SEM3E_HUMAN
ID SEM3E_HUMAN Reviewed; 775 AA.
AC O15041; B4E1P1; Q75M94; Q75M97;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Semaphorin-3E;
DE Flags: Precursor;
GN Name=SEMA3E; Synonyms=KIAA0331, SEMAH;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP VARIANTS PRO-208; CYS-619; LEU-703 AND VAL-717.
RX PubMed=15235037; DOI=10.1136/jmg.2003.017640;
RA Lalani S.R., Safiullah A.M., Molinari L.M., Fernbach S.D., Martin D.M.,
RA Belmont J.W.;
RT "SEMA3E mutation in a patient with CHARGE syndrome.";
RL J. Med. Genet. 41:E94-E94(2004).
CC -!- FUNCTION: Plays an important role in signaling via the cell surface
CC receptor PLXND1. Mediates reorganization of the actin cytoskeleton,
CC leading to the retraction of cell projections. Promotes focal adhesion
CC disassembly and inhibits adhesion of endothelial cells to the
CC extracellular matrix. Regulates angiogenesis, both during embryogenesis
CC and after birth. Can down-regulate sprouting angiogenesis. Required for
CC normal vascular patterning during embryogenesis. Plays an important
CC role in ensuring the specificity of synapse formation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PLXND1. {ECO:0000250}.
CC -!- INTERACTION:
CC O15041; Q9Y4D7: PLXND1; NbExp=2; IntAct=EBI-7283693, EBI-310731;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15041-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15041-2; Sequence=VSP_046237;
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20789.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002329; BAA20789.2; ALT_INIT; mRNA.
DR EMBL; AK303925; BAG64853.1; -; mRNA.
DR EMBL; AC004954; AAC69513.1; -; Genomic_DNA.
DR EMBL; AC006204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079799; AAS07488.1; -; Genomic_DNA.
DR EMBL; AC079987; AAS07487.1; -; Genomic_DNA.
DR CCDS; CCDS34674.1; -. [O15041-1]
DR CCDS; CCDS55121.1; -. [O15041-2]
DR RefSeq; NP_001171600.1; NM_001178129.1. [O15041-2]
DR RefSeq; NP_036563.1; NM_012431.2. [O15041-1]
DR AlphaFoldDB; O15041; -.
DR SMR; O15041; -.
DR BioGRID; 115072; 3.
DR IntAct; O15041; 1.
DR MINT; O15041; -.
DR STRING; 9606.ENSP00000303212; -.
DR GlyGen; O15041; 5 sites.
DR iPTMnet; O15041; -.
DR PhosphoSitePlus; O15041; -.
DR BioMuta; SEMA3E; -.
DR jPOST; O15041; -.
DR MassIVE; O15041; -.
DR PaxDb; O15041; -.
DR PeptideAtlas; O15041; -.
DR PRIDE; O15041; -.
DR ProteomicsDB; 48396; -. [O15041-1]
DR ProteomicsDB; 5776; -.
DR Antibodypedia; 29599; 289 antibodies from 31 providers.
DR DNASU; 9723; -.
DR Ensembl; ENST00000427262.6; ENSP00000405052.1; ENSG00000170381.14. [O15041-2]
DR Ensembl; ENST00000643230.2; ENSP00000496491.1; ENSG00000170381.14. [O15041-1]
DR GeneID; 9723; -.
DR KEGG; hsa:9723; -.
DR MANE-Select; ENST00000643230.2; ENSP00000496491.1; NM_012431.3; NP_036563.1.
DR UCSC; uc003uhy.3; human. [O15041-1]
DR CTD; 9723; -.
DR DisGeNET; 9723; -.
DR GeneCards; SEMA3E; -.
DR GeneReviews; SEMA3E; -.
DR HGNC; HGNC:10727; SEMA3E.
DR HPA; ENSG00000170381; Low tissue specificity.
DR MalaCards; SEMA3E; -.
DR MIM; 608166; gene.
DR neXtProt; NX_O15041; -.
DR OpenTargets; ENSG00000170381; -.
DR Orphanet; 138; CHARGE syndrome.
DR PharmGKB; PA35649; -.
DR VEuPathDB; HostDB:ENSG00000170381; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000158437; -.
DR HOGENOM; CLU_009051_5_0_1; -.
DR InParanoid; O15041; -.
DR OMA; GPHKMPC; -.
