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   24-JAN-2024, entry version 155.
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   GlyCosmos; Q9Z143; 3 sites, No reported glycans.
DR   GlyGen; Q9Z143; 3 sites.
DR   iPTMnet; Q9Z143; -.
DR   PhosphoSitePlus; Q9Z143; -.
DR   PaxDb; 10116-ENSRNOP00000009269; -.
DR   Ensembl; ENSRNOT00000009269.5; ENSRNOP00000009269.4; ENSRNOG00000006784.5.
DR   Ensembl; ENSRNOT00055021488; ENSRNOP00055017403; ENSRNOG00055012601.
DR   Ensembl; ENSRNOT00060003470; ENSRNOP00060002368; ENSRNOG00060002224.
DR   Ensembl; ENSRNOT00065028099; ENSRNOP00065022214; ENSRNOG00065016833.
DR   GeneID; 29745; -.
DR   KEGG; rno:29745; -.
DR   UCSC; RGD:3658; rat.
DR   AGR; RGD:3658; -.
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; PRKIVWD; -.
DR   OrthoDB; 5342713at2759; -.
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 cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
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   CDD; cd11261; Sema_4F; 1.
DR   Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR047085; Sem4F_Sema_dom.
DR   InterPro; IPR045791; Sema4F_C.
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; SEMAPHORIN; 1.
DR   PANTHER; PTHR11036:SF72; SEMAPHORIN-4F; 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; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   PROSITE; PS51004; SEMA; 1.
DR   Genevisible; Q9Z143; RN.
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
//