SEM4F_RAT
ID SEM4F_RAT Reviewed; 776 AA.
AC Q9Z143;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Semaphorin-4F;
DE AltName: Full=Semaphorin-W;
DE Short=Sema W;
DE Flags: Precursor;
GN Name=Sema4f;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; 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 INTERACTION WITH DLG4, AND SUBCELLULAR LOCATION.
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 [3]
RP FUNCTION.
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 (By similarity). Might also
CC regulate differentiation of oligodendroglial precursor cells
CC (PubMed:21945643). Has growth cone collapse activity against retinal
CC ganglion-cell axons (PubMed:10051670). {ECO:0000250|UniProtKB:Q9Z123,
CC ECO:0000269|PubMed:10051670, 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:0000269|PubMed:10051670};
CC Single-pass type I membrane protein {ECO:0000305}. Postsynaptic density
CC {ECO:0000269|PubMed:11483650}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9Z123}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9Z123}. Note=Colocalizes with DLG4 at synapses.
CC {ECO:0000250|UniProtKB:Q9Z123}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in the developing embryo
CC (PubMed:10051670). Expressed at high levels in the lung and adult
CC central nervous system, including the dorsal root ganglia
CC (PubMed:10051670). {ECO:0000269|PubMed:10051670}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AB002563; BAA75629.1; -; mRNA.
DR RefSeq; NP_062145.1; NM_019272.1.
DR AlphaFoldDB; Q9Z143; -.
DR SMR; Q9Z143; -.
DR STRING; 10116.ENSRNOP00000009269; -.
DR GlyGen; Q9Z143; 3 sites.
DR iPTMnet; Q9Z143; -.
DR PhosphoSitePlus; Q9Z143; -.
DR PaxDb; Q9Z143; -.
DR Ensembl; ENSRNOT00000009269; ENSRNOP00000009269; ENSRNOG00000006784.
DR GeneID; 29745; -.
DR KEGG; rno:29745; -.
DR UCSC; RGD:3658; rat.
DR CTD; 10505; -.
DR RGD; 3658; Sema4f.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159592; -.
DR HOGENOM; CLU_009051_6_0_1; -.
DR InParanoid; Q9Z143; -.
DR OMA; FTSQWEP; -.
DR OrthoDB; 64683at2759; -.
DR PhylomeDB; Q9Z143; -.
DR TreeFam; TF352903; -.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR PRO; PR:Q9Z143; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000006784; Expressed in frontal cortex and 16 other tissues.
DR Genevisible; Q9Z143; RN.
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; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA: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; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA: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:0007411; P:axon guidance; IDA:RGD.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA: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; IDA: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..39
FT /evidence="ECO:0000255"
FT CHAIN 40..776
FT /note="Semaphorin-4F"
FT /id="PRO_0000032332"
FT TOPO_DOM 40..665
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..686
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 687..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..515
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 517..568
FT /note="PSI"
FT DOMAIN 585..640
FT /note="Ig-like C2-type"
FT REGION 702..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 774..776
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Z123"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z123"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z123"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
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 278..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 302..348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 518..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 527..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 592..633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 776 AA; 84298 MW; 20763182CC6C93CA CRC64;
MLARAERPRP GPRPPPVFPF PPPLSLLLLL AILSAPVCGR VPRSVPRTSL PISEADSYLT
RFAASHTYNY SALLVDPASH TLYVGARDSI FALTLPFSGE RPRRIDWMVP ETHRQNCRKK
GKKEDECHNF IQILAIVNAS HLLTCGTFAF DPKCGVIDVS SFQQVERLES GRGKCPFEPA
QRSAAVMAGG VLYTATVKNF LGTEPIISRA VGRAEDWIRT ETLSSWLNAP AFVAAMVLSP
AEWGDEDGDD EIFFFFTETS RVLDSYERIK VPRVARVCAG DLGGRKTLQQ RWTTFLKADL
LCPGPEHGRA SGVLQAMAEL RPQPGAGTPI FYGIFSSQWE GAAISAVCAF RPQDIRAVLN
GPFRELKHDC NRGLPVMDNE VPQPRPGECI ANNMKLQQFG SSLSLPDRVL TFIRDHPLMD
RPVFPADGRP LLVTTDTAYL RVVAHRVTSL SGKEYDVLYL GTEDGHLHRA VRIGAQLSVL
EDLALFPEPQ PVESMKLYHD WLLVGSHTEV TQVNTSNCGR LQSCSECILA QDPVCAWSFR
LDACVAHAGE HRGMVQDIES ADVSSLCPKE PGEHPVVFEV PVATVGHVVL PCSPSSAWAS
CVWHQPSGVT ALTPRRDGLE VVVTPGAMGA YACECQEGGA ARVVAAYSLV WGSQRGPSNR
AHTVVGAGLV GFLLGVLAAS LTLLLIGRRQ QRRRQRELLA RDKVGLDLGA PPSGTTSYSQ
DPPSPSPEDE RLPLALGKRG SGFGGFPPPF LLDSCPSPAH IRLTGAPLAT CDETSI
