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 13-FEB-2019, entry version 173. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 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- RT length human cDNAs encoding secretion or membrane proteins from oligo- RT capped cDNA 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 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 RT project: 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 RT DNA in the mnd2 region of mouse chromosome 6 reveals coding regions of RT three new genes."; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Has growth cone collapse activity against retinal CC ganglion-cell axons. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. 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 UniGene; Hs.25887; -. DR ProteinModelPortal; O95754; -. DR SMR; O95754; -. DR BioGrid; 115764; 21. DR IntAct; O95754; 1. DR STRING; 9606.ENSP00000350547; -. DR iPTMnet; O95754; -. DR PhosphoSitePlus; O95754; -. DR BioMuta; SEMA4F; -. DR EPD; O95754; -. DR jPOST; O95754; -. DR PaxDb; O95754; -. DR PeptideAtlas; O95754; -. DR PRIDE; O95754; -. DR ProteomicsDB; 51023; -. DR ProteomicsDB; 51024; -. [O95754-2] DR DNASU; 10505; -. DR Ensembl; ENST00000339773; ENSP00000342675; ENSG00000135622. [O95754-2] DR Ensembl; ENST00000357877; ENSP00000350547; ENSG00000135622. [O95754-1] DR GeneID; 10505; -. DR KEGG; hsa:10505; -. DR UCSC; uc002sna.3; human. [O95754-1] DR CTD; 10505; -. DR DisGeNET; 10505; -. DR EuPathDB; HostDB:ENSG00000135622.12; -. DR GeneCards; SEMA4F; -. DR HGNC; HGNC:10734; SEMA4F. DR HPA; HPA064095; -. DR HPA; HPA065969; -. DR MIM; 603706; gene. DR neXtProt; NX_O95754; -. DR OpenTargets; ENSG00000135622; -. DR PharmGKB; PA35656; -. DR eggNOG; KOG3611; Eukaryota. DR eggNOG; ENOG410XQZC; LUCA. DR GeneTree; ENSGT00940000159592; -. DR HOGENOM; HOG000116087; -. DR HOVERGEN; HBG093234; -. DR InParanoid; O95754; -. DR KO; K06521; -. DR OMA; QLSPRPC; -. DR OrthoDB; 64683at2759; -. DR PhylomeDB; O95754; -. DR TreeFam; TF352903; -. DR GeneWiki; SEMA4F; -. DR GenomeRNAi; 10505; -. DR PRO; PR:O95754; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000135622; Expressed in 159 organ(s), highest expression level in frontal cortex. DR ExpressionAtlas; O95754; baseline and differential. DR Genevisible; O95754; HS. 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:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central. DR GO; GO:0038191; F:neuropilin binding; IBA:GO_Central. DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; TAS:ProtInc. 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; 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 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; Complete proteome; Developmental protein; KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 34 {ECO:0000255}. FT CHAIN 35 770 Semaphorin-4F. FT /FTId=PRO_0000032330. FT TOPO_DOM 35 659 Extracellular. {ECO:0000255}. FT TRANSMEM 660 680 Helical. {ECO:0000255}. FT TOPO_DOM 681 770 Cytoplasmic. {ECO:0000255}. FT DOMAIN 42 510 Sema. {ECO:0000255|PROSITE- FT ProRule:PRU00352}. FT DOMAIN 512 563 PSI. FT DOMAIN 580 635 Ig-like C2-type. FT MOD_RES 718 718 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Z123}. FT MOD_RES 720 720 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Z123}. FT CARBOHYD 64 64 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 133 133 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 509 509 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 112 122 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 140 149 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 273 384 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 297 343 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 513 530 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 522 539 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT DISULFID 587 628 {ECO:0000255|PROSITE-ProRule:PRU00352}. FT VAR_SEQ 120 274 Missing (in isoform Short). FT {ECO:0000303|PubMed:10051670, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_006043. FT CONFLICT 533 533 S -> N (in Ref. 1; BAA75631). FT {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 //