COPIA_DROME
ID COPIA_DROME Reviewed; 1409 AA.
AC P04146; Q03728; Q24280; Q24555; Q24585; Q24586; Q24587; Q53XF8; Q8T391;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Copia protein;
DE AltName: Full=Gag-int-pol protein;
DE Contains:
DE RecName: Full=Copia VLP protein;
DE Contains:
DE RecName: Full=Copia protease;
DE EC=3.4.23.-;
GN Name=GIP; Synonyms=COPIA;
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 [GENOMIC DNA].
RX PubMed=2410772; DOI=10.1128/mcb.5.7.1630-1638.1985;
RA Mount S.M., Rubin G.M.;
RT "Complete nucleotide sequence of the Drosophila transposable element copia:
RT homology between copia and retroviral proteins.";
RL Mol. Cell. Biol. 5:1630-1638(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 2-10, AND
RP ALTERNATIVE SPLICING.
RX PubMed=2409449; DOI=10.1038/315773a0;
RA Emori Y., Shiba T., Kanaya S., Inouye S., Yuki S., Saigo K.;
RT "The nucleotide sequences of copia and copia-related RNA in Drosophila
RT virus-like particles.";
RL Nature 315:773-776(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=2538806; DOI=10.1093/nar/17.5.2134;
RA Miller K., Rosenbaum J., Zbrzezna V., Pogo A.O.;
RT "The nucleotide sequence of Drosophila melanogaster copia-specific 2.1-kb
RT mRNA.";
RL Nucleic Acids Res. 17:2134-2134(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT), AND MUTAGENESIS OF
RP ASP-292.
RC TISSUE=Larva;
RX PubMed=1689241; DOI=10.1002/j.1460-2075.1990.tb08140.x;
RA Yoshioka K., Honma H., Zushi M., Kondo S., Togashi S., Miyake T., Shiba T.;
RT "Virus-like particle formation of Drosophila copia through autocatalytic
RT processing.";
RL EMBO J. 9:535-541(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P04146-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P04146-2; Sequence=VSP_005226;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD27357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X04456; CAA28054.2; -; Genomic_DNA.
DR EMBL; X04456; CAD27357.1; ALT_INIT; Genomic_DNA.
DR EMBL; X02599; CAA26444.1; -; Genomic_DNA.
DR EMBL; X02599; CAA26445.1; -; Genomic_DNA.
DR EMBL; X02600; CAA26446.1; -; mRNA.
DR EMBL; X02600; CAA26447.1; -; mRNA.
DR EMBL; X13719; CAA31997.1; -; mRNA.
DR EMBL; X54147; CAA38086.1; -; Genomic_DNA.
DR EMBL; BT011428; AAR99086.1; -; mRNA.
DR PIR; A03324; OFFFCP.
DR AlphaFoldDB; P04146; -.
DR MEROPS; A11.001; -.
DR PeptideAtlas; P04146; -.
DR PRIDE; P04146; -.
DR FlyBase; FBgn0013437; copia\GIP.
DR ChiTaRS; Gip; fly.
DR PRO; PR:P04146; -.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR025724; GAG-pre-integrase_dom.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR013103; RVT_2.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF13976; gag_pre-integrs; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF07727; RVT_2; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aspartyl protease; ATP-binding;
KW Direct protein sequencing; Hydrolase; Metal-binding; Nucleotide-binding;
KW Protease; Transposable element; Zinc; Zinc-finger.
