ID   LST2_ANOGA              Reviewed;        1161 AA.
AC   Q7QAJ2;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 6.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Lateral signaling target protein 2 homolog;
GN   ORFNames=AGAP003678;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
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).
CC   -!- FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR)
CC       signaling. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lst-2 family. {ECO:0000305}.
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DR   EMBL; AAAB01008888; EAA08780.5; -; Genomic_DNA.
DR   RefSeq; XP_313459.5; XM_313459.5.
DR   AlphaFoldDB; Q7QAJ2; -.
DR   SMR; Q7QAJ2; -.
DR   STRING; 7165.AGAP003678-PA; -.
DR   PaxDb; Q7QAJ2; -.
DR   GeneID; 1274352; -.
DR   KEGG; aga:AgaP_AGAP003678; -.
DR   VEuPathDB; VectorBase:AGAP003678; -.
DR   eggNOG; KOG1819; Eukaryota.
DR   HOGENOM; CLU_007360_1_1_1; -.
DR   InParanoid; Q7QAJ2; -.
DR   OMA; DAPRCMA; -.
DR   OrthoDB; 451347at2759; -.
DR   PhylomeDB; Q7QAJ2; -.
DR   Proteomes; UP000007062; Chromosome 2R.
DR   GO; GO:0031901; C:early endosome membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15731; FYVE_LST2; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR043269; FYVE_LST2.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..1161
FT                   /note="Lateral signaling target protein 2 homolog"
FT                   /id="PRO_0000378959"
FT   ZN_FING         1099..1159
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          417..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..918
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          992..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..510
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..668
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..701
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..741
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..773
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..831
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..918
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1072
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1077..1095
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         1154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ   SEQUENCE   1161 AA;  125467 MW;  84BC9910EDDA5DD6 CRC64;
     MVTTIVIACT FRAGTTHHSW CAAVALRAGS FAADDKSLLA RFYHADRALT AIASELDSFD
     GRAEPVRCTR LVSRLRQGQD RVLAITNQIM DELLGDDRAQ RAFRVKFPEE VLQESLAGQL
     WFGAECLAAG SSILNREAES AKMRPLAKAV TKSLEIVRNR LREQCLRNNT PNSPTLRLDI
     NDAATEQLYE SLKIFDRLFA EFELVYVSAM VQVKTKQEYE MQELICVLFS ETLQRALKTG
     LLEQEQVDSY DPALMFSIPR LAIIAGLVIF REGPLNMDQP ADNISEMFRP FRKLLIKMRD
     LLHALTKQEL YQLEKLLCTN EEISASEQLI CDEKGRSGGD GGSGSGGTAA AGVKEFDALE
     PVGESQEHVV IVTTVTTTNA PNVVGDGPGA TGCTDATSGA DGRLHIVSQG YGVSTGATGS
     SGFGSGRGGC SSSSTSRPKQ RHNQAHLRQR GAPRHSSQSF APEASYAGDD REPVVEEDNN
     NHLRKEIEEE DVDDDMEEEE EDEEEDEVDD DAMLKDGLVT TDCASGYLIP NTNFGNLLQT
     NEAPLTDSFI ATDDELRLLG AETASSPPAM TQANIDSILA ASAAGSGGQQ QQQQQQQLID
     SDSGHGTANH STDMSPELET ERTVVAAGQP NANDAPLDGS VSKQQPVRDR SRSGSSTVHK
     HAEISESSSD YEEADVDDEP DDVDADDDDE EEDDVVGEVE EQNDSEPTFN RKVGGAPKEA
     FRSQLRCKAA RNHRKSSHHR PRPSTSSSSS SAAYRNKSQS HQHHHHHHHH HHHSYAESAE
     GTSSVVSTIT TSNNSTSNGS TRHHSRMQQQ HQQHQQQRNS SSSCDTSPTQ SECSDAQEVA
     LAIRAAGRNK FKSTENLLHR LFVCIAGVAD QLQTNFAADL RKMLRSVFIM NSSPPEPDEP
     PEPSGSEEES KDSQHNHPSD LFEFRASEQD VITADQQNHS GGSSQSIYSA EEANPEQDSV
     FGSSGDSSPV RRTASVESRN VTVNVSVSVV ASSPVGAGGA GGGGMVGGSR TGQERSVSLS
     EACIVVEGGK ASAGGGGGTR RHSASGSKND YGRSRSSPSS PVNSNTGGGG GGNHHSSAHH
     TAHEQQRRMP EEPPRWIPDC DAPRCMACAS AFTPFRRRHH CRNCGGVFCG VCSNLSKPLP
     KYGLTKAVRV CRDCYIHEVG V