ID Q7QHP4_ANOGA Unreviewed; 879 AA.
AC Q7QHP4;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 3.
DT 24-JAN-2024, entry version 121.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial {ECO:0000256|ARBA:ARBA00018307};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
DE Flags: Fragment;
GN ORFNames=AgaP_AGAP011286 {ECO:0000313|EMBL:EAA05165.3};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA05165.3};
RN [1] {ECO:0000313|EMBL:EAA05165.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA05165.3};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA05165.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA05165.3};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA05165.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA05165.3};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA05165.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA05165.3};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA05165.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA05165.3};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001837};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004325}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAA05165.3}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAAB01008816; EAA05165.3; -; Genomic_DNA.
DR RefSeq; XP_309360.3; XM_309360.4.
DR AlphaFoldDB; Q7QHP4; -.
DR STRING; 7165.Q7QHP4; -.
DR PaxDb; 7165-AGAP011286-PA; -.
DR GeneID; 1270645; -.
DR KEGG; aga:AgaP_AGAP011286; -.
DR VEuPathDB; VectorBase:AGAP011286; -.
DR eggNOG; KOG0447; Eukaryota.
DR HOGENOM; CLU_012302_0_0_1; -.
DR OMA; ESQTDAF; -.
DR OrthoDB; 48011at2759; -.
DR PhylomeDB; Q7QHP4; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR045817; OPA1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF67; DYNAMIN-LIKE 120 KDA PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF19434; OPA1_C; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 204..479
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT COILED 118..170
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 815..874
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EAA05165.3"
SQ SEQUENCE 879 AA; 101692 MW; B1CE37E7D368116C CRC64;
QEFLRPPNAS GWQYYGGQQQ RHYGMLIGRV LRGVLKLRYL VLGSAIGGGV TLNKRYEEWK
DGLPDMKWLE EVFPDNEKWA GFTKNLLAVK DAVKDSIEIA TKEELRAKNT VNAKGLSAED
SRKRVDTLQA QVDSLQTEIM NVQLKYQREV EKLEKENRDL RQQYLILKTN RKQPTKKRIK
KSLIDMYSEV LDELSGYDTS YTTADHLPRV VVVGDQSSGK TSVLESIAQA RIFPRGSGEM
MTRAPVKVTL SEGPYHVAQF RDSEREYDLT KESDLAELRR DVEIRMRNSV RGGKTVSMDV
ISMTVKGPGL QRMVLVDLPG IISTQTVDMA PDTRDQIKHM TEHYMSNPNA IILCIQDGSV
DAERSNVTDL VSQCDPLGKR TIFVLTKVDL AEDLADPNRI RKILSGKLFP MKALGYFAVV
TGRGRKDDSI ETIREYEEKF FKNSKLFQSG VTMSHQVTTR NLSLAVADRF WKMVRETIEQ
QADAFKATRF NLETEWKNNF PRLRESGRDE LFEKAKGEVL DEVVNLSQVS AKKWEELMNS
KLWEKLSSYV FENIYLPAAQ SGSQNSFNTM VDIKLRQWAE QALPAKSVEA GWEALQKEFQ
HLMEVARRTP DHDDLYDNLK SAVIDEAIRR HSWEDKAIDM LRVIQLNTLE DRSVHDKQEW
DQAVRFFEAS VKDKLQATET TIGEMFGPST SQKWLHWRSS TEEQNKRRQV KSELDKILDS
DSKHSPTLSY DELTTVRKNL QRGNVEVETD YIRETWYPIY RRHFLKQALN RAYDCRKAYY
LYSQQGSDCE VNCSDVVLFW RIQQVIKVTA NALRQQVINR EARRLDKEIK EVLDEYGEDD
EKKLQLLTGK RVQLAEELIR VRQIQEKLEE FINALNLEK
//