ID K7DF99_PANTR Unreviewed; 1481 AA.
AC K7DF99;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
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};
GN Name=MAGI3 {ECO:0000313|EMBL:JAA39634.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA39634.1};
RN [1] {ECO:0000313|EMBL:JAA39634.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA39634.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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; GABE01005105; JAA39634.1; -; mRNA.
DR RefSeq; XP_513660.5; XM_513660.5.
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: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; 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 2: Evidence at transcript level;
KW Kinase {ECO:0000313|EMBL:JAA39634.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:JAA39634.1}.
FT DOMAIN 27..106
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 114..190
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 293..326
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 339..372
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 410..478
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 578..641
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 726..808
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 851..938
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1021..1103
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 182..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1481 AA; 162907 MW; 1B9B103B4AD9AA5E CRC64;
MSKTLKKKKH WLSKVQECAV SWAGPPGDFG AEIRGGAERG EFPYLGRLRE EPGGGTCCVV
SGKAPSPGDV LLEVNGTPVS GLTNRDTLAV IRHFREPIRL KTVKPGKVIN KDLRHYLSLQ
FQKGSIDHKL QQVIRDNLYL RTIPCTTRAP RDGEVPGVDY NFISVEQFKA LEESGALLES
GTYDGNFYGT PKPPAEPSPF QPDPVDQVLF DNEFDAESQR KRTTSVSKME RMDSSLPEEE
EDEDKEAING SGNAENRERH SESSDWMKTV PSYNQTNSSM DFRNYMMRDE TLEPLPKNWE
MAYTDTGMIY FIDHNTKTTT WLDPRLCKKA KAPEDCEDGE LPYGWEKIED PQYGTYYVDH
LNQKTQFENP VEEAKRKKQL GQAEIGSSKP DLEKSHFTRD PSQLKGVLVR ASLKKSTMGF
GFTIIGGDRP DEFLQVKNVL KDGPAAQDGK IAPGDVIVDI NGNCVLGHTH ADVVQMFQLV
PVNQYVNLTL CRGYPLPDDS EDPVVDIVAA TPVINGQSLT KGETCMNPQD FKPGAMVLEQ
NGKSGHTLTG DGLNGPSDTS EQRISMASSG SSQPELVTIP LIKGPKGFGF AIADSPTGQK
VKMILDSQWC QGLQKGDIIK EIYHQNVQNL THLQVVEVLK QFPVGADVPL LILRGGPPSP
TKTAKMKTDK KENAGSLEAI NEPIPQPMPF PPSIIRSGSP KLDPSEVYLK SKTLYEDKPP
NTKDLDVFLR KQESGFGFRV LGGDGPDQSI YIGAIIPLGA AEKDGRLRAA DELMCIDGIP
VKGKSHKQVL DLMTTAARNG HVLLTVRRKI FYGEKQPEDD SSQAFISTQN GSPRLNRAEV
PARPAPQEPY DVVLQRKENE GFGFVILTSK NKPPPGVIPH KIGRVIEGSP ADRCGKLKVG
DHISAVNGQS IVELSHDNIV QLIKDAGVTV TLTVIAEEEH HGPPSGTNSA RQSPALQHRP
MGQSQANHIP GDRSALEGEI GKDVSTSYRH SWSDHKHLAQ PDTAVISVVG SRHNQSLGCY
PVELERGPRG FGFSLRGGKE YNMGLFILRL AEDGPAIKDG RIHVGDQIVE INGEPTQGIT
HTRAIELIQA GGNKVLLLLR PGTGLIPDHG DWDINNPSSS NVIYDEQSPL PPSSHFASIF
EESHVPVIEE SLRVQICEKA EELKDIVPEE KSTLNENQPE IKHQSLLQKN VSKRDPPSSH
GHSNKKNLLK VENGVTRRGR SVSPKKPASQ HSEEHLDKIP SPLKNNPKRR PRDRSLSPSK
GENKSCQVST RAGSGQDQCR KSRGRSASPK KQQKIEGSKA PSNAEAKLLE GKSRRIAGYT
GSNAEQIPDG KEKSDVIRKD AKQNQLEKSR TRSPEKKSKR MVEKSLPSKM TNKTTSKEVS
ENEKGKKVTT GETSSSNDKI GENVQLSEKR LKQEPEEKVV SNKTEDHKGK ELEAADKNKE
TGRFKPESSS PVKKTPITPG PWKVPSGNKV TGTIGMAEKR Q
//
