SEM4F_MOUSE
ID SEM4F_MOUSE Reviewed; 777 AA.
AC Q9Z123; Q505G0; Q9R1Y1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Semaphorin-4F;
DE AltName: Full=Semaphorin-W;
DE Short=Sema W;
DE Flags: Precursor;
GN Name=Sema4f; Synonyms=Semaw;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and BALB/cJ; TISSUE=Brain;
RX PubMed=10051670; DOI=10.1073/pnas.96.5.2491;
RA Encinas J.A., Kikuchi K., Chedotal A., de Castro F., Goodman C.S.,
RA Kimura T.;
RT "Cloning, expression, and genetic mapping of Sema W, a member of the
RT semaphorin family.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2491-2496(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH DLG4, MOTIF, AND MUTAGENESIS OF 775-THR--ILE-777.
RX PubMed=11483650; DOI=10.1046/j.1471-4159.2001.00447.x;
RA Schultze W., Eulenburg V., Lessmann V., Herrmann L., Dittmar T.,
RA Gundelfinger E.D., Heumann R., Erdmann K.S.;
RT "Semaphorin4F interacts with the synapse-associated protein SAP90/PSD-95.";
RL J. Neurochem. 78:482-489(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-725 AND SER-727, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=21945643; DOI=10.1016/j.mcn.2011.09.003;
RA Armendariz B.G., Bribian A., Perez-Martinez E., Martinez A., de Castro F.,
RA Soriano E., Burgaya F.;
RT "Expression of Semaphorin 4F in neurons and brain oligodendrocytes and the
RT regulation of oligodendrocyte precursor migration in the optic nerve.";
RL Mol. Cell. Neurosci. 49:54-67(2012).
CC -!- FUNCTION: Probable cell surface receptor that regulates
CC oligodendroglial precursor cell migration (PubMed:21945643). Might also
CC regulate differentiation of oligodendroglial precursor cells (By
CC similarity). Has growth cone collapse activity against retinal
CC ganglion-cell axons (By similarity). {ECO:0000250|UniProtKB:Q9Z143,
CC ECO:0000269|PubMed:21945643}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with DLG4/SAP90 (via PDZ
CC domain 2); this interaction may promote translocation of DLG4/SAP90 to
CC the membrane. {ECO:0000269|PubMed:11483650}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9Z143}. Perikaryon
CC {ECO:0000269|PubMed:21945643}. Cell projection, dendrite
CC {ECO:0000269|PubMed:21945643}. Note=Colocalizes with DLG4 at synapses.
CC {ECO:0000269|PubMed:21945643}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the adult brain, where it
CC shows particularly strong expression in the hippocampus, corpus
CC callosum, granular layer and deep nuclei of the cerebellum, and the
CC mitral layer of the olfactory bulb (at protein level)
CC (PubMed:21945643). At the cellular level, detected in neuronal
CC precursors, postmitotic neurons, pyramidal neurons, and glial cells
CC including mature oligodendocytes and oligodendroglial precursor cells
CC (at protein level) (PubMed:21945643). {ECO:0000269|PubMed:21945643}.
CC -!- DEVELOPMENTAL STAGE: During 14 dpc expression is abundant in the
CC cerebral cortex, hippocampus, brain stem and the mitral and glomerular
CC layers of the olfactory bulb, expression in the olfactory bulb remains
CC evident into adulthood (at protein level) (PubMed:21945643). Expressed
CC in proliferative layers and oligodendroglial precursor cells (OPCs)
CC during embryonic development (14-16 dpc), in regions such as the
CC ganglionic eminence, mamillothalamic tract, neuroepithelium, and
CC cortical plate (at protein level) (PubMed:21945643). Expressed in
CC migrating OPCs along the optic nerve at 16.5 dpc (at protein level)
CC (PubMed:21945643). During late embryonic development (18 dpc)
CC expression is abundant in pyramidal and granular cells of the
CC hippocampus, and OPCs in the migratory pathway and embryonic fimbria of
CC the hippocampus (at protein level) (PubMed:21945643). At postnatal day
CC 1 (P1) expression is abundant in the corpus callosum, anterior
CC commissure, and several nerve nuclei in the hindbrain, such as the
CC oculomotor nucleus, the periaqueductal gray area, the facial nucleus,
CC the colliculli, and the raphe and pararubral nuclei, as well as in the
CC proliferative layers of the anterior subventricular zone, with
CC expression remaining evident into adulthood (at protein level)
CC (PubMed:21945643). A significant abundance of protein is apparent in
CC the arcuate and posterior hypothalamic nuclei at P10, and additionally
CC in hypothalamic OPCs, expression becomes evident in the arcuate nucleus
CC at P15 (at protein level) (PubMed:21945643). Abundant expression
CC throughout the embryonic brain from 14 dpc onwards with decreased
CC expression in all areas of the brain in adulthood, however expression
CC remains relatively abundant (PubMed:21945643).
CC {ECO:0000269|PubMed:21945643}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AB021291; BAA75630.1; -; mRNA.
