SEMA_VACCC
ID SEMA_VACCC Reviewed; 403 AA.
AC P21062;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 29-SEP-2021, entry version 79.
DE RecName: Full=Semaphorin-like protein A39;
DE Flags: Precursor;
GN ORFNames=A39R;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11514717; DOI=10.1099/0022-1317-82-9-2083;
RA Gardner J.D., Tscharke D.C., Reading P.C., Smith G.L.;
RT "Vaccinia virus semaphorin A39R is a 50-55 kDa secreted glycoprotein that
RT affects the outcome of infection in a murine intradermal model.";
RL J. Gen. Virol. 82:2083-2093(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 15-396.
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 host 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host VESPR. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11514717}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; M35027; AAA48169.1; -; Genomic_DNA.
DR PIR; E42521; E42521.
DR PDB; 3NVX; X-ray; 2.00 A; A/B=15-396.
DR PDBsum; 3NVX; -.
DR SMR; P21062; -.
DR EvolutionaryTrace; P21062; -.
DR Proteomes; UP000008269; Genome.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..403
FT /note="Semaphorin-like protein A39"
FT /id="PRO_0000099327"
FT DOMAIN 15..403
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3NVX"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 169..180
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:3NVX"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:3NVX"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:3NVX"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:3NVX"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:3NVX"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 373..386
FT /evidence="ECO:0007829|PDB:3NVX"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:3NVX"
SQ SEQUENCE 403 AA; 45741 MW; 08A384C7D68F374B CRC64;
MIPLLFILFY FANGIEWHKF ETSEEIISTY LLDDVLYTGV NGAVYTFSNN KLNKTGLTNN
NYITTSIKVE DADKDTLVCG TNNGNPKCWK IDGSDDPKHR GRGYAPYQNS KVTIISYNEC
VLSDINISKE GIKRWRRFDG PCGYDLYTAD NVIPKDGLRG AFVDKDGTYD KVYILFTDTI
GSKRIVKIPY IAQMCLNDEG GPSSLSSHRW STFLKVELEC DIDGRSYRQI IHSRTIKTDN
DTILYVFFDS PYSKSALCTY SMNTIKQSFS TSKLEGYTKQ LPSPAPGICL PAGKVVSHTT
FEVIEKYNVL DDIIKPLSNQ PIFEGPSGVK WFDIKEKENE HREYRIYFIK ENSIYSFDTK
SKQTRSSQVD ARLFSVMVTS KPLFIADIGI GVGMPQMKKI LKM
