ID A0A2Y9IMI8_ENHLU Unreviewed; 576 AA.
AC A0A2Y9IMI8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=MAGUK p55 subfamily member 7 {ECO:0000256|ARBA:ARBA00017019};
GN Name=LOC111139311 {ECO:0000313|RefSeq:XP_022347275.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022347275.1};
RN [1] {ECO:0000313|RefSeq:XP_022347275.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022347275.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004202}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR RefSeq; XP_022347275.1; XM_022491567.1.
DR AlphaFoldDB; A0A2Y9IMI8; -.
DR STRING; 391180.A0A2Y9IMI8; -.
DR KEGG; elk:111139311; -.
DR OrthoDB; 2873706at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.10.287.650; L27 domain; 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; IPR036892; L27_dom_sf.
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; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; L27 domain; 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; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022427};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 10..65
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 67..122
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 139..220
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 228..298
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 368..560
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
SQ SEQUENCE 576 AA; 65560 MW; 61B6568FE6D05F17 CRC64;
MPALSTGAGS DAGLYELLAA LPAQLQPHVD SQEDLTFLWD MFGEKSLHSL VKIHEKLHYY
EKQNPVPILH GAAVLADDLA EELQNKPLNS EIRELLKLLS KPNVKALLSV HDTVAQKNYD
PVLPPMPDDI DDEEDSVKII RLVKNREPLG ATIKKDEQTG AIVVARIMRG GAADRSGLIH
VGDELREVNG IPVEDKRPEE IIQILAQSQG AITFKIIPSI KEETPSKEGK MFIKALFDYD
PSEDKAIPCK EAGLSFKKGD ILQIMSQDDV TWWQAKHADD ANPRAGLIPS KHFQERRLAL
RRPEILVQPL KVSNRKSSGF RRSFRLSRKD KKTNKSMYEC KKSDQYDTAD VPTYEEVTPY
RRQTNEKYRL VVLVGPVGVG LNELKRKLLI SDTQHYGVTV PHTTRARRSQ ESDGVEYIFI
SKHLFETDVQ NNKFIEYGEY KNNYYGTSID SVRSVLAKNK VCLLDVQPHT VKHLRTLEFK
PYVIFIKPPS IERLRETRKN AKIISSRDDQ GAAKPFTEED FQEMIKSAQI MENQYGHLFD
KIIVNDDLTV AFNELKTTFD KLETEAHWVP VSWLHS
//