DR EMBL; AB022316; BAA75634.1; -; Genomic_DNA.
DR EMBL; CH466523; EDK99043.1; -; Genomic_DNA.
DR EMBL; BC094567; AAH94567.1; -; mRNA.
DR CCDS; CCDS20264.1; -.
DR RefSeq; NP_035480.3; NM_011350.4.
DR AlphaFoldDB; Q9Z123; -.
DR SMR; Q9Z123; -.
DR BioGRID; 203170; 5.
DR STRING; 10090.ENSMUSP00000000641; -.
DR GlyConnect; 2699; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9Z123; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q9Z123; -.
DR PhosphoSitePlus; Q9Z123; -.
DR EPD; Q9Z123; -.
DR MaxQB; Q9Z123; -.
DR PaxDb; Q9Z123; -.
DR PRIDE; Q9Z123; -.
DR ProteomicsDB; 256943; -.
DR Antibodypedia; 47483; 159 antibodies from 24 providers.
DR DNASU; 20355; -.
DR Ensembl; ENSMUST00000000641; ENSMUSP00000000641; ENSMUSG00000000627.
DR GeneID; 20355; -.
DR KEGG; mmu:20355; -.
DR UCSC; uc009clo.2; mouse.
DR CTD; 10505; -.
DR MGI; MGI:1340055; Sema4f.
DR VEuPathDB; HostDB:ENSMUSG00000000627; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159592; -.
DR HOGENOM; CLU_009051_6_0_1; -.
DR InParanoid; Q9Z123; -.
DR OMA; FTSQWEP; -.
DR OrthoDB; 64683at2759; -.
DR PhylomeDB; Q9Z123; -.
DR TreeFam; TF352903; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR BioGRID-ORCS; 20355; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q9Z123; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z123; protein.
DR Bgee; ENSMUSG00000000627; Expressed in trigeminal ganglion and 190 other tissues.
DR ExpressionAtlas; Q9Z123; baseline and differential.
DR Genevisible; Q9Z123; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; ISO:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:MGI.
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:0031290; P:retinal ganglion cell axon guidance; ISO:MGI.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR045791; Sema4F_C.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015512; Semaphorin_4F.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR PANTHER; PTHR11036:SF72; PTHR11036:SF72; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF19428; Sema4F_C; 1.
DR SMART; SM00423; PSI; 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; Cell projection; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Neurogenesis; Phosphoprotein; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..777
FT /note="Semaphorin-4F"
FT /id="PRO_0000032331"
FT TOPO_DOM 41..667
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..516
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 518..569
FT /note="PSI"
FT DOMAIN 586..641
FT /note="Ig-like C2-type"
FT REGION 703..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 775..777
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:11483650"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 146..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 279..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 303..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 519..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 528..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 593..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VARIANT 490
FT /note="T -> P (in strain: BALB/c)"
FT VARIANT 659
FT /note="A -> S (in strain: BALB/c)"
FT MUTAGEN 775..777
FT /note="Missing: Loss of interaction with DLG4."
FT /evidence="ECO:0000269|PubMed:11483650"
SQ SEQUENCE 777 AA; 84490 MW; 3338F4F0AEFBF0DA CRC64;
MLARAERPRP GPRPPPVSLF PPPSSLLLLL LAMLSAPVCG RVPRSVPRTS LPISEADSYL
TRFAAPHTYN YSALLVDPAS HTLYVGARDS IFALTLPFSG EKPRRIDWMV PETHRQNCRK
KGKKEDECHN FIQILAIANA SHLLTCGTFA FDPKCGVIDV SSFQQVERLE SGRGKCPFEP
AQRSAAVMAG GVLYTATVKN FLGTEPIISR AVGRAEDWIR TETLSSWLNA PAFVAAMVLS
PAEWGDEDGD DEIFFFFTET SRVLDSYERI KVPRVARVCA GDLGGRKTLQ QRWTTFLKAD
LLCPGPEHGR ASGVLQDMTE LRPQPGAGTP LFYGIFSSQW EGAAISAVCA FRPQDIRAVL
NGPFRELKHD CNRGLPVMDN EVPQPRPGEC ITNNMKFQQF GSSLSLPDRV LTFIRDHPLM
DRPVFPADGR PLLVTTDTAY LRVVAHRVTS LSGKEYDVLY LGTEDGHLHR AVRIGAQLSV
LEDLALFPET QPVESMKLYH DWLLVGSHTE VTQVNTSNCG RLQSCSECIL AQDPVCAWSF
RLDACVAHAG EHRGMVQDIE SADVSSLCPK EPGEHPVVFE VPVATVGHVV LPCSPSSAWA
SCVWHQPSGV TSLTPRRDGL EVVVTPGAMG AYACECQEGG AARVVAAYSL VWGSQRGPAN
RAHTVVGAGL VGFFLGVLAA SLTLLLIGRR QQRRRQRELL ARDKVGLDLG APPSGTTSYS
QDPPSPSPED ERLPLALGKR GSGFGGFPPP FLLDSCPSPA HIRLTGAPLA TCDETSI
