SEM6B_MOUSE
ID SEM6B_MOUSE Reviewed; 886 AA.
AC O54951;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Semaphorin-6B;
DE AltName: Full=Semaphorin VIB;
DE Short=Sema VIB;
DE AltName: Full=Semaphorin-N;
DE Short=Sema N;
DE Flags: Precursor;
GN Name=Sema6b; Synonyms=Seman;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBUNIT, AND INTERACTION WITH SRC.
RX PubMed=9361278; DOI=10.1006/mcne.1997.0644;
RA Eckhardt F., Behar O., Calautti E., Yonezawa K., Nishimoto I.,
RA Fishman M.C.;
RT "A novel transmembrane semaphorin can bind c-src.";
RL Mol. Cell. Neurosci. 9:409-419(1997).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20484647; DOI=10.1523/jneurosci.0073-10.2010;
RA Tawarayama H., Yoshida Y., Suto F., Mitchell K.J., Fujisawa H.;
RT "Roles of semaphorin-6B and plexin-A2 in lamina-restricted projection of
RT hippocampal mossy fibers.";
RL J. Neurosci. 30:7049-7060(2010).
RN [3]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-667, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=32169168; DOI=10.1016/j.ajhg.2020.02.011;
RA Hamanaka K., Imagawa E., Koshimizu E., Miyatake S., Tohyama J.,
RA Yamagata T., Miyauchi A., Ekhilevitch N., Nakamura F., Kawashima T.,
RA Goshima Y., Mohamed A.R., Ch'ng G.S., Fujita A., Azuma Y., Yasuda K.,
RA Imamura S., Nakashima M., Saitsu H., Mitsuhashi S., Mizuguchi T.,
RA Takata A., Miyake N., Matsumoto N.;
RT "De novo truncating variants in the last exon of SEMA6B Cause progressive
RT myoclonic epilepsy.";
RL Am. J. Hum. Genet. 106:549-558(2020).
CC -!- FUNCTION: Functions as a cell surface repellent for mossy fibers of
CC developping neurons in the hippocampus where it plays a role in axon
CC guidance (PubMed:20484647). May function through the PLXNA4 receptor
CC expressed by mossy cell axons (PubMed:20484647).
CC {ECO:0000269|PubMed:20484647}.
CC -!- SUBUNIT: Homodimer (PubMed:9361278). Binds specifically the SH3 domain
CC of the protooncogene C-SRC (PubMed:9361278).
CC {ECO:0000269|PubMed:9361278}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20484647};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In adulthood, it is expressed ubiquitously.
CC {ECO:0000269|PubMed:32169168, ECO:0000269|PubMed:9361278}.
CC -!- DEVELOPMENTAL STAGE: During development it is expressed in subregions
CC of the nervous system and is particularly prominent in muscle
CC (PubMed:9361278, PubMed:32169168). Expressed at embryonic day 18.5 dpc
CC (PubMed:32169168). {ECO:0000269|PubMed:32169168,
CC ECO:0000269|PubMed:9361278}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Sema6b are viable and fertile but
CC display abnormal projection of hippocampal mossy fibers.
CC {ECO:0000269|PubMed:20484647}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AF036585; AAC00493.1; -; mRNA.
DR CCDS; CCDS28896.1; -.
DR RefSeq; NP_001123928.1; NM_001130456.1.
DR RefSeq; NP_038690.1; NM_013662.2.
DR RefSeq; XP_006523993.1; XM_006523930.3.
DR AlphaFoldDB; O54951; -.
DR SMR; O54951; -.
DR BioGRID; 203174; 4.
DR STRING; 10090.ENSMUSP00000130985; -.
DR GlyGen; O54951; 6 sites.
DR iPTMnet; O54951; -.
DR PhosphoSitePlus; O54951; -.
DR PaxDb; O54951; -.
DR PRIDE; O54951; -.
DR ProteomicsDB; 256948; -.
DR Antibodypedia; 57701; 117 antibodies from 23 providers.
DR DNASU; 20359; -.
DR Ensembl; ENSMUST00000001256; ENSMUSP00000001256; ENSMUSG00000001227.
DR Ensembl; ENSMUST00000167545; ENSMUSP00000130985; ENSMUSG00000001227.
DR GeneID; 20359; -.
DR KEGG; mmu:20359; -.
DR UCSC; uc008dbd.2; mouse.
DR CTD; 10501; -.
DR MGI; MGI:1202889; Sema6b.
DR VEuPathDB; HostDB:ENSMUSG00000001227; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159170; -.
DR HOGENOM; CLU_009051_2_1_1; -.
DR InParanoid; O54951; -.
DR OMA; QKRVMRL; -.
DR OrthoDB; 119118at2759; -.
DR PhylomeDB; O54951; -.
DR TreeFam; TF316102; -.
DR BioGRID-ORCS; 20359; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Sema6b; mouse.
DR PRO; PR:O54951; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O54951; protein.
DR Bgee; ENSMUSG00000001227; Expressed in superior frontal gyrus and 123 other tissues.
DR ExpressionAtlas; O54951; baseline and differential.
DR Genevisible; O54951; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IMP:UniProtKB.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Membrane; Methylation; Neurogenesis; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..886
FT /note="Semaphorin-6B"
FT /id="PRO_0000032342"
FT TOPO_DOM 27..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..525
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 655..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 667
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 145..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 268..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 293..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 487..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 528..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 534..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 538..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 886 AA; 95467 MW; E5F56D125CDA574D CRC64;
MWTPRVPPPR PALSFFLLLL LGVTYGLFPE EPPPLSVAPR DYLSHYPVFV GSGPGRLTAA
EGAEDLNIQR VLRVNRTLFI GDRDNLYQVE LEPSTSTELR YQRKLTWRSN PSDIDVCRMK
GKQEGECRNF VKVLLLRDES TLFVCGSNAF NPICANYSMD TLQLLGDSIS GMARCPYDPK
HANVALFSDG MLFTATVTDF LAIDAVIYRS LGDRPTLRTV KHDSKWFKEP YFVHAVEWGS
HVYFFFREIA MEFNYLEKVV VSRVARVCKN DVGGSPRVLE KQWTSFLKAR LNCSVPGDSH
FYFNVLQAVT GVVSLGGRPV ILAVFSTPSN SIPGSAVCAF DMNQVAAVFE GRFREQKSPE
SIWTPVPEDQ VPRPRPGCCA APGMQYNASS ALPDEILNFV KTHPLMDEAV PSLGHSPWIV
RTLMRHQLTR VAVDVGAGPW GNQTIVFLGS EAGTVLKFLV KPNASVSGTT GPSIFLEEFE
TYRPDRCGRP SSAGEWGQRL LSLELDAASG GLLAAFPRCV VRVPVARCQL YSGCMKNCIG
SQDPYCGWAP DGSCIFLRPG TSATFEQDVS GASTSGLGDC TGLLRASLSD DRAGLVSVNL
LVTSSVAAFV VGAVVSGFSV GWFVGLRERR ELARRKDKEA ILAHGGSEAV LSVSRLGERR
GTGPGGRGGA GGGPGGPPEA LLAPLMQNGW TKAALLHGGP HDLDTGLLPT PEQTPLPQKR
LPTPHPHAHA LGSRAWDHSH ALLSASASTS LLLLAPARAS EQPQVPAEPG PESRLCAPRS
CRASHPGDFP LTPHASPDRR RVVSAPTGPL DPSVGDGLPG PWSPPATSSL RRPGPHGPPT
AALRRTHTFN SGEARPGGHR PRRHPPADST HLLPCGTGER TAPPVP
