ID A0A3P8QWQ8_ASTCA Unreviewed; 926 AA.
AC A0A3P8QWQ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Disks large homolog 1 {ECO:0000256|ARBA:ARBA00044189};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000033496.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000033496.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000033496.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR AlphaFoldDB; A0A3P8QWQ8; -.
DR STRING; 8154.ENSACLP00000033496; -.
DR Ensembl; ENSACLT00000034293.1; ENSACLP00000033496.1; ENSACLG00000022610.1.
DR GeneTree; ENSGT00940000159409; -.
DR OMA; WIASSDF; -.
DR Proteomes; UP000265100; Chromosome 18.
DR Bgee; ENSACLG00000022610; Expressed in brain and 7 other cell types or tissues.
DR GO; GO:0031594; C:neuromuscular junction; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 3.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR019583; DLG1-4_PDZ_assoc.
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; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23119; DISCS LARGE; 1.
DR PANTHER; PTHR23119:SF5; DISKS LARGE HOMOLOG 1; 1.
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; L27 domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
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; 3.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 4..64
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 222..309
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 317..404
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 467..548
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 582..652
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 736..911
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 107..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 103103 MW; F141296BB1A41F27 CRC64;
MPVRKKDAQR ALQLLEQYRA KLNHTEDRQL RHSIQRVIDI FQSNLFQALI DIQEFYEVTL
LDSQRWVESS KGADPMAPVN LWDFSSLQST TVTSDTLPSL STSIEKYRHH DEDSSPQDQS
SPQLTEEAGG PELVQVAEKN LSLIENVHGY VTHAHISPMK QAEAAPPSSP IIPVIPILPI
PAETTAIPPT SQANPPPVVV NADSLDTPPY VNGTEADYEY EEITLERGNS GLGFSIAGGT
DNPHIGEDPS IFITKVIPGG AAAQDGRLRV NDVILRVNEV DVRDVTHSRA VEALKEAGSL
VRLYVRRRKP VSEKVMEIKL VKGPKGLGFS IAGGVGNQHI PGDNSIYVTK IIEGGAAHKD
GRLQIGDKLL AVNSSCLEEV SHEHAVTALK NTPDVVYLKV AKPNSVFMND SFAPPDLTNS
YSQRMENHIS PPNFLGQPVP PPASSGRYSP TPKSTLGDDD VTREPRKVVL HRGATGLGFN
IVGGEDGEGI FISFILAGGP ADLSGELRKG DRLVSVNGVD LRNATHEQAA AALKNAGQTV
TIVAHYRPEE YSRFEAKIHD LREQMMNSSI SSGSGSLRTS QKRSLYVRAL FDYDKTRDSG
LPSQGLNFKF GDILHVVNAS DDEWWQARQL TAQGEVEEVG VIPSKRRVEK KERARLKTVK
FNAKSRDRGS LNDKRKKNLF SRKFPFYKSK EASEQETSDV DQHVTSNASD SESSYRGQEE
YVLSYEPVVQ QEVNYTRPVI ILGPMKDRIN DDLISEFPDK FGSCVPHTTR PKRDYEVDGR
DYHFVISREQ MEKDIQDHKF IEAGQYNNHL YGTSVQSVRE VAEKGKHCIL DVSGNAIKRL
QLAQLHPIAI FIKPKSVENI MEMNKRLTEE QGKKTFDRAN KLEQEFTEHF TAIVQGDTLE
EIYDQVKQII EEQSGPFIWV QSKEKL
//
