8; X-ray; 3.60 A; A=19-570.
PDB; 3OKW; X-ray; 2.30 A; A/B=19-571.
PDB; 3OKY; X-ray; 2.20 A; B=19-571.
PDBsum; 3AFC; -.
PDBsum; 3AL8; -.
PDBsum; 3OKW; -.
PDBsum; 3OKY; -.
ProteinModelPortal; O35464; -.
SMR; O35464; -.
DIP; DIP-59220N; -.
ELM; O35464; -.
IntAct; O35464; 2.
MINT; O35464; -.
STRING; 10090.ENSMUSP00000019791; -.
iPTMnet; O35464; -.
PhosphoSitePlus; O35464; -.
MaxQB; O35464; -.
PaxDb; O35464; -.
PRIDE; O35464; -.
Ensembl; ENSMUST00000019791; ENSMUSP00000019791; ENSMUSG00000019647. [O35464-1]
Ensembl; ENSMUST00000076043; ENSMUSP00000075420; ENSMUSG00000019647. [O35464-3]
Ensembl; ENSMUST00000156422; ENSMUSP00000121442; ENSMUSG00000019647. [O35464-1]
GeneID; 20358; -.
KEGG; mmu:20358; -.
UCSC; uc008ewa.1; mouse. [O35464-1]
UCSC; uc008ewb.1; mouse. [O35464-3]
CTD; 57556; -.
MGI; MGI:1203727; Sema6a.
eggNOG; KOG3611; Eukaryota.
eggNOG; ENOG410XQZC; LUCA.
GeneTree; ENSGT00760000119134; -.
HOGENOM; HOG000232047; -.
HOVERGEN; HBG072910; -.
InParanoid; O35464; -.
KO; K06842; -.
PhylomeDB; O35464; -.
TreeFam; TF316102; -.
ChiTaRS; Sema6a; mouse.
EvolutionaryTrace; O35464; -.
PRO; PR:O35464; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000019647; -.
ExpressionAtlas; O35464; baseline and differential.
Genevisible; O35464; MM.
GO; GO:0030424; C:axon; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030215; F:semaphorin receptor binding; IGI:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0051642; P:centrosome localization; IMP:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
GO; GO:0106089; P:negative regulation of cell adhesion involved in sprouting angiogenesis; ISO:MGI.
GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR002165; Plexin_repeat.
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; PF01437; PSI; 1.
Pfam; PF01403; Sema; 1.
SMART; SM00630; Sema; 1.
SUPFAM; SSF101912; SSF101912; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 1031 Semaphorin-6A.
/FTId=PRO_0000032340.
TOPO_DOM 19 649 Extracellular. {ECO:0000255}.
TRANSMEM 650 670 Helical. {ECO:0000255}.
TOPO_DOM 671 1031 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 512 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
COMPBIAS 792 819 Pro-rich.
MOD_RES 698 698 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H2E6}.
MOD_RES 953 953 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H2E6}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20877282}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20877282,
ECO:0000269|PubMed:20881961}.
CARBOHYD 434 434 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20877282,
ECO:0000269|PubMed:20881961}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 107 117
DISULFID 135 144
DISULFID 258 369
DISULFID 283 328
DISULFID 477 506
DISULFID 515 533
DISULFID 521 568
DISULFID 525 542
VAR_SEQ 439 464 Missing (in isoform 2).
{ECO:0000303|PubMed:10993894}.
/FTId=VSP_012097.
VAR_SEQ 577 631 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012098.
MUTAGEN 191 191 L->R: Strongly reduced affinity for
PLXNA2. {ECO:0000269|PubMed:20877282}.
MUTAGEN 212 212 H->N: Strongly reduced affinity for
PLXNA2. {ECO:0000269|PubMed:20881961}.
MUTAGEN 322 322 I->E: Abolishes homodimerization.
{ECO:0000269|PubMed:20877282}.
MUTAGEN 393 393 K->E: Strongly reduced affinity for
PLXNA2. {ECO:0000269|PubMed:20881961}.
MUTAGEN 415 415 M->C: Formation of disulfide-linked
homodimer. {ECO:0000269|PubMed:20881961}.
