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Database: UniProt
Entry: A0A218US26_9PASE
LinkDB: A0A218US26_9PASE
Original site: A0A218US26_9PASE 
ID   A0A218US26_9PASE        Unreviewed;      1277 AA.
AC   A0A218US26;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 {ECO:0000313|EMBL:OWK56132.1};
GN   Name=MAGI2 {ECO:0000313|EMBL:OWK56132.1};
GN   ORFNames=RLOC_00002377 {ECO:0000313|EMBL:OWK56132.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK56132.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK56132.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK56132.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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:OWK56132.1}.
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DR   EMBL; MUZQ01000172; OWK56132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218US26; -.
DR   STRING; 299123.ENSLSDP00000023777; -.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00992; PDZ_signaling; 6.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.30.42.10; -; 6.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1.
DR   PANTHER; PTHR10316:SF27; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF16663; MAGI_u1; 1.
DR   Pfam; PF00595; PDZ; 6.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 6.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 6.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 6.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OWK56132.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:OWK56132.1}.
FT   DOMAIN          17..101
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          109..185
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   DOMAIN          303..336
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          349..382
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          427..496
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          605..668
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          764..846
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          906..996
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1141..1223
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          203..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          849..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        860..899
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1035
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1072
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1277 AA;  141493 MW;  72FF5E294CCD7F95 CRC64;
     MSKGLKKKSH WTSRVHEIVI VRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYEGGSKL
     VPEELLLEVN ETPVAGLTIR DVLAVIKHCK DPIRLKCVKQ GGIVDKDLRH YLNLRFQKGS
     VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EDFMELEKSG ALLESGTYED
     NYYGTPKPPA EPAPLLLNVT DQILPGATPG AEGKRKRNKS VSNMEKTGIE PPEEEEEERP
     VVNGNDVTVT PESSEHEEKS TAVSGEASTT QPCPAPGYGQ PEEAKEDMDV TKQTKPEEND
     DLGPLPDNWE MAYTEKGEVY FIDHNTKTTS WLDPRLAKKA KPPEECKENE LPYGWEKIDD
     PIYGTYYVDH INRRTQFENP VLEAKRKLQQ HNMPNAELGT KPMQAQGFRE KPLFTRDASQ
     LKGTFLSTTL KKSNMGFGFT IIGGDEPDEF LQVKSVIPDG PAAQDGKMET GDVIVYINEV
     CVLGHTHADV VKLFQSVPIG QSVNLVLCRG YPLPFDPEDP ANSMVPPLAV MERPPVVVNG
     RHNYETYLEY ISRTSQSVPD VTDRPPHSLH SIPADSQLDS TFPPPAHDDN VSMASSGATQ
     AELMTLTIVK GAQGFGFTIA DSPTGQRVKQ ILDIQGCPGL CEGDLIVEIN QQNVQNLSHA
     EVVDILKECP VGSETSLIIH RGGFFSPWKT PKPMMERWEN QGSPQTSVSA PAMPQNIPYP
     PTLHRSSFPD STEAFDPRKP DPYELYEKSR AIYESRRPDY KELDVHLRRM ESGFGFRILG
     GDEPGQPILI GAVIAMGSAD RDGRLHPGDE LVYVDGIPVA GKTHRYVIDL MHNAARNGQV
     NLTVRRKVLP TGEPCPENGR SPGSVSTHHS SPRSDYTTYA NSNHAASGSS ATPPEGFASH
     SLQTSDVVIH RKENEGFGFV IISSLNRPDS GSTITVPHKI GRIIDGSPAD RCAKLKVGDR
     ILAVNGQSII NMPHADIVKL IKDAGLSVTL RIIPQEELNS PASAPGSEKQ SPMAQQHSPM
     AQQSPLAQQS PVAQHSPVAQ PPPPQPLQPQ GHENSYRSEV KARQDVKPDI RQPPFTDYRQ
     SSTDYRQPPL DYRHPPVMDY QQPPPLDYRQ PPLMDYRQHS PDTRQFPLSE YRQPQDFDYF
     TVDLEKGAKG FGFSIRGGRE YKMDLYVLRL AEDGPAVRNG RMRVGDQIIE INGESTRDMT
     HARAIELIKS GGRRVRLLLK RGTGQVPEYG MVPSSLSMCM KSDKHGSPYF YLLGHPKDTT
     NQTPGVLPLP PPQVCRK
//
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