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Database: UniProt
Entry: A0A096LWV1_POEFO
LinkDB: A0A096LWV1_POEFO
Original site: A0A096LWV1_POEFO 
ID   A0A096LWV1_POEFO        Unreviewed;      1227 AA.
AC   A0A096LWV1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 {ECO:0000256|ARBA:ARBA00016171};
DE   AltName: Full=Membrane-associated guanylate kinase inverted 3 {ECO:0000256|ARBA:ARBA00033438};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000023642.1, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000023642.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC       {ECO:0000256|ARBA:ARBA00007014}.
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DR   EMBL; AYCK01005417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01005418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A096LWV1; -.
DR   STRING; 48698.ENSPFOP00000023642; -.
DR   Ensembl; ENSPFOT00000028360.1; ENSPFOP00000023642.1; ENSPFOG00000013628.2.
DR   eggNOG; KOG3209; Eukaryota.
DR   GeneTree; ENSGT00940000156496; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   CDD; cd00992; PDZ_signaling; 5.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.30.42.10; -; 5.
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:SF10; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00228; PDZ; 5.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 5.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50106; PDZ; 5.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT   DOMAIN          60..93
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          106..139
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          185..254
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          359..422
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          544..627
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          679..766
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          827..909
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          765..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          928..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..797
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1074
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1178..1202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1210..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1227 AA;  133602 MW;  4D5CD6E75B37EEC9 CRC64;
     MDRMDSTAPE EEEEEERPPM VNGVGEHKDK ADWRKTVPSY NQSAGAMDMR VWNTLDESQE
     PLPKNWEMAY TETGMVYFID HNTKTTTWLD PRLAKKAKPP EKCIEGELPY GWEKIEDPQF
     GTYYVDHINQ KTQFENPVME AKRKLSDDTP TAVQPPAAAP SEEEPARGLR GFTRDPSQLQ
     GSILQTSLKK SPLGFGFTII GGDRPDEFLQ VKNVLPDGPA AHDNKIAPGD VIVDINGACV
     LGKTHADVVQ MFQSIPINQY VDLVLCRGYP LPEDSNSSED ASASLNASKE ASPTPSSSNP
     QEPHFTVPDG GHLSRQAAAV PALSNGGRHH HHPQQHQHLP LTHNQEAPDP TLLQPELVSV
     PLVKGPGGFG FAIADCPLGQ KVKMILDAQW CRGLLKGDVI KEINRQNVQT LSHAQVVDIL
     KDLPVGSEVN VLVLRGGQTS PVKSLKPERA SMPHATSQHS LQHPPHAVSH QLPHPASQPV
     VQLQQRQEMA NSTETLSQPE VLSNALPVST NTLRSSSPKP DPSELYLKSK AMLDSKPPNT
     KDLDVFIKRN QESGFGFRVL GGEGPDQPVY IGAIVPLGAA EKDGRLRAGD ELLCIDGVPV
     KGKSHKQVLE LMTNAARNGQ VMLTVRRKLT HTEGGEEEES GQQPQQVASA LVNSSPKVPR
     VEAPNAVQPA QLPRPESFDV TLQRKDNEGF GFVILTSKNK PPPGVIPHKI GRIIEGSPTD
     RIGRMKVGDR ISAVNGQSIM ELSHNDIVQL IKDAGNTVTL TVVPEEDSAP PSGTNSVKHS
     PSIQHRAMGQ QPSSHLDRAA ESEMRNSLQP NEMGAIATSG PKQGCFVVEL ERSQRGFGFS
     LRGGKEYNMG LYILRLAEEG PALKDGRIHV GDQIVEINGE ATQGITHTRA IELIQAGGNK
     VHLLLRPGQG LVPDHSTKDK VAIPTTSFPR LSASDDQSSP ASPSTGWSPS SSKVFAPDEP
     SAGDYRVPGF PGAGQEHGRQ ANRSRGQQIP THNHRRSTSP RKTGQSDYKS GSPRKMAEGQ
     MDNVEHSQNP QKTMEDVSKE RKTSGQKDQR SSSPRKGSKR ELDPVLHSKN PEDPQSPRRP
     AGQQPAGEVR DWRHKGEDAT HPQERGAAES GDKSWGADDH HKKGKRAQKE AAAQKSHRER
     AGSDADPATT GQRGRRERAE KEYPEAKYQG PAEQANRRDP RGSSSSIQDP NCNGTSTSKK
     APITPGPWKV PSSTKIQSHV DSTYADI
//
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