ID A0A3B3QM52_9TELE Unreviewed; 1176 AA.
AC A0A3B3QM52;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Membrane associated guanylate kinase, WW and PDZ domain containing 1 {ECO:0000313|Ensembl:ENSPKIP00000006650.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000006650.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000006650.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR AlphaFoldDB; A0A3B3QM52; -.
DR Ensembl; ENSPKIT00000030679.1; ENSPKIP00000006650.1; ENSPKIG00000022734.1.
DR GeneTree; ENSGT00940000155820; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF77; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1 ISOFORM X1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF16666; MAGI_u5; 1.
DR Pfam; PF00595; PDZ; 5.
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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 17..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 93..184
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 300..333
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 347..380
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 431..500
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 604..682
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 784..866
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 944..1040
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1072..1154
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 181..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..745
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 128178 MW; 0F8A01B360B9C7DE CRC64;
MSRVVQKKNH WSSKLTESSL CRDERGGFHV ELRGGAENGQ FSYVDDINED LVTYQYGGLT
EGELILEVEG LSVSGLPLYD VLEVVKNCKG PVRFRTVRQG SKLNKDLKHY LSQRFQKSSP
DYELQQTIRD NLYRHAVPCT TRPPRNGEVP GVDYNFLSVQ DFLKLEKSGT LLEIGTYEGN
YYGTPKPPSQ PPSGRVITSD ALQDSLPSSP LSTSRRSKSY NDMQNAGIVS PENEEDADEL
PDMSSSFTGD SSEPDEQPSV RLPPSRERAP SYGVTAPLLA TDGSRQTHGQ LRLPEEDLLG
PLPDNWEMAY TENGEVYFID HNTKTTSWID PRCLEKPQKP LEECEDDELP AGWEKIEDPV
YGVYYVDHIN RKTQYENPIL EAKRKKQLGQ QPVEEWIEER SSAGPPLASF PNSGKPFFTR
NPAELKGTFI HTKLKKSRRG FGFTVVGGDE PDEFLQIKSL VLDGPAALDG KMETGDVIVS
VNETCVLGYT HSQVVKIFQS IPIGSMVDLE LCRGYPLPFD PDDPNTSLVT SVAILDKEPI
IVNGQESYDS PTSRGSQPGG GMNGAKEPRP YSPSAEVAPD GTPAYPSDVV TLASSIATQP
ELITVHMEKG EKGFGFTIAD SPTGGGQRVK QIVDYPRCRG LKEGDILVEV NKRNVQSMTH
NQVVDLLSKC PKGSEVTMLV QRGRHPPQHQ QLERRDSQGS SQHSLSSHRS AHTDSPVHAI
PAPASESAPP PLPPGPLPQD PVDPMAQKKP DPFKIWAQSR SMYESRCEYA GPAERFLPDL
QEQDIFLWRK DTGFGFRILG GNEPGEPIYI GHIVKYGAAD EDGRLRSGDE LICVDGTAVV
GKSHQLVVQL MQQAAKQGHV NLTVRRKTGF GVSKLDGEVP PSPASSHHSS TQAPSLTEEK
RTPQGSQNSL NTVSSGSGST SGIGSGGGGG SGGGVVPIAV QPYDVEIRRG ENEGFGFVIV
SSVSRPDAGT TFAGNTCVAM PHKIGRIIEG SPADRCGKLK VGDRILAVNG CSITNKSHSD
IVNLIKEAGK TVTLRIIPGD ESSNASLLTN AEKIATITTT HTAQQQEAEY YSVDLERDTK
GFGFSLRGGR EYNMDLYVLR LAEDGAAVRN GKMRVGDEIL EINGESTKNM KHGRAIELIK
NGGRRVCLVL KRGDGSVPEY GGSIYESVAF SHAFSP
//
