ID A0A3B3SAG1_9TELE Unreviewed; 531 AA.
AC A0A3B3SAG1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=MAGUK p55 subfamily member 7 {ECO:0000256|ARBA:ARBA00017019};
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:ENSPKIP00000027724.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000027724.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR AlphaFoldDB; A0A3B3SAG1; -.
DR Ensembl; ENSPKIT00000008495.1; ENSPKIP00000027724.1; ENSPKIG00000009545.1.
DR GeneTree; ENSGT00940000156232; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23122:SF39; MAGUK P55 SUBFAMILY MEMBER 7; 1.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 18..77
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 94..175
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 183..253
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 323..515
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 264..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 59959 MW; EE40D8FB6F2103BA CRC64;
MLFRFPCLAG EPPNCVSTPP GLFELLATLP SQLKPHVDSQ ADCAFLQDMF GEKSLQALVK
SLLSVHDTVA QKSYDPQLPP MPDDIDEDED SVKIIRLVKN KEPLGATIKR DECTGAIVVA
RIMRGGAADR SGLIHVGDEL KEVNGIPVDD KKPEEIIHIL AQSQGAITFK IIPGIKEDAQ
DRQPKMFVKS LFDFDPSEDK AIPCKEAGLA FKKGDVLQIM SQDDATWWQA RHEGDANPRA
GLIPSKQFQE RRFALRRPGV LAQPQKVSNR RSSSLRRSFR LSRKDRKTNK SMYECKKSDQ
YDTADVPTYE EVTTYCRPPS GQHRLVVLVG PTGVGLNELK RKLLISDPQH FGVTVPHTTR
VKRSQESEGV EYHFISKHLF ETDVQNNKFV EHGEYRGNYY GTSLDSVRSV LSKNKVCLLD
VQPHTIKHLR TAEFKPYVVF VKPPTIERLR ETRRDAKVIS GKDDKCLAKP FSEEDFLEMI
NTSRVMEAQY GYLFDKVIVN DDLTSAFSDL NGALKKLETE THWVPVSWTH S
//