FT CHAIN 1..270
FT /note="Copia VLP protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026135"
FT CHAIN 271..1409
FT /note="Copia protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026136"
FT DOMAIN 476..644
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 230..247
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 760..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /note="For protease activity"
FT /evidence="ECO:0000250"
FT VAR_SEQ 392..1374
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:2538806"
FT /id="VSP_005226"
FT VARIANT 1265..1288
FT /note="STTGYLFKMFDFNLICWNTKRQNS -> VQQGIYSKCLILISFVGIQRDRTQ
FT (in variant copia-related)"
FT VARIANT 1289..1409
FT /note="Missing (in variant copia-related)"
FT MUTAGEN 292
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1689241"
FT CONFLICT 191
FT /note="S -> N (in Ref. 2; CAA26447)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> V (in Ref. 2; CAA26447)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="Q -> E (in Ref. 2; CAA26447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1409 AA; 162818 MW; BE89440763A47691 CRC64;
MDKAKRNIKP FDGEKYAIWK FRIRALLAEQ DVLKVVDGLM PNEVDDSWKK AERCAKSTII
EYLSDSFLNF ATSDITARQI LENLDAVYER KSLASQLALR KRLLSLKLSS EMSLLSHFHI
FDELISELLA AGAKIEEMDK ISHLLITLPS CYDGIITAIE TLSEENLTLA FVKNRLLDQE
IKIKNDHNDT SKKVMNAIVH NNNNTYKNNL FKNRVTKPKK IFKGNSKYKV KCHHCGREGH
IKKDCFHYKR ILNNKNKENE KQVQTATSHG IAFMVKEVNN TSVMDNCGFV LDSGASDHLI
NDESLYTDSV EVVPPLKIAV AKQGEFIYAT KRGIVRLRND HEITLEDVLF CKEAAGNLMS
VKRLQEAGMS IEFDKSGVTI SKNGLMVVKN SGMLNNVPVI NFQAYSINAK HKNNFRLWHE
RFGHISDGKL LEIKRKNMFS DQSLLNNLEL SCEICEPCLN GKQARLPFKQ LKDKTHIKRP
LFVVHSDVCG PITPVTLDDK NYFVIFVDQF THYCVTYLIK YKSDVFSMFQ DFVAKSEAHF
NLKVVYLYID NGREYLSNEM RQFCVKKGIS YHLTVPHTPQ LNGVSERMIR TITEKARTMV
SGAKLDKSFW GEAVLTATYL INRIPSRALV DSSKTPYEMW HNKKPYLKHL RVFGATVYVH
IKNKQGKFDD KSFKSIFVGY EPNGFKLWDA VNEKFIVARD VVVDETNMVN SRAVKFETVF
LKDSKESENK NFPNDSRKII QTEFPNESKE CDNIQFLKDS KESENKNFPN DSRKIIQTEF
PNESKECDNI QFLKDSKESN KYFLNESKKR KRDDHLNESK GSGNPNESRE SETAEHLKEI
GIDNPTKNDG IEIINRRSER LKTKPQISYN EEDNSLNKVV LNAHTIFNDV PNSFDEIQYR
DDKSSWEEAI NTELNAHKIN NTWTITKRPE NKNIVDSRWV FSVKYNELGN PIRYKARLVA
RGFTQKYQID YEETFAPVAR ISSFRFILSL VIQYNLKVHQ MDVKTAFLNG TLKEEIYMRL
PQGISCNSDN VCKLNKAIYG LKQAARCWFE VFEQALKECE FVNSSVDRCI YILDKGNINE
NIYVLLYVDD VVIATGDMTR MNNFKRYLME KFRMTDLNEI KHFIGIRIEM QEDKIYLSQS
AYVKKILSKF NMENCNAVST PLPSKINYEL LNSDEDCNTP CRSLIGCLMY IMLCTRPDLT
TAVNILSRYS SKNNSELWQN LKRVLRYLKG TIDMKLIFKK NLAFENKIIG YVDSDWAGSE
IDRKSTTGYL FKMFDFNLIC WNTKRQNSVA ASSTEAEYMA LFEAVREALW LKFLLTSINI
KLENPIKIYE DNQGCISIAN NPSCHKRAKH IDIKYHFARE QVQNNVICLE YIPTENQLAD
IFTKPLPAAR FVELRDKLGL LQDDQSNAE
