DLG1_XENTR
ID DLG1_XENTR Reviewed; 927 AA.
AC Q28C55; B1H2J2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Disks large homolog 1;
GN Name=dlg1; ORFNames=TEgg018e06.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential multidomain scaffolding protein required for normal
CC development. Recruits channels, receptors and signaling molecules to
CC discrete plasma membrane domains in polarized cells. May play a role in
CC adherens junction assembly, signal transduction and cell proliferation
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q12959};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q62696}. Cell junction
CC {ECO:0000250|UniProtKB:Q12959}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q12959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q28C55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q28C55-2; Sequence=VSP_036927, VSP_036928;
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; CR942446; CAJ82322.1; -; mRNA.
DR EMBL; BC161021; AAI61021.1; -; mRNA.
DR RefSeq; NP_001039116.1; NM_001045651.1. [Q28C55-1]
DR AlphaFoldDB; Q28C55; -.
DR SMR; Q28C55; -.
DR STRING; 8364.ENSXETP00000007496; -.
DR PaxDb; Q28C55; -.
DR ABCD; Q28C55; 1 sequenced antibody.
DR GeneID; 733937; -.
DR KEGG; xtr:733937; -.
DR CTD; 1739; -.
DR Xenbase; XB-GENE-1016132; dlg1.
DR eggNOG; KOG0708; Eukaryota.
DR HOGENOM; CLU_001715_4_3_1; -.
DR InParanoid; Q28C55; -.
DR OrthoDB; 807583at2759; -.
DR Reactome; R-XTR-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-XTR-8849932; Synaptic adhesion-like molecules.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003464; Expressed in 2-cell stage embryo and 13 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR019590; DLG1_PEST_dom.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR015143; L27_1.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR019583; PDZ_assoc.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF09058; L27_1; 1.
DR Pfam; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM01277; MAGUK_N_PEST; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..927
FT /note="Disks large homolog 1"
FT /id="PRO_0000370362"
FT DOMAIN 4..64
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 223..310
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 318..405
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 466..547
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 581..651
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 737..912
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 692..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 670..686
FT /note="QSFNDKRKKNLFSRKFP -> VVKKNMYYHMSQSINKK (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036927"
FT VAR_SEQ 687..927
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_036928"
SQ SEQUENCE 927 AA; 103401 MW; 76F247742FBECEBD CRC64;
MPVRKQDTQR ALTLLEEYRC KLHQTEDKQL RKSIERVIGI FQSNLFQALI DIQEFYEVTL
LDNPKSSDNA KPTEPVQTIN TWEYSSLPNS TATCETLPSS LILNVEKYRY PDDDITSQEP
SSPHMLNDGR NVELVQISEK NISQKENIQG LVSHSLISPL KTPEADTPCP PIVPVIPVIP
VPAESNVIPS STPQANPPPV IVNTDLETPA YVNGTDAEYE YEEITLERGT SGLGFSIAGG
TDNPHIGDDI SIFITKIISG GAAAQDGRLR VNDCILRVNE VDVHDVTHSK AVEALKEAGS
IVRLYVRRRK PVTEKIMDIK LVKGPKGLGF SIAGGVGNQH IPGDNSIYVT KIIEGGAAHK
DGRLQIGDKL LAVNTVCLEE VSHEDAVTAL KNTSDFVNLK VAKPTTMYMN DNYAPPDITN
SYSQQVDNHI SPSGFIGHPL PPSPGRYSPA PKGMLEDDDL TREPRKVVLQ RGTTGLGFNI
VGGEDGEGIF ISFILAGGPA DLSGELQKGD RIMSVNGVDL KSATHEQAAA ALKNAGQTVT
IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL
PSQGLNFKFG DILHVVNASD DEWWQARQVT ADGESEEIGV IPSKRRVEKK ERARLKTVKF
NSKARGDKGQ SFNDKRKKNL FSRKFPFYKN KDQSEMETSD VDQHVTSNAS DSESSYRGQE
EYVLSYEPVN QQEVNYSRPV IILGPTKDRV NDDLISEFPE KFGSCVPHTT RPKRDYEIDG
RDYHFVTSRE QMEKDIQDHR FIEAGQYNSH LYGTSVQSVK EVAERGKHCI LDVSGNAIKR
LQIAQLYPIA IFIKPKSVEN IIEMSKRVTE EQGRKTYERA MKLEQEFTEH FTAIVQGDTL
EEIYNQIKQI IEEQSSTFIW VPAKEKL
