SEMA_ECTVM
ID SEMA_ECTVM Reviewed; 399 AA.
AC Q8JL80;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 02-JUN-2021, entry version 73.
DE RecName: Full=Semaphorin-like protein 139;
DE Flags: Precursor;
GN Name=EVM139; Synonyms=SEMA;
OS Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=265874;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7747448; DOI=10.1006/viro.1995.1208;
RA Mossman K., Upton C., Buller R.M., McFadden G.;
RT "Species specificity of ectromelia virus and vaccinia virus interferon-
RT gamma binding proteins.";
RL Virology 208:762-769(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10725549; DOI=10.1016/s0168-1702(99)00135-5;
RA Chen N., Buller R.M., Wall E.M., Upton C.;
RT "Analysis of host response modifier ORFs of ectromelia virus, the causative
RT agent of mousepox.";
RL Virus Res. 66:155-173(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9495531; DOI=10.1016/s0168-1702(97)00122-6;
RA Wall E.M., Cao J.X., Chen N., Buller R.M.L., Upton C.;
RT "A novel poxvirus gene and its human homolog are similar to an E. coli
RT lysophospholipase.";
RL Virus Res. 52:157-167(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Chen N., Danila M.I., Feng Z., Buller M.L., Wang C., Han X., Lefkowitz E.,
RA Upton C.;
RT "The genomic sequence of ectromelia virus, the causative agent of
RT mousepox.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12941926; DOI=10.1128/jvi.77.18.10139-10146.2003;
RA Ribas G., Rivera J., Saraiva M., Campbell R.D., Alcami A.;
RT "Genetic variability of immunomodulatory genes in ectromelia virus isolates
RT detected by denaturing high-performance liquid chromatography.";
RL J. Virol. 77:10139-10146(2003).
RN [6]
RP INTERACTION WITH HOST VESPR.
RX PubMed=9586637; DOI=10.1016/s1074-7613(00)80552-x;
RA Comeau M.R., Johnson R., DuBose R.F., Petersen M., Gearing P.,
RA VandenBos T., Park L., Farrah T., Buller R.M., Cohen J.I., Strockbine L.D.,
RA Rauch C., Spriggs M.K.;
RT "A poxvirus-encoded semaphorin induces cytokine production from monocytes
RT and binds to a novel cellular semaphorin receptor, VESPR.";
RL Immunity 8:473-482(1998).
RN [7]
RP FUNCTION.
RX PubMed=15611227; DOI=10.4049/jimmunol.174.1.51;
RA Walzer T., Galibert L., Comeau M.R., De Smedt T.;
RT "Plexin C1 engagement on mouse dendritic cells by viral semaphorin A39R
RT induces actin cytoskeleton rearrangement and inhibits integrin-mediated
RT adhesion and chemokine-induced migration.";
RL J. Immunol. 174:51-59(2005).
RN [8]
RP FUNCTION.
RX PubMed=15657950; DOI=10.1002/eji.200425669;
RA Walzer T., Galibert L., De Smedt T.;
RT "Poxvirus semaphorin A39R inhibits phagocytosis by dendritic cells and
RT neutrophils.";
RL Eur. J. Immunol. 35:391-398(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 15-399.
RX PubMed=20727575; DOI=10.1016/j.cell.2010.07.040;
RA Liu H., Juo Z.S., Shim A.H., Focia P.J., Chen X., Garcia K.C., He X.;
RT "Structural basis of semaphorin-plexin recognition and viral mimicry from
RT Sema7A and A39R complexes with PlexinC1.";
RL Cell 142:749-761(2010).
CC -!- FUNCTION: Acts as a semaphorin-like protein and binds to host plexin C1
CC receptor. May alter the movement of plexin C1-expressing cells
CC including dendritic cells, monocytes, or granulocytes in the proximity
CC of infected cells. May also regulate host cell cytoskeleton of
CC neighboring cells to improve viral infection.
CC {ECO:0000269|PubMed:15611227, ECO:0000269|PubMed:15657950}.
CC -!- SUBUNIT: Interacts with host VESPR. {ECO:0000269|PubMed:9586637}.
CC -!- INTERACTION:
CC Q8JL80; O60486: PLXNC1; Xeno; NbExp=3; IntAct=EBI-2927425, EBI-2927384;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; AF012825; AAM92444.1; -; Genomic_DNA.
DR EMBL; AJ574801; CAE00473.1; -; Genomic_DNA.
DR EMBL; AJ574802; CAE00474.1; -; Genomic_DNA.
DR EMBL; AJ574803; CAE00475.1; -; Genomic_DNA.
DR EMBL; AJ574804; CAE00476.1; -; Genomic_DNA.
DR EMBL; AJ574805; CAE00477.1; -; Genomic_DNA.
DR RefSeq; NP_671658.1; NC_004105.1.
DR PDB; 3NVN; X-ray; 2.26 A; A=15-399.
DR PDB; 6VXK; EM; 3.10 A; A/C=15-399.
DR PDBsum; 3NVN; -.
DR PDBsum; 6VXK; -.
DR SMR; Q8JL80; -.
DR IntAct; Q8JL80; 1.
DR GeneID; 951586; -.
DR KEGG; vg:951586; -.
DR EvolutionaryTrace; Q8JL80; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 1.
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; PF01403; Sema; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..399
FT /note="Semaphorin-like protein 139"
FT /id="PRO_0000412614"
FT DOMAIN 15..399
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 36..48
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 63..77
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 166..192
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:3NVN"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6VXK"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:3NVN"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3NVN"
FT STRAND 369..389
FT /evidence="ECO:0007829|PDB:3NVN"
SQ SEQUENCE 399 AA; 45358 MW; BD7B76AF04C0838D CRC64;
MIPLLFILFY FTNCIEWHKF ETSEEIISTY LIDDVLYTGV NGAVYTFSNN ELNKTGLTNN
NNYITTSIKV EDTLVCGTNN GNPKCWKIDG SEDPKYRGRG YAPYQNSKVT IISHNECVLS
DINISKEGIK RWRRFDGPCG YDLYTADNVI PKDGVRGAFV DKDGTYDKVY ILFTDTIDTK
RIVKIPYIAQ MCLNDEGGPS SLSSHRWSTF LKVELECDID GRSYRQIIHS KAIKTDNDTI
LYVFFDSPYS KSALCTYSMN AIKHSFSTSK LGGYTKQLPS PAPGICLPAG KVVPHTTFDI
IEQYNELDDI IKPLSQPIFE GPSGVKWFDI KEKENEHREY RIYFIKENTI YSFDTKSKQT
RSAQVDARLF SVMVTSKPLF IADIGIGVGI PRMKKILKM
