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Database: UniProt
Entry: A0A1Y9J025_ANOQN
LinkDB: A0A1Y9J025_ANOQN
Original site: A0A1Y9J025_ANOQN 
ID   A0A1Y9J025_ANOQN        Unreviewed;      1103 AA.
AC   A0A1Y9J025;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=MAGUK p55 subfamily member 5 {ECO:0000256|ARBA:ARBA00032294};
OS   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA016454-PC, ECO:0000313|Proteomes:UP000076407};
RN   [1] {ECO:0000313|Proteomes:UP000076407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AQUA016454-PC}
RP   IDENTIFICATION.
RC   STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA016454-PC};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004221}. Cell junction, adherens junction
CC       {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004236}. Cell projection, axon
CC       {ECO:0000256|ARBA:ARBA00004489}. Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus
CC       {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Perikaryon
CC       {ECO:0000256|ARBA:ARBA00004484}.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC       {ECO:0000256|ARBA:ARBA00007014}.
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DR   AlphaFoldDB; A0A1Y9J025; -.
DR   STRING; 34691.A0A1Y9J025; -.
DR   EnsemblMetazoa; AQUA016454-RC; AQUA016454-PC; AQUA016454.
DR   VEuPathDB; VectorBase:AQUA016454; -.
DR   Proteomes; UP000076407; Unassembled WGS sequence.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd12036; SH3_MPP5; 1.
DR   Gene3D; 1.20.1270.460; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR004172; L27_dom.
DR   InterPro; IPR035601; MPP5_SH3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR   PANTHER; PTHR23122:SF14; PROTEIN PALS1; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          518..574
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          665..744
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          757..828
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          907..1087
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          66..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..144
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1103 AA;  120734 MW;  E524350CE0F74489 CRC64;
     MRILKHWPRR RSGSSIVVLG GDDTLKPSIP IDDYQEDLEM YNMLAANQDN GPHREMAVDV
     PESFIARNKT PPRYPPPRST VTAAAASTPA TPASTQVNHV SNAMPQVAKH HHHQHHNHHH
     QQQQHPNHHL HHHHPPSSVH HNTHHHHGGG GDGGVSLELE PLDSYSERHL SSLDSSSQEY
     VKKGIIGGGG VGGGGSSKAP SSLGSVTSEF EPSLNGFGPL HGKHHHHSTV GGGGDLLRGS
     LSTNRSPSPA SSGDLGPPEY DVGPHRELPV DVPDSFVEMV KGPPRYPPPK PLIIKDAIRK
     KESCSSSESI DKPKPQTQSP SPPARNELNG SSKPVPPPRD HLRIEKDGRL TNRAPVPAPQ
     VPDRKIVPNA SSQHQHIGQV LEPTPDQLDS IKKFQEQLRR RREDEERIAA QNDFLRNSLR
     GSQRLRALQD NPIEKPPVGV DNEAYADDEV VAAAAEKIIG YGELVAALQR LQGHLNKHGL
     AALAGRVTAA QSLLLGPGIA RALAVRTAVL ERRRPKIPNP ICPNAQALAK DCVESLAQSR
     SQTAIELCDL LSTYEMEGLL LAHDRIASTT DRSPIASYGG SPITVPVPLG TASNNTASNN
     TTTSNNNNSI NNNTLTSAVK PATVMPSIPN NASLVNNNNN NIAKREPMSV PLGVLRDGSQ
     DHIKIIQIEK SSEPLGATIR NEGEAVVIGR VVRGGAAEKS GLLHEGDEIL EVNGIEMRGK
     SVNDVCALLG SMTGTLTFLV VPAGVPQILP GLGMRDPPVL HVRAHFDYDP EDDLYIPCRE
     LGISFQKGDV LHVISRDDPN WWQAYREGEE DQTLAGLIPS QSFQHQRESM KLAIAGEVGL
     RTRKDINGKA GGGSTLLCAR KGRKKKKKAS SEHGYPLYAT ATADDPDPEE ILTYEEVALY
     YPRASHKRPI VLIGPPNIGR HELRQRLMAD SERFAAAIPH TSRAQREGEV PGQDYHFISR
     QQFESDILAR KFVEHGEYEK AYYGTSLEAI RAVVASGKIC VLNLHPQSLK LLRSSDLKPY
     TVLVAPPSLE KLRQKRIRTG EPYKEEELKE IIATARDMEA RWGHLFDMII INNDTERAYH
     QLLAEINSLE REPQWVPSSW LHN
//
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