ID A0A2Y9MSR4_DELLE Unreviewed; 639 AA.
AC A0A2Y9MSR4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=MAGUK p55 subfamily member 4 {ECO:0000313|RefSeq:XP_022423986.1};
GN Name=MPP4 {ECO:0000313|RefSeq:XP_022423986.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022423986.1};
RN [1] {ECO:0000313|RefSeq:XP_022423986.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022423986.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: 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_022423986.1; XM_022568278.1.
DR AlphaFoldDB; A0A2Y9MSR4; -.
DR STRING; 9749.A0A2Y9MSR4; -.
DR KEGG; dle:111172066; -.
DR InParanoid; A0A2Y9MSR4; -.
DR OrthoDB; 2873706at2759; -.
DR Proteomes; UP000248483; Unplaced.
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 CDD; cd12034; SH3_MPP4; 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; IPR035600; MPP4_SH3.
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:SF34; MAGUK P55 SUBFAMILY MEMBER 4; 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; PF00018; SH3_1; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 27..82
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 83..140
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 157..238
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 245..315
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 430..619
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..624
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 72632 MW; 8BD39FCD7278F15F CRC64;
MIQSDKGADP PDSKDKKDEK LSTVTNPENG ISQILRLVLQ ELNLFYSRDV NGVCLLYDLL
HSPWLQALLK VYDCLQEFKG KKLIPATPHA QALSYEVVKI LHETPKSPEI QELRQILQAP
HLKALLSAHD TVAQKDFEPL LPPLPDNIPE SEEAMRIVCM VKNQQPLGAT IKRHEMTGDI
LVARVIHGGL AERSGLLYAG DKLVEVNGVS VEGLDPEQVI HILAMSRGTI IFKVVPVSDP
PVNSQKMVYV RAMTEYWPQE DPAIPCMDAG LPFQKGDILQ IVDQNDALWW QARKISDLGT
CAGLIPSTHL LKRKQREFWW SQPYQPHNNL KSTISISMEE EDDMKIDEKC VEADEETFES
EELSEDKEEF VGYGQKFYIA GFRRSMRLCR RWSHLRQLRA KVCGANTCSG AAGAPYEEVV
RYQRRPADKH RLIVLVGPSG VGVNELRRQL IELDPNRFQS AVPHTTRSKK SYEMDGREYH
YVSKETFESL MYSHRMLEYG EYKGHLYGTS VDAVQAVLDE GKICVMDLEP QGIQVARTHE
LKPYVIFIKP SSMSCMKQSR KNAKIITNYF VDMKFKDEDL QEMEDLAQKM ETQFGQFLDH
VIVNDSLQDA CAQLLSAVQK AQEEPQWVPA TWVSSDTES
//