CONFLICT 172 172 A -> V (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 201 201 L -> P (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 337 337 N -> D (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 585 585 S -> N (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 685 685 Q -> R (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 703 704 TK -> SE (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 735 735 P -> S (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 766 766 Q -> E (in Ref. 3; AAB86408).
{ECO:0000305}.
CONFLICT 856 856 I -> T (in Ref. 1; AAG29494).
{ECO:0000305}.
CONFLICT 863 888 KSPNHGVNLVENLDSLPPKVPQREAS -> ESSPYVLKQFS
EAFNRQGIILSVAVE (in Ref. 3; AAB86408).
{ECO:0000305}.
STRAND 27 30 {ECO:0000244|PDB:3OKY}.
HELIX 32 35 {ECO:0000244|PDB:3OKY}.
STRAND 60 64 {ECO:0000244|PDB:3OKY}.
STRAND 67 71 {ECO:0000244|PDB:3OKY}.
STRAND 73 80 {ECO:0000244|PDB:3OKY}.
HELIX 81 83 {ECO:0000244|PDB:3OKY}.
STRAND 86 89 {ECO:0000244|PDB:3OKY}.
STRAND 93 96 {ECO:0000244|PDB:3OKY}.
HELIX 101 109 {ECO:0000244|PDB:3OKY}.
TURN 114 116 {ECO:0000244|PDB:3OKY}.
STRAND 120 128 {ECO:0000244|PDB:3OKY}.
STRAND 131 136 {ECO:0000244|PDB:3OKY}.
TURN 138 140 {ECO:0000244|PDB:3OKY}.
STRAND 143 148 {ECO:0000244|PDB:3OKY}.
TURN 149 151 {ECO:0000244|PDB:3OKY}.
STRAND 154 160 {ECO:0000244|PDB:3OKW}.
TURN 162 164 {ECO:0000244|PDB:3OKY}.
STRAND 174 178 {ECO:0000244|PDB:3OKY}.
STRAND 181 189 {ECO:0000244|PDB:3OKY}.
STRAND 195 200 {ECO:0000244|PDB:3OKY}.
TURN 214 216 {ECO:0000244|PDB:3OKY}.
STRAND 221 228 {ECO:0000244|PDB:3OKY}.
STRAND 231 239 {ECO:0000244|PDB:3OKY}.
HELIX 241 243 {ECO:0000244|PDB:3OKY}.
STRAND 244 247 {ECO:0000244|PDB:3OKY}.
STRAND 250 258 {ECO:0000244|PDB:3OKY}.
STRAND 266 269 {ECO:0000244|PDB:3OKY}.
STRAND 277 281 {ECO:0000244|PDB:3OKY}.
STRAND 287 289 {ECO:0000244|PDB:3OKY}.
STRAND 295 299 {ECO:0000244|PDB:3OKY}.
STRAND 303 305 {ECO:0000244|PDB:3OKY}.
STRAND 308 316 {ECO:0000244|PDB:3OKY}.
STRAND 319 322 {ECO:0000244|PDB:3OKY}.
STRAND 325 331 {ECO:0000244|PDB:3OKY}.
HELIX 332 338 {ECO:0000244|PDB:3OKY}.
STRAND 343 348 {ECO:0000244|PDB:3OKY}.
STRAND 353 355 {ECO:0000244|PDB:3OKY}.
HELIX 358 360 {ECO:0000244|PDB:3OKY}.
TURN 374 377 {ECO:0000244|PDB:3OKY}.
HELIX 381 383 {ECO:0000244|PDB:3OKY}.
HELIX 386 394 {ECO:0000244|PDB:3OKY}.
STRAND 397 400 {ECO:0000244|PDB:3OKY}.
HELIX 405 407 {ECO:0000244|PDB:3OKY}.
STRAND 410 413 {ECO:0000244|PDB:3OKY}.
STRAND 415 418 {ECO:0000244|PDB:3OKY}.
STRAND 420 429 {ECO:0000244|PDB:3OKY}.
TURN 430 433 {ECO:0000244|PDB:3OKY}.
STRAND 435 442 {ECO:0000244|PDB:3OKY}.
STRAND 445 452 {ECO:0000244|PDB:3OKY}.
