ID H9F7C8_MACMU Unreviewed; 1046 AA.
AC H9F7C8;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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};
DE Flags: Fragment;
GN Name=MAGI3 {ECO:0000313|EMBL:AFE70537.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE70537.1};
RN [1] {ECO:0000313|EMBL:AFE70537.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE70537.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR EMBL; JU326781; AFE70537.1; -; mRNA.
DR AlphaFoldDB; H9F7C8; -.
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; 5.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.30.42.10; -; 5.
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:SF10; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 5.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 5.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 5.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 2: Evidence at transcript level;
KW Kinase {ECO:0000313|EMBL:AFE70537.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:AFE70537.1}.
FT DOMAIN 35..111
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 214..247
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 260..293
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 331..399
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 499..562
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 647..729
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 772..859
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 942..1024
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 103..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFE70537.1"
SQ SEQUENCE 1046 AA; 115059 MW; B26D89CC303497DB CRC64;
SGLTNRDTLA VIRHFREPIR LKTVKPGKVI NKDLRHYLSL QFQKGSIDHK LQQVIRDNLY
LRTIPCTTRA PRDGEVPGVD YNFISVEQFK ALEESGALLE SGTYDGNFYG TPKPPAEPSP
FQPDPVDQVL FDNEFDAESQ RKRTTSVSKM ERMDSSLPEE EEDEDKEAIN GSGNAENRER
HSESSDWMKT VPSYNQTNSS MDFRNYMMRD ETLEPLPKNW EMAYTDTGMI YFIDHNTKTT
TWLDPRLCKK AKAPEDCEDG ELPYGWEKIE DPQYGTYYVD HLNQKTQFEN PVEEAKRKKQ
LGQAEIGSSK PDMEKSHFTR DPSQLKGVLV RASLKKSTMG FGFTIIGGDR PDEFLQVKNV
LKDGPAAQDG KIAPGDVIVD INGNCVLGHT HADVVQMFQL VPVNQYVNLT LCRGYPLPDD
SEDPVVDIVA ATPVINGQSL TKGETCMNPQ DFKPGTMVLE QNGKSGHTLT GDGLNGPSDT
SEQRVSMASS GSSQPELVTI PLIKGPKGFG FAIADSPTGQ KVKMILDSQW CQGLQKGDII
KEIYHQNVQN LTHLQVVEVL KQFPVGADVP LLILRGGPPS PTKTTKMKTD KKENSGSLEA
INEPIPQPMP FPPSIIRSGS PKLDPSEVYL KSKTLYEDKP PNTKDLDVFL RKQESGFGFR
VLGGDGPDQS IYIGAIIPLG AAEKDGRLRA ADELMCIDGI PVKGKSHKQV LDLMTTAARN
GHVLLTVRRK IFYGEKQPED DSSQAFISTQ NGSPRLNRAE VPARPAPQEP YDVVLQRKEN
EGFGFVILTS KNKPPPGVIP HKIGRVIEGS PADRCGKLKV GDHISAVNGQ SIVELSHDNI
VQLIKDAGVT VTLTVIAEEE HHGPPSGTNS ARQSPALQHR PVGQSQANHI PGDRSGLEGE
IGKDVCTSYR HSWSDHKHLA QPDPAVIPVV GSRHNQSLGC YPVELERGPR GFGFSLRGGK
EYNMGLFILR LAEDGPAIKD GRIHVGDQIV EINGEPTQGI THTRAIELIQ AGGNKVLLLL
RPGTGLIPDH GLAPSGLCSY VKPEQH
//
