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Database: UniProt
Entry: E2AZ20_CAMFO
LinkDB: E2AZ20_CAMFO
Original site: E2AZ20_CAMFO 
ID   E2AZ20_CAMFO            Unreviewed;       797 AA.
AC   E2AZ20;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Protein enabled {ECO:0000313|EMBL:EFN61315.1};
GN   ORFNames=EAG_00946 {ECO:0000313|EMBL:EFN61315.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN61315.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the Ena/VASP family.
CC       {ECO:0000256|ARBA:ARBA00009785}.
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DR   EMBL; GL444070; EFN61315.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2AZ20; -.
DR   STRING; 104421.E2AZ20; -.
DR   InParanoid; E2AZ20; -.
DR   OMA; YQQMVQV; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   CDD; cd01207; EVH1_Ena_VASP-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR038023; VASP_sf.
DR   InterPro; IPR014885; VASP_tetra.
DR   InterPro; IPR000697; WH1/EVH1_dom.
DR   PANTHER; PTHR11202:SF22; PROTEIN ENABLED; 1.
DR   PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR   Pfam; PF08776; VASP_tetra; 1.
DR   Pfam; PF00568; WH1; 1.
DR   SMART; SM00461; WH1; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          1..98
FT                   /note="WH1"
FT                   /evidence="ECO:0000259|PROSITE:PS50229"
FT   REGION          133..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..328
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..573
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   797 AA;  83814 MW;  63307BECD4B154F5 CRC64;
     MVYDDVNKKW IPSGSSSGLS KVQLYHHQVN NTFRVVGRKL QDHEIVINCA ILKGLKYNQA
     TVTFHQWRDN KQVYGLNFSS KDDADAFARA MLQALDVLSN GSNISRSLAP TTATTTQQQT
     AYQQQQQQQQ QQQSQATAQY EEDMGYSESH TSVLTGCSQG RSARISLSLG HLPTGGQTAL
     LVGTAITTPE HPNNATVSGA VGTVIQMGCA RGSPGDGHTR TMTREDVAII QERRMSQQSQ
     ATGSPNPISP SCPPTAQQQQ QQQQQQQQQS GHHRTSSAPP APQPPQQQQS ALMQGVVMAP
     APPQMSTGPP VPPPQPPIAP PAPPCPPAMM NFNSSAAPTP PMMMTQYAQS PSSQSNLANQ
     QPQAIYVTNQ ASQYGAVPTS NQYAASAASA GGTGSTGASN VVGQSPNQYP QSSNPSNFYG
     TNSQTSNYAT GGQTNAGQYN QSTGNQAAPY GTGGNQYGSS SSINQYAAGP PPPGPGSQYA
     VAQPGQSQYG SIVSQAQAQY GGAASPAVPV AGATNPYGTP SNSVNQYAAA GLHTVAANAY
     APIASSGPPP PPMIPLTGIA APPPPPPPPV PNANNSTASA SSVSSSSDPP PDTNSLAAAL
     QARLKKKQQQ SQPVENSGSS TSSSGSGSSG NYGTLGRGGG GGMASMMDEM AKTLARRRAA
     AEKKQPEQPP EPESSPDKKS WDKNNTSNNK FSNGAESPKS VRKRFGSASE DTLLKVNGVN
     DGTSFTAQEM EAFKVEIIKE VRKEFQKMKQ EIIDGTDILL LQSLRKNLVA LIRILVDSTS
     MFVGKWKNQN SCRRYIR
//
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