ID M3XMF2_MUSPF Unreviewed; 639 AA.
AC M3XMF2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Membrane palmitoylated protein 4 {ECO:0000313|Ensembl:ENSMPUP00000000252.1};
GN Name=MPP4 {ECO:0000313|Ensembl:ENSMPUP00000000252.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000252.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000000252.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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 EMBL; AEYP01060356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XMF2; -.
DR STRING; 9669.ENSMPUP00000000252; -.
DR Ensembl; ENSMPUT00000000256.1; ENSMPUP00000000252.1; ENSMPUG00000000255.1.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000156444; -.
DR HOGENOM; CLU_001715_5_0_1; -.
DR InParanoid; M3XMF2; -.
DR OMA; PACWIRP; -.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 24..80
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 87..137
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 154..235
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 242..312
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"
SQ SEQUENCE 639 AA; 72066 MW; BB1E94498F2E64C2 CRC64;
RTQSDRGAHP LDKKNMKPST ATNPENGVSQ ILRLVLRELN LFYSRDVNGV CLLYDLLHSP
WLQALLKVYN CLLEFKEKKL VPATTHAQTL SCEVVGLLRE TPKSPEIQEL KQILQDPHFK
ALLSAHDSVA QKDFEPLLPP LPDNIPESEE AMRIVCIVKN QQPLGATIKR HEMTGDILVA
RVIHGGLAER SGLLYAGDKL VEVNGVPVEG LDPEQVIHIL AMSRGTIMFK VVPVSAPPVN
SQKTVYVRAM TEYWPQEDPA IPCMDAGLPF QKGDILQIVD QNDALWWQAR KISDLGTCAG
LIPSNHLLKR KQREFWWSQP YQPPSGLKPT ISISMEDDDM KIDEKCVEAG ETIDEETFES
EELSEDKEEF VGSGQKFFIA GFRRSMRLCR RKSHLGQLRA GLGGGGGGLP APGAPYEEVV
RYQRRPSEQH RLVVLVGPSG VGVNELRRQL IELNPEQFQS AVPHTTRSKK SYEVDGREYH
YVSKEVFESL VYSHRMLEHG EYKGHLYGTS VDAVQTVLDE GKICVMDLEP QGIQLARTQE
LKPYVIFIKP SSMSRMKQSR KNAKIITDYF VDMKFKDEDL QEMEDLAQKM EAQFGQFFDH
VIVNDNLQDA CAQLVSAIQK AQEEPQWVPA TWISSDTES
//
