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Database: UniProt
Entry: A0A182QC38_9DIPT
LinkDB: A0A182QC38_9DIPT
Original site: A0A182QC38_9DIPT 
ID   A0A182QC38_9DIPT        Unreviewed;      1355 AA.
AC   A0A182QC38;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=MAGUK p55 subfamily member 5 {ECO:0000256|ARBA:ARBA00032294};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF007196-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., 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 farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF007196-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF007196-PA};
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   EMBL; AXCN02001476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 69004.A0A182QC38; -.
DR   EnsemblMetazoa; AFAF007196-RA; AFAF007196-PA; AFAF007196.
DR   VEuPathDB; VectorBase:AFAF007196; -.
DR   OrthoDB; 2873706at2759; -.
DR   Proteomes; UP000075886; 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; -; 2.
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; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
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          784..840
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          917..996
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1009..1080
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1159..1339
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          256..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..414
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1355 AA;  148152 MW;  C85FA2B6F5906B13 CRC64;
     MQQRTTTPAG PPTASSSGKQ VVELNGYVII LVESRDGKIK LYGSPADKDN LEVADEILDV
     NERKLEDSPR AEVIKHIHEC IQSCMIKLRV KRRSDSRLAG ELGNAVQDAF VIAVEQQARE
     RLQRLSALKR ITPLNQQSQA KGGATQDLSF LKEASPIYVT SLSAVPSGAT VATNNNNTVA
     AGVTGAASAA STSAYHTSTL HHSLVNNNNL NSNIGKPQGG GGLDSTANSY YSNLTNTFLA
     NGHGSKREQL ATLSEGELEP QDEPQYESSG NISRGGTEVL LGDQNLRQES RPRRRSGSSI
     VVLGGDDTLK PSIPIDDYQE DLEMYNMLAA NQDNGPHREM AVDVPESFIA RNKTPPRYPP
     PRSASAAVAA TTAAPATPAS TQVIHVSNAM PQVAKHHQQQ HHHHQHHHHP HHHPAANGGG
     VSLELEPLDS YSDRHLSSLD SSQECVKKGG SSKGPSSLGS VTSEFDPLSV SLTNGYGHQL
     RKHANDLRGS LSTNRSTSPS SSGDLGPPEY DVGPHRELPV DVPDSFVEIV KGPPRYPPPK
     PLIIKDVIRK KESCSSSESI DKPKPQSPQS PARNELNGST KPVPPPRDHL RIEKDGRLTN
     RAPVPAPQVP DRKIAPIASQ HQHIGQVLEP TPDQLDSIKK FQEQLRRRRE DEERIAAQND
     FLRNSLRGSQ RLRALQDNPI EKPPVGVDNE AYAEDEVVEK IIGMHHLRWV PSDGNLIRTF
     ARPFTGYSEL VAALQRLQGH LNKHGLATLA GRVTAAQSLL LGPGIARALA VRTAVLERRR
     PKVPNPICPN AQALAKDCVE SLAQSGSPTA IELCDLLSTY EMEGLLLAHD RIASTTDRSP
     IASYGGSPVT VPMPSLSNNI NNNNTLTSAA VKPATVMPSI PNNASLVNNN NNNIAKREPM
     SVPLGVLRDG SQDHIKIIQI EKSSEPLGAT IRNEGEAVVI GRVVRGGAAE KSGLLHEGDE
     ILEVNGIEMR GKSVNDVCAL LGSMTGTLTF LVVPAGVPQI LPGLGMRDPP VLHVRAHFDY
     DPEDDLYIPC RELGISFQKG DVLHVISRDD PNWWQAYREG EEDQTLAGLI PSQSFQHQRE
     SMKLAIAGEV GLRTRKDING KAGGGSTLLC ARKGRKKKKK ASSEHGYPLY ATATADDPDP
     EEILTYEEVA LYYPRASHKR PIVLIGPPNI GRHELRQRLM ADSERFAAAI PHTSRAQREG
     EVPGQDYHFI SRQQFESDIL ARKFVEHGEY EKAYYGTSLE AIRAVVASGK ICVLNLHPQS
     LKLLRSSDLK PYTVLVAPPS LEKLRQKRIR TGEPYKEEEL KEIIATARDM EARWGHLFDM
     IIINNDTERA YHQLLAEINS LEREPQWVPS SWLHN
//
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