SEM4E_DANRE
ID SEM4E_DANRE Reviewed; 766 AA.
AC Q9YHX4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Semaphorin-4E;
DE AltName: Full=Semaphorin-7;
DE AltName: Full=Semaphorin-Z7;
DE Short=Sema Z7;
DE Flags: Precursor;
GN Name=sema4e; Synonyms=sema7, semaz7;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9867349; DOI=10.1016/s0925-4773(98)00124-5;
RA Halloran M.C., Severance S.M., Yee C.S., Gemza D.L., Kuwada J.Y.;
RT "Molecular cloning and expression of two novel zebrafish semaphorins.";
RL Mech. Dev. 76:165-168(1998).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AF073289; AAC72345.1; -; mRNA.
DR RefSeq; NP_571124.1; NM_131049.1.
DR AlphaFoldDB; Q9YHX4; -.
DR SMR; Q9YHX4; -.
DR STRING; 7955.ENSDARP00000056251; -.
DR PaxDb; Q9YHX4; -.
DR PRIDE; Q9YHX4; -.
DR GeneID; 796377; -.
DR KEGG; dre:796377; -.
DR CTD; 796377; -.
DR ZFIN; ZDB-GENE-990715-7; sema4e.
DR eggNOG; KOG3611; Eukaryota.
DR InParanoid; Q9YHX4; -.
DR PhylomeDB; Q9YHX4; -.
DR PRO; PR:Q9YHX4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0043931; P:ossification involved in bone maturation; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
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; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
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; PTHR11036; 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 SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..766
FT /note="Semaphorin-4E"
FT /id="PRO_0000032329"
FT TOPO_DOM 25..664
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..685
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..499
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 501..552
FT /note="PSI"
FT DOMAIN 555..640
FT /note="Ig-like C2-type"
FT REGION 724..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..111
FT /evidence="ECO:0000250"
FT DISULFID 129..138
FT /evidence="ECO:0000250"
FT DISULFID 261..373
FT /evidence="ECO:0000250"
FT DISULFID 285..329
FT /evidence="ECO:0000250"
FT DISULFID 502..519
FT /evidence="ECO:0000250"
FT DISULFID 511..528
FT /evidence="ECO:0000250"
FT DISULFID 577..623
FT /evidence="ECO:0000250"
SQ SEQUENCE 766 AA; 85617 MW; 0ACBC693FE7D830C CRC64;
MMSLLAVLCV LYVWSPAMLT GGLGSTLDSL PRKTVPIGSN GGRLFREEGI WNYTTMLLRD
DLNLLILGAR EAIFALDLDD ITIKKAMLKW EVTRDQQNDC SNKGKDATND CKNYIRILHK
KNDGRMYVCG TKAFNPTCGY LSYADGKLTL EILQEDTKGK CPFDPFQRYT SAMVDGAYYS
ATSMNFRGSE PVMMRSTEES IRTEFTSTWL SEPNFIHMAH IPEGQSNPDG DDDKIYLFFS
ETAVEYESYT KVDVSRVARV CKGDLGGQRT LQKKWTSFLK ARLDCQVPNT NLPLLVQDVF
HLCPDDWTTC VFYAVFTPQS DSSQYSAVCS YKIEDIKTVF SKGKFKAPFN VETSFVKWVM
YSGELPDPRP GACIDNHARE KGITKSLELP DKTLQFVKDK PLMDQAVTAE QPLLVKRGAA
FTRIVVTTAT ALNGTSHQVM FIGTKSGSVL KAVNYNGEMV IMEEIQLFDP SEPIKILRLS
SSKKQLYVGS EVGVVQLSIS ECGRYQTCLD CVLARDPHCG WDLDTEHCAT INSIHRTRSS
TVIQSLNDGD ASQCPAIGVS KPVNISFYHG NTVKLGCQPY SNLAQVKWQF NGEPIKPSNT
IQILSDGLMI FNASLDATGY YTCSSIETVS QRKYQTQHVA YDVKMWSESG TTASLHHVKE
KERTLVAMVV ILSLVLAALL IWNLYKGHLS LPCLHRRVKA TQNRHEDDAN QVQPQRLASS
VVNFNSNNNH ANDQRYSSSR ETDRLSTTAG STGQMSLKYI DDESEI