HELIX 455 457 {ECO:0000244|PDB:3AFC}.
STRAND 464 470 {ECO:0000244|PDB:3OKY}.
HELIX 474 477 {ECO:0000244|PDB:3OKY}.
STRAND 489 493 {ECO:0000244|PDB:3OKY}.
HELIX 494 496 {ECO:0000244|PDB:3OKY}.
STRAND 498 502 {ECO:0000244|PDB:3OKY}.
STRAND 507 512 {ECO:0000244|PDB:3OKY}.
HELIX 516 518 {ECO:0000244|PDB:3OKY}.
HELIX 522 527 {ECO:0000244|PDB:3OKY}.
STRAND 533 536 {ECO:0000244|PDB:3OKY}.
TURN 537 540 {ECO:0000244|PDB:3OKY}.
STRAND 541 544 {ECO:0000244|PDB:3OKY}.
STRAND 557 559 {ECO:0000244|PDB:3OKW}.
SEQUENCE 1031 AA; 114433 MW; 38565A81A4DA3BDB CRC64;
MRPAALLLCL TLLHCAGAGF PEDSEPISIS HGNYTKQYPV FVGHKPGRNT TQRHRLDIQM
IMIMNRTLYV AARDHIYTVD IDTSHTEEIY CSKKLTWKSR QADVDTCRMK GKHKDECHNF
IKVLLKKNDD TLFVCGTNAF NPSCRNYRVD TLETFGDEFS GMARCPYDAK HANIALFADG
KLYSATVTDF LAIDAVIYRS LGDSPTLRTV KHDSKWLKEP YFVQAVDYGD YIYFFFREIA
VEYNTMGKVV FPRVAQVCKN DMGGSQRVLE KQWTSFLKAR LNCSVPGDSH FYFNILQAVT
DVIRINGRDV VLATFSTPYN SIPGSAVCAY DMLDIANVFT GRFKEQKSPD STWTPVPDER
VPKPRPGCCA GSSSLEKYAT SNEFPDDTLN FIKTHPLMDE AVPSIINRPW FLRTMVRYRL
TKIAVDNAAG PYQNHTVVFL GSEKGIILKF LARIGSSGFL NGSLFLEEMN VYNPEKCSYD
GVEDKRIMGM QLDRASGSLY VAFSTCVIKV PLGRCERHGK CKKTCIASRD PYCGWVRESG
SCAHLSPLSR LTFEQDIERG NTDGLGDCHN SFVALNGHAS SLYPSTTTSD SASRDGYESR
GGMLDWNDLL EAPGSTDPLG AVSSHNHQDK KGVIRESYLK SNDQLVPVTL LAIAVILAFV
MGAVFSGIIV YCVCDHRRKD VAVVQRKEKE LTHSRRGSMS SVTKLSGLFG DTQSKDPKPE
AILTPLMHNG KLATPSNTAK MLIKADQHHL DLTALPTPES TPTLQQKRKP NRGSREWERN
QNIINACTKD MPPMGSPVIP TDLPLRASPS HIPSVVVLPI TQQGYQHEYV DQPKMSEVVA
QMALEDQAAT LEYKTIKEHL SSKSPNHGVN LVENLDSLPP KVPQREASLG PPGTSLSQTG
LSKRLEMQHS SSYGLEYKRS YPTNSLTRSH QTTTLKRNNT NSSNSSHLSR NQSFGRGDNP
PPAPQRVDSI QVHSSQPSGQ AVTVSRQPSL NAYNSLTRSG LKRTPSLKPD VPPKPSFAPL
STSMKPNDAC T


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E2275m Mouse,M-Sema G,Mus musculus,Sema J,Sema4d,Semacl2,Semaj,Semaphorin-4D,Semaphorin-C-like 2,Semaphorin-J
E2276m Mouse,Mus musculus,Sema N,Sema VIB,Sema6b,Seman,Semaphorin VIB,Semaphorin-6B,Semaphorin-N
20-783-71106 MOUSE ANTI HUMAN CDw108 FITC - Semaphorin-L; Sema L; Semaphorin-K1; Sema K1; CD108 antigen Monoclonal 0.1 mg


 

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