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Database: UniProt
Entry: L5KLQ7_PTEAL
LinkDB: L5KLQ7_PTEAL
Original site: L5KLQ7_PTEAL 
ID   L5KLQ7_PTEAL            Unreviewed;       669 AA.
AC   L5KLQ7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=MAGUK p55 subfamily member 6 {ECO:0000313|EMBL:ELK12589.1};
GN   ORFNames=PAL_GLEAN10021835 {ECO:0000313|EMBL:ELK12589.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK12589.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004202}.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC       {ECO:0000256|ARBA:ARBA00007014}.
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DR   EMBL; KB030660; ELK12589.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KLQ7; -.
DR   STRING; 9402.L5KLQ7; -.
DR   eggNOG; KOG0609; Eukaryota.
DR   InParanoid; L5KLQ7; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.287.650; L27 domain; 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; IPR036892; L27_dom_sf.
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:SF45; PROTEIN PALS2; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF101288; L27 domain; 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; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022427};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT   DOMAIN          127..178
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          179..237
FT                   /note="L27"
FT                   /evidence="ECO:0000259|PROSITE:PS51022"
FT   DOMAIN          259..338
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          344..413
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          467..654
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          53..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..117
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  74270 MW;  30130AB1BA4019B9 CRC64;
     MNISSGAVQA VLPPPALALE WGEGHARALS PQVVSFPTAL ECLIRRSRSA SASVRRVSDP
     ASPPGTLPAQ KNTRCLRKEA GGALARKRAL VRGAPYQPSA AAPPVPRHCP AAAPARPSPF
     PSVDSALGAA MQQVLDNLTE LPSSTGAEEI DLIFLKGIME NPIVKSLAKA HERLEDSKLE
     AVSDNNLELV NEILEDITPL INVDENAAEL VGILKEPHFQ SLLEAHDIVA SKCYDSPPSS
     PEMNNSVNNQ LLPVDAIRIL GIHKRAGEPL GVTFRVENND LVIARILHGG MIDRQGLLHV
     GDIIKEVNGH EVGNNPKELQ ELLKNISGSV TLKILPSYRD TITPQQVFVK CHFDYNPYND
     NLIPCKEAGL KFSKGEILQI VNREDPNWWQ ASHVKEGGSA GLIPSQFLEE KRKAFVRRDW
     DNSGPFCGTI SSKKKKKMMY LTTRNAEFDR HEIQIYEEVA KMPPFQRKTL VLIGAQGVGR
     RSLKNRFIVL NPTRFGTTVP FTSRKPREDE KDGQAYKFVS RSEMEADIKA GKYLEHGEYE
     GNLYGTKIDS ILEVVQTGRT CILDVNPQAL KVLRTSEFMP YVVFIAAPEL ETLRAMHKAV
     VDAGITTKLL TDSDLKKTVD ESARIQRAYN HYFDLIIIND NLDKAFEKLQ TAIEKLRMEP
     QWVPISWVY
//
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