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VEGFH_ORFN2
ID   VEGFH_ORFN2             Reviewed;         133 AA.
AC   P52584;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-JUN-2021, entry version 86.
DE   RecName: Full=Vascular endothelial growth factor homolog;
DE   Flags: Precursor;
GN   ORFNames=A2R;
OS   Orf virus (strain NZ2) (OV NZ-2).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Parapoxvirus.
OX   NCBI_TaxID=10259;
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8254780; DOI=10.1128/jvi.68.1.84-92.1994;
RA   Lyttle D.J., Fraser K.M., Fleming S.B., Mercer A.A., Robinson A.J.;
RT   "Homologs of vascular endothelial growth factor are encoded by the poxvirus
RT   orf virus.";
RL   J. Virol. 68:84-92(1994).
CC   -!- FUNCTION: Induces endothelial proliferation.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC       {ECO:0000305}.
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DR   EMBL; S67520; AAB29220.2; -; Genomic_DNA.
DR   PIR; B49530; B49530.
DR   PDB; 2GNN; X-ray; 2.30 A; A/B/C/D=21-133.
DR   PDB; 3V6B; X-ray; 3.20 A; A=21-133.
DR   PDBsum; 2GNN; -.
DR   PDBsum; 3V6B; -.
DR   SMR; P52584; -.
DR   DIP; DIP-29295N; -.
DR   IntAct; P52584; 1.
DR   KEGG; ag:AAB29220; -.
DR   EvolutionaryTrace; P52584; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   CDD; cd00135; PDGF; 1.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR023581; PD_growth_factor_CS.
DR   InterPro; IPR000072; PDGF/VEGF_dom.
DR   Pfam; PF00341; PDGF; 1.
DR   SMART; SM00141; PDGF; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00249; PDGF_1; 1.
DR   PROSITE; PS50278; PDGF_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Growth factor; Mitogen;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..133
FT                   /note="Vascular endothelial growth factor homolog"
FT                   /id="PRO_0000023417"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        61
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        70
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..114
FT                   /evidence="ECO:0000250"
FT   HELIX           27..34
FT                   /evidence="ECO:0007829|PDB:2GNN"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:2GNN"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:2GNN"
FT   STRAND          58..69
FT                   /evidence="ECO:0007829|PDB:2GNN"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:2GNN"
FT   STRAND          76..91
FT                   /evidence="ECO:0007829|PDB:2GNN"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:2GNN"
FT   STRAND          101..116
FT                   /evidence="ECO:0007829|PDB:2GNN"
SQ   SEQUENCE   133 AA;  14715 MW;  917C0F6883030C39 CRC64;
     MKLLVGILVA VCLHQYLLNA DSNTKGWSEV LKGSECKPRP IVVPVSETHP ELTSQRFNPP
     CVTLMRCGGC CNDESLECVP TEEVNVSMEL LGASGSGSNG MQRLSFVEHK KCDCRPRFTT
     TPPTTTRPPR RRR
 
 
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