SEM4F_HUMAN
ID SEM4F_HUMAN Reviewed; 770 AA.
AC O95754; Q542Y7; Q9NS35;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Semaphorin-4F;
DE AltName: Full=Semaphorin-M;
DE Short=Sema M;
DE AltName: Full=Semaphorin-W;
DE Short=Sema W;
DE Flags: Precursor;
GN Name=SEMA4F; Synonyms=SEMAM, SEMAW;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC 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 MRNA] (ISOFORM LONG).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
RC 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 347-770.
RA Jang W., Spilson S.V., Hua A., Roe B., Meisler M.H.;
RT "Large-scale comparative sequence analysis of human and mouse genomic DNA
RT in the mnd2 region of mouse chromosome 6 reveals coding regions of three
RT new genes.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable cell surface receptor that regulates
CC oligodendroglial precursor cell migration (By similarity). 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:Q9Z123,
CC ECO:0000250|UniProtKB:Q9Z143}.
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:0000250|UniProtKB:Q9Z123}.
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:0000250|UniProtKB:Q9Z123}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9Z123}. Note=Colocalizes with DLG4 at synapses.
CC {ECO:0000250|UniProtKB:Q9Z123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O95754-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O95754-2; Sequence=VSP_006043;
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB022317; BAA75631.1; -; mRNA.
DR EMBL; AL136552; CAB66487.1; -; mRNA.
DR EMBL; AK075384; BAC11584.1; -; mRNA.
DR EMBL; AC006544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018361; AAH18361.1; -; mRNA.
DR EMBL; BC038411; AAH38411.1; -; mRNA.
DR EMBL; AF053369; AAF80660.1; -; mRNA.
DR CCDS; CCDS1955.1; -. [O95754-1]
DR CCDS; CCDS62942.1; -. [O95754-2]
DR RefSeq; NP_001258590.1; NM_001271661.1. [O95754-2]
DR RefSeq; NP_001258591.1; NM_001271662.1.
DR RefSeq; NP_004254.2; NM_004263.4. [O95754-1]
DR AlphaFoldDB; O95754; -.
DR SMR; O95754; -.
DR BioGRID; 115764; 48.
DR IntAct; O95754; 11.
DR STRING; 9606.ENSP00000350547; -.
DR GlyGen; O95754; 3 sites.
DR iPTMnet; O95754; -.
DR PhosphoSitePlus; O95754; -.
DR BioMuta; SEMA4F; -.
DR EPD; O95754; -.
DR MassIVE; O95754; -.
DR PaxDb; O95754; -.
DR PeptideAtlas; O95754; -.
DR PRIDE; O95754; -.
DR ProteomicsDB; 51023; -. [O95754-1]
DR ProteomicsDB; 51024; -. [O95754-2]
DR Antibodypedia; 47483; 159 antibodies from 24 providers.
DR DNASU; 10505; -.
DR Ensembl; ENST00000339773.9; ENSP00000342675.5; ENSG00000135622.13. [O95754-2]
DR Ensembl; ENST00000357877.7; ENSP00000350547.2; ENSG00000135622.13. [O95754-1]
DR GeneID; 10505; -.
DR KEGG; hsa:10505; -.
DR MANE-Select; ENST00000357877.7; ENSP00000350547.2; NM_004263.5; NP_004254.2.
DR UCSC; uc002sna.3; human. [O95754-1]
DR CTD; 10505; -.
DR DisGeNET; 10505; -.
DR GeneCards; SEMA4F; -.
DR HGNC; HGNC:10734; SEMA4F.
DR HPA; ENSG00000135622; Low tissue specificity.
DR MIM; 603706; gene.
DR neXtProt; NX_O95754; -.
DR OpenTargets; ENSG00000135622; -.
DR PharmGKB; PA35656; -.
DR VEuPathDB; HostDB:ENSG00000135622; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159592; -.
DR HOGENOM; CLU_009051_6_0_1; -.
DR InParanoid; O95754; -.
DR OMA; FTSQWEP; -.
DR OrthoDB; 64683at2759; -.
DR PhylomeDB; O95754; -.
DR TreeFam; TF352903; -.
DR PathwayCommons; O95754; -.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR SignaLink; O95754; -.
DR BioGRID-ORCS; 10505; 12 hits in 1072 CRISPR screens.
DR GeneWiki; SEMA4F; -.
DR GenomeRNAi; 10505; -.
DR Pharos; O95754; Tbio.
DR PRO; PR:O95754; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95754; protein.
DR Bgee; ENSG00000135622; Expressed in endothelial cell and 140 other tissues.
DR ExpressionAtlas; O95754; baseline and differential.
DR Genevisible; O95754; HS.
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; IDA:LIFEdb.
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:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
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:0007399; P:nervous system development; TAS:ProtInc.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..770
FT /note="Semaphorin-4F"
FT /id="PRO_0000032330"
FT TOPO_DOM 35..659
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..510
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 512..563
FT /note="PSI"
FT DOMAIN 580..635
FT /note="Ig-like C2-type"
FT REGION 696..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 768..770
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Z123"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z123"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z123"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 140..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 273..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 297..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 513..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 522..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 587..628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 120..274
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10051670,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006043"
FT CONFLICT 533
FT /note="S -> N (in Ref. 1; BAA75631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 83511 MW; CFBB74B41DF0E9C8 CRC64;
MPASAARPRP GPGQPTASPF PLLLLAVLSG PVSGRVPRSV PRTSLPISEA DSCLTRFAVP
HTYNYSVLLV DPASHTLYVG ARDTIFALSL PFSGERPRRI DWMVPEAHRQ NCRKKGKKED
ECHNFVQILA IANASHLLTC GTFAFDPKCG VIDVSRFQQV ERLESGRGKC PFEPAQRSAA
VMAGGVLYAA TVKNYLGTEP IITRAVGRAE DWIRTDTLPS WLNAPAFVAA VALSPAEWGD
EDGDDEIYFF FTETSRAFDS YERIKVPRVA RVCAGDLGGR KTLQQRWTTF LKADLLCPGP
EHGRASSVLQ DVAVLRPELG AGTPIFYGIF SSQWEGATIS AVCAFRPQDI RTVLNGPFRE
LKHDCNRGLP VVDNDVPQPR PGECITNNMK LRHFGSSLSL PDRVLTFIRD HPLMDRPVFP
ADGHPLLVTT DTAYLRVVAH RVTSLSGKEY DVLYLGTEDG HLHRAVRIGA QLSVLEDLAL
FPEPQPVENM KLYHSWLLVG SRTEVTQVNT TNCGRLQSCS ECILAQDPVC AWSFRLDECV
AHAGEHRGLV QDIESADVSS LCPKEPGERP VVFEVPVATA AHVVLPCSPS SAWASCVWHQ
PSGVTALTPR RDGLEVVVTP GAMGAYACEC QEGGAAHVVA AYSLVWGSQR DAPSRAHTVG
AGLAGFFLGI LAASLTLILI GRRQQRRRQR ELLARDKVGL DLGAPPSGTT SYSQDPPSPS
PEDERLPLAL AKRGSGFGGF SPPFLLDPCP SPAHIRLTGA PLATCDETSI