DR OrthoDB; 158418at2759; -.
DR PhylomeDB; O15041; -.
DR TreeFam; TF352628; -.
DR PathwayCommons; O15041; -.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR SignaLink; O15041; -.
DR BioGRID-ORCS; 9723; 14 hits in 1057 CRISPR screens.
DR ChiTaRS; SEMA3E; human.
DR GenomeRNAi; 9723; -.
DR Pharos; O15041; Tbio.
DR PRO; PR:O15041; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O15041; protein.
DR Bgee; ENSG00000170381; Expressed in cortical plate and 141 other tissues.
DR ExpressionAtlas; O15041; baseline and differential.
DR Genevisible; O15041; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0048018; F:receptor ligand activity; IDA:ARUK-UCL.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:ARUK-UCL.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:UniProtKB.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IDA:ARUK-UCL.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:ARUK-UCL.
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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:ARUK-UCL.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015513; Semaphorin_3E.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR PANTHER; PTHR11036:SF22; PTHR11036:SF22; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Neurogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..775
FT /note="Semaphorin-3E"
FT /id="PRO_0000032317"
FT DOMAIN 32..516
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 581..669
FT /note="Ig-like C2-type"
FT REGION 742..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..115
FT /evidence="ECO:0000250"
FT DISULFID 133..142
FT /evidence="ECO:0000250"
FT DISULFID 270..382
FT /evidence="ECO:0000250"
FT DISULFID 294..342
FT /evidence="ECO:0000250"
FT DISULFID 519..537
FT /evidence="ECO:0000250"
FT DISULFID 654..729
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046237"
FT VARIANT 208
FT /note="R -> P (in dbSNP:rs61729612)"
FT /evidence="ECO:0000269|PubMed:15235037"
FT /id="VAR_080476"
FT VARIANT 619
FT /note="R -> C (in dbSNP:rs143631464)"
FT /evidence="ECO:0000269|PubMed:15235037"
FT /id="VAR_080477"
FT VARIANT 703
FT /note="S -> L (found in a patient with CHARGE syndrome;
FT unknown pathological significance; dbSNP:rs121918341)"
FT /evidence="ECO:0000269|PubMed:15235037"
FT /id="VAR_080478"
FT VARIANT 717
FT /note="I -> V (in dbSNP:rs61729610)"
FT /evidence="ECO:0000269|PubMed:15235037"
FT /id="VAR_080479"
SQ SEQUENCE 775 AA; 89228 MW; CD6079C1AE48F779 CRC64;
MASAGHIITL LLWGYLLELW TGGHTADTTH PRLRLSHKEL LNLNRTSIFH SPFGFLDLHT
MLLDEYQERL FVGGRDLVYS LSLERISDGY KEIHWPSTAL KMEECIMKGK DAGECANYVR
VLHHYNRTHL LTCGTGAFDP VCAFIRVGYH LEDPLFHLES PRSERGRGRC PFDPSSSFIS
TLIGSELFAG LYSDYWSRDA AIFRSMGRLA HIRTEHDDER LLKEPKFVGS YMIPDNEDRD
DNKVYFFFTE KALEAENNAH AIYTRVGRLC VNDVGGQRIL VNKWSTFLKA RLVCSVPGMN
GIDTYFDELE DVFLLPTRDH KNPVIFGLFN TTSNIFRGHA ICVYHMSSIR AAFNGPYAHK
EGPEYHWSVY EGKVPYPRPG SCASKVNGGR YGTTKDYPDD AIRFARSHPL MYQAIKPAHK
KPILVKTDGK YNLKQIAVDR VEAEDGQYDV LFIGTDNGIV LKVITIYNQE MESMEEVILE
ELQIFKDPVP IISMEISSKR QQLYIGSASA VAQVRFHHCD MYGSACADCC LARDPYCAWD
GISCSRYYPT GTHAKRRFRR QDVRHGNAAQ QCFGQQFVGD ALDKTEEHLA YGIENNSTLL
ECTPRSLQAK VIWFVQKGRE TRKEEVKTDD RVVKMDLGLL FLRLHKSDAG TYFCQTVEHS
FVHTVRKITL EVVEEEKVED MFNKDDEEDR HHRMPCPAQS SISQGAKPWY KEFLQLIGYS
NFQRVEEYCE KVWCTDRKRK KLKMSPSKWK YANPQEKKLR SKPEHYRLPR HTLDS
