CF1A_DROME
ID CF1A_DROME Reviewed; 427 AA.
AC P16241; Q24460; Q86P26; Q9VRY9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 5.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=POU domain protein CF1A;
DE AltName: Full=Chorion factor 1A;
DE Short=CF1-A;
DE AltName: Full=Protein drifter;
DE AltName: Full=Ventral veins lacking protein;
GN Name=vvl; Synonyms=Cf1a; ORFNames=CG10037;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=1673230; DOI=10.1038/350577a0;
RA Treacy M.N., He X., Rosenfeld M.G.;
RT "I-POU: a POU-domain protein that inhibits neuron-specific gene
RT activation.";
RL Nature 350:577-584(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1680380; DOI=10.1016/0925-4773(91)90045-8;
RA Billin A.N., Cockerill K.A., Poole S.J.;
RT "Isolation of a family of Drosophila POU domain genes expressed in early
RT development.";
RL Mech. Dev. 34:75-84(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-427, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=1967821; DOI=10.1038/343467a0;
RA Johnson W.A., Hirsh J.;
RT "Binding of a Drosophila POU-domain protein to a sequence element
RT regulating gene expression in specific dopaminergic neurons.";
RL Nature 343:467-470(1990).
RN [7]
RP SHOWS THAT CF1A DOES NOT ASSOCIATE WITH ACJ6.
RX PubMed=8986770; DOI=10.1073/pnas.93.26.15097;
RA Turner E.E.;
RT "Similar DNA recognition properties of alternatively spliced Drosophila POU
RT factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15097-15101(1996).
CC -!- FUNCTION: Binds to a DNA sequence element required for the expression
CC of the dopa decarboxylase gene (Ddc) in specific dopaminergic neurons.
CC Could also play an early role in specific ectodermal cells, and a
CC subsequent role in the embryonic nervous system.
CC {ECO:0000269|PubMed:1680380, ECO:0000269|PubMed:1967821}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Coexpressed with acj6 in overlapping subsets of
CC neurons in the embryonic epidermis and central nervous system. First
CC detected in the precursor of the tracheal pits and the stomodeal
CC invagination and later in the peripheral nervous system.
CC {ECO:0000269|PubMed:1673230, ECO:0000269|PubMed:1680380,
CC ECO:0000269|PubMed:1967821}.
CC -!- DEVELOPMENTAL STAGE: Expressed at maximal levels in early embryos (6-12
CC hours). Expressed at lower levels during development.
CC {ECO:0000269|PubMed:1680380}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to interact with acj6.
CC {ECO:0000305|PubMed:1673230}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA41341.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X58435; CAA41341.1; ALT_FRAME; mRNA.
DR EMBL; M81959; AAA28831.1; -; mRNA.
DR EMBL; AE014296; AAF50641.3; -; Genomic_DNA.
DR EMBL; BT003517; AAO39521.1; -; mRNA.
DR EMBL; X52252; CAA36496.1; -; Genomic_DNA.
DR PIR; S19095; S19095.
DR RefSeq; NP_001286957.1; NM_001300028.1.
DR RefSeq; NP_523948.1; NM_079224.5.
DR AlphaFoldDB; P16241; -.
DR SMR; P16241; -.
DR BioGRID; 64202; 19.
DR DIP; DIP-17200N; -.
DR IntAct; P16241; 7.
DR STRING; 7227.FBpp0076653; -.
DR PaxDb; P16241; -.
DR DNASU; 38752; -.
DR EnsemblMetazoa; FBtr0076944; FBpp0076653; FBgn0086680.
DR EnsemblMetazoa; FBtr0345911; FBpp0311831; FBgn0086680.
DR GeneID; 38752; -.
DR KEGG; dme:Dmel_CG10037; -.
DR CTD; 38752; -.
DR FlyBase; FBgn0086680; vvl.
DR VEuPathDB; VectorBase:FBgn0086680; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000171806; -.
DR HOGENOM; CLU_404003_0_0_1; -.
DR InParanoid; P16241; -.
DR OMA; TMTSQVM; -.
DR OrthoDB; 752252at2759; -.
DR SignaLink; P16241; -.
DR BioGRID-ORCS; 38752; 0 hits in 3 CRISPR screens.
DR ChiTaRS; vvl; fly.
DR GenomeRNAi; 38752; -.
DR PRO; PR:P16241; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0086680; Expressed in wing disc and 37 other tissues.
DR ExpressionAtlas; P16241; baseline and differential.
DR Genevisible; P16241; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0035284; P:brain segmentation; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; TAS:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR GO; GO:0002807; P:positive regulation of antimicrobial peptide biosynthetic process; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR016362; TF_POU_3.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PIRSF; PIRSF002629; Transcription_factor_POU; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Homeobox; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..427
FT /note="POU domain protein CF1A"
FT /id="PRO_0000100774"
FT DOMAIN 212..286
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 304..363
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 39..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 83..102
FT /note="SWSALHPDPWMQTHHTHHLP -> LMECPPSGSVDANPSYAPSA (in
FT Ref. 6; CAA36496)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..140
FT /note="GMASPHAAWHA -> ACLAPCRLAC (in Ref. 6; CAA36496)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="A -> G (in Ref. 6; CAA36496)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="H -> N (in Ref. 5; AAO39521)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..375
FT /note="PPNTLGGDMMDG -> AKYARRRHDGR (in Ref. 6; CAA36496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 45927 MW; 161F40CF3DBB8BF7 CRC64;
MAATSYMTPP SGDLDMALGG GGYHTSSPRS AADAGEMKYM QHHHHHHAAA AAAAHHQLPS
SPSPNGQGNG GGLGLGSGSG LGSWSALHPD PWMQTHHTHH LPAAAAVASA ADTVKQEMSH
LSQQTRIQQG MASPHAAWHA PHAGHYAPTG GSPLQYHHAM NGMLHHPAHA VAAAHHQSVA
PLHHTLRGES PQLHIHHHMG GGDRDAISGG EEDTPTSDDL EAFAKQFKQR RIKLGFTQAD
VGLALGTLYG NVFSQTTICR FEALQLSFKN MCKLKPLLQK WLEEADSTTG SPTSIDKIAA
QGRKRKKRTS IEVSVKGALE QHFHKQPKPS AQEITSLADS LQLEKEVVRV WFCNRRQKEK
RMTPPNTLGG DMMDGMPPGH MHHGGYHPHH DMHGSPMGTH SHSHSPPMLS PQNMQSSAVA
AHQLAAH
